目录号 | 产品详情 | 靶点 | |
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T37819 | |||
Brain-derived acidic fibroblast growth factor (102-111) is a peptide fragment of brain-derived acidic fibroblast growth factor (aFGF). aFGF is an angiogenic vascular endothelial cell mitogen produced in bovine brain that has sequence homology to interleukin-1. It also shares sequence homology with the known neuropeptides neuromedin C , bombesin , neuromedin K , substance K , substance P , physalaemin, and eledoisin. aFGF (102-111) corresponds to amino acid residues 102-111 of the fulllength peptide. | |||
T37595 | |||
Brain-derived acidic fibroblast growth factor (brain-derived aFGF) (1-11) is a peptide fragment of brain-derived aFGF. Brain-derived aFGF is an angiogenic vascular endothelial cell mitogen produced in bovine brain that has sequence homology to interleukin-1. aFGF (1-11) corresponds to amino acid residues 1-11 of the full length peptide. | |||
T37820 | |||
Brain-derived basic fibroblast growth factor (1-24) (brain-derived bFGF) is a peptide fragment of brain-derived bFGF. bFGF is a peptide produced in bovine brain that is protective in a rat model of pressure-induced retinal ischemia. bFGF (1-24) corresponds to amino acid residues 1-24 of the full length peptide. | |||
T0084 | MAO Monoamine Oxidase | ||
Moclobemide (Ro111163) 是可逆的、可透过血脑屏障的单胺氧化酶 (MAO-A) 抑制剂,能够抑制 hMAO-A (IC50=6.061 μM)。它上调慢性应激小鼠海马祖细胞的增殖。 | |||
T6920 | FGFR c-RET JAK CDK PDGFR Src AMPK | ||
ON123300 是一种可透过血脑屏障的多激酶抑制剂,作用于 CDK4、CDK6、Ark5、PDGFRβ、FGFR1、RET 和 Fyn,IC50值为3.9、9.82、5、26、26、9.2和11 nM。它在脑肿瘤中抑制 Akt 磷酸化及激活 Erk。 | |||
T1667 | Apoptosis FLT CSF-1R PDGFR Src c-Kit | ||
Tandutinib (CT53518) 是一种选择性 FLT3抑制剂,其 IC50为 0.22 μM。它还抑制c-Kit 和PDGFR,其IC50分别为 0.17 μM 和 0.20 μM。它可穿透血脑屏障,用于急性骨髓性白血病。 | |||
T76321 | |||
Brain Derived BasicFibroblast Growth Factor(1-24) (FGF basic 1-24) 是一种合成肽,表现出抗细菌和抗HBV 的活性。Brain Derived BasicFibroblast Growth Factor(1-24) 可用于感染性疾病和免疫性疾病的研究。 | |||
T4779 | Others Endogenous Metabolite | ||
4-Methylcatechol (3,4-Dihydroxytoluene) 是 p-toluate 的代谢物,它是 Catechol 2,3-Dioxygenase 的自杀性底物抑制剂。 | |||
T7568 | Trk receptor | ||
LM22A-4 是特异性的tyrosine kinase receptor B 激动剂,常用于研究神经系统疾病。 | |||
T0183 | Others | ||
Pramiracetam (CI-879) 来源于piracetam,能改善脑外伤引起的认知障碍。它是更有效的促智药物。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-05510 | BDNF Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
BDNF is a member of thenerve growth factorfamily. It is highly expressed in hippocampus, amygdala, cerebral cortex and cerebellum. It also can be detected in heart, lung, skeletal muscle, testis, prostate and placenta. BDNF is induced by cortical neurons, and is necessary for survival of striatal neurons in the brain. During development, BDNF promotes the survival and differentiation of selected neuronal populations of the peripheral and central nervous systems. It participates in axonal growth, pathfinding and in the modulation of dendritic growth and morphology. It functions as the major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (LTP), long-term depression (LTD), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.
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TMPJ-00135 | BDNF Protein, Human/Murine/Rat, Recombinant | Human,Mouse,Rat | E. coli | ||
Brain-Derived Neurotrophic Factor (BDNF) is a member of the neurotrophin family. Along with other structurally related neurotrophic factors NGF, NT-3 and NT-4, BDNF binds with high affinity to the TrkB kinase receptor. It also binds with the LNGFR (for low-affinity nerve growth factor receptor, also known as p75). BDNF promotes the survival, growth and differentiation of neurons. It serves as a major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS. BDNF expression is altered in neurodegenerative disorders such as Parkinson's and Alzheimer's disease.
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TMPJ-00134 | pro-BDNF Protein, Human, Recombinant | Human | E. coli | ||
The precursor form of Brain-Derived Neurotrophic Factor (pro-BDNF) interacts preferentially with the pan-neurotrophin receptor p75 (p75NTR) and vps10p domain-containing receptor sortilin and induces neuronal apoptosis, whereas mature BDNF selectively binds with high affinity to the TrkB kinase receptor and promotes the survival, growth and differentiation of neurons. As proneurotrophins and mature neurotrophins elicit opposite biological effects, Pro-BDNF cleavage in the neuronal system is regulated in a specific and cell-context dependent manner. Pro-BDNF plays important role in negative regulation of neurotrophic actions in the brain.
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TMPH-03251 | BDNF Protein, Rat, Recombinant (His) | Rat | E. coli | ||
Important signaling molecule that activates signaling cascades downstream of NTRK2. During development, promotes the survival and differentiation of selected neuronal populations of the peripheral and central nervous systems. Participates in axonal growth, pathfinding and in the modulation of dendritic growth and morphology. Major regulator of synaptic transmission and plasticity at adult synapses in many regions of the CNS. The versatility of BDNF is emphasized by its contribution to a range of adaptive neuronal responses including long-term potentiation (LTP), long-term depression (LTD), certain forms of short-term synaptic plasticity, as well as homeostatic regulation of intrinsic neuronal excitability.; Important signaling molecule that activates signaling cascades downstream of NTRK2. Activates signaling cascades via the heterodimeric receptor formed by NGFR and SORCS2. Signaling via NGFR and SORCS2 plays a role in synaptic plasticity and long-term depression (LTD). Binding to NGFR and SORCS2 promotes neuronal apoptosis. Promotes neuronal growth cone collapse.
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TMPJ-00671 | FABP7 Protein, Human, Recombinant (His) | Human | E. coli | ||
Fatty Acid-Binding Protein 7 (FABP7) is a cytoplasm protein that belongs to the Fatty-acid Binding Protein (FABP) family of calycin superfamily. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids. FABP7 is predominately expressed in brain and neural tissues. FABP7 is involved in fatty acid uptake and intracellular transport and is important in brain development. FABP7 plays a critical role in the transport of a so far unknown hydrophobic ligand with potential morphogenic activity during CNS development. FABP7 is required for the establishment of the radial glial fiber system in developing brain, a system that is necessary for the migration of immature neurons to establish cortical layers.
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TMPY-04069 | Neurotrophin 3 Protein, Human, Recombinant | Human | E. coli | ||
NTF3 (Neurotrophin 3) is a Protein Coding gene. The protein encoded by this gene is a member of the neurotrophin family, that controls the survival and differentiation of mammalian neurons. This protein is closely related to both nerve growth factor and brain-derived neurotrophic factor. NTF3 is a key mediator of neuronal development during the early neurogenic period. NTF3 is a novel target gene of POU3F2 and that the POU3F2/NTF3 pathway plays a role in the process of neuronal differentiation. NTF3 is capable of activating TrkB to induce anoikis resistance, and show that NTF3 is also a direct target of miR-200c. NTF3 is broadly expressed in the ovary, spleen, and other tissues. Diseases associated with NTF3 include Hypochondriasis and Demyelinating Disease.
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TMPJ-01469 | NGF Protein, Human, Recombinant (E. colli) | Mouse | E.coli | ||
NGF is the first member discovered in the Neurotrophin family, which includes brain-derived neurotrophic factor (BDNF), neurotrophin-3 (NT-3), and neurotrophin-4 (NT-4). These proteins belong to the cysteine-knot family of growth factors that assume stable dimeric structures. Mouse beta -NGF is a homodimer of two 120 amino acid polypeptides. It shares approximately 90% homology at the amino acid level with human beta -NGF and 95.8% with rat beta -NGF. NGF signaling has been shown to play an important role in neuroprotection and repair. β-NGF acts as a growth and differentiation factor for B lymphocytes, and enhances B-cell survival. It is a potent neurotrophic factor that signals through its receptor β-NGFR, and plays a crucial role in the development and preservation of the sensory and sympathetic nervous systems.
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TMPY-01442 | DMBT1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Deleted in malignant brain tumors 1 protein, also known as glycoprotein 34, surfactant pulmonary-associated D-binding protein, DMBT1 and GP34, is a secreted protein which belongs to theDMBT1 family. DMBT1 contains 2CUB domains, 14SRCR domains and 1ZP domain. It is highly expressed in alveolar and macrophage tissues. In some macrophages, expression is detected on the membrane, and in other macrophages, it is strongly expressed in the phagosome/phagolysosome compartments. Defects in DMBT1 are involved in the development of glioma (GLM). Gliomas are central nervous system neoplasms derived from glial cells and comprise astrocytomas, glioblastoma multiforme, oligodendrogliomas , and ependymomas. DMBT1 may be considered as a candidate tumor suppressor for brain, lung, esophageal, gastric, and colorectal cancers. It may play roles in mucosal defense system, cellular immune defense and epithelial differentiation. DMBT1 may play a role as an opsonin receptor for SFTPD and SPAR in macrophage tissues throughout the body, including epithelial cells lining the gastrointestinal tract. It may be an important factor in fate decision and differentiation of transit-amplifying ductular (oval) cells within the hepatic lineage. DMBT1 may function as a binding protein in saliva for the regulation of taste sensation. It binds to HIV-1 envelope protein and has been shown to both inhibit and facilitate viral transmission.
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TMPY-02231 | TrkB Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
TrkB receptor also known as TrkB tyrosine kinase or BDNF/NT-3 growth factors receptor or neurotrophic tyrosine kinase, receptor, type 2 (NTRK2) is a single transmembrane catalytic receptor with intracellular tyrosine kinase activity. TrkB/NTRK2 is a member of the neurotrophic tyrosine receptor kinase (NTRK) family. TrkB tyrosine kinase (TrkB) or NTRK2 is coupled to the Ras, Cdc42/Rac/RhoG, MAPK, PI3-K, and PLCgamma signaling pathways. There are four members of the Trk family; TrkA, TrkB, and TrkC and a related p75NTR receptor. Each family member binds different neurotrophins with varying affinities. TrkB/NTRK has the highest affinity for brain-derived neurotrophic factor (BDNF) and is involved in neuronal plasticity, long-term potentiation, and apoptosis of CNS neurons. Other neurotrophins includenerve growth factor(NGF), neurotrophin-3 and neurotrophin-4. TrkB/NTRK is a membrane-bound receptor that, upon neurotrophin binding, phosphorylates itself and members of the MAPK pathway. Signaling through this kinase leads to cell differentiation. Mutations in TrkB/NTRK have been associated with obesity and mood disorders.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-00751 | TrkB Protein, Human, Recombinant (His) | Human | HEK293 | ||
TrkB receptor also known as TrkB tyrosine kinase or BDNF/NT-3 growth factors receptor or neurotrophic tyrosine kinase, receptor, type 2 (NTRK2) is a single transmembrane catalytic receptor with intracellular tyrosine kinase activity. TrkB/NTRK2 is a member of the neurotrophic tyrosine receptor kinase (NTRK) family. TrkB tyrosine kinase (TrkB) or NTRK2 is coupled to the Ras, Cdc42/Rac/RhoG, MAPK, PI3-K, and PLCgamma signaling pathways. There are four members of the Trk family; TrkA, TrkB, and TrkC and a related p75NTR receptor. Each family member binds different neurotrophins with varying affinities. TrkB/NTRK has the highest affinity for brain-derived neurotrophic factor (BDNF) and is involved in neuronal plasticity, long-term potentiation, and apoptosis of CNS neurons. Other neurotrophins includenerve growth factor(NGF), neurotrophin-3 and neurotrophin-4. TrkB/NTRK is a membrane-bound receptor that, upon neurotrophin binding, phosphorylates itself and members of the MAPK pathway. Signaling through this kinase leads to cell differentiation. Mutations in TrkB/NTRK have been associated with obesity and mood disorders.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-00740 | SDF-1 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
The human stromal cell-derived factor-1 (SDF1), also known as CXCL12, is a small (8 kDa) cytokine highly conserved chemotactic cytokine belonging to the large family of CXC chemokines. SDF1 is expressed in two isoforms from a single gene that encodes two splice variants, SDF1α and SDF1β, which are identical except for the four residues present in the C-terminus of SDF1β but absent from SDF1α. The chemokine CXCL12 [stromal cell-derived factor-1 (SDF-1)] binds primarily to CXC receptor 4 (CXCR4; CD184). The binding of CXCL12 to CXCR4 induces intracellular signaling through several divergent pathways initiating signals related to chemotaxis, cell survival and/or proliferation, increase in intracellular calcium, and gene transcription. CXCL12 and CXCR4 that have been widely characterized in peripheral tissues and delineate their main functions in the CNS. Extensive evidence supports CXCL12 as a key regulator for early development of the CNS. In the mature CNS, CXCL12 modulates neurotransmission, neurotoxicity and neuroglial interactions. CXCL12 has crucial roles in the formation of multiple organ systems during embryogenesis and in the regulation of bone marrow haematopoiesis and immune function in the postnatal organism. Although considered an important factor in normal bone metabolism, recent studies implicate CXCL12 in the pathogenesis of several diseases involving the skeleton, including rheumatoid arthritis and cancers that metastasize to bone. The CXCL12/CXCR4 axis is involved in tumor progression, angiogenesis, metastasis, and survival. Pathologically enhanced CXCL12 signaling may promote the formation of new vessels through recruiting circulating endothelial progenitor cells or directly enhancing the migration/growth of endothelial cells. Therefore, CXCL12 signaling represents an important mechanism that regulates brain tumor angiogenesis/vasculogenesis and may provide potential targets for anti-angiogenic therapy in malignant gliomas.
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TMPY-02591 | SDF-1 Protein, Human, Recombinant | Human | E. coli | ||
The human stromal cell-derived factor-1 (SDF1), also known as CXCL12, is a small (8 kDa) cytokine highly conserved chemotactic cytokine belonging to the large family of CXC chemokines. SDF1 is expressed in two isoforms from a single gene that encodes two splice variants, SDF1α and SDF1β, which are identical except for the four residues present in the C-terminus of SDF1β but absent from SDF1α. The chemokine CXCL12 [stromal cell-derived factor-1 (SDF-1)] binds primarily to CXC receptor 4 (CXCR4; CD184). The binding of CXCL12 to CXCR4 induces intracellular signaling through several divergent pathways initiating signals related to chemotaxis, cell survival and/or proliferation, increase in intracellular calcium, and gene transcription. CXCL12 and CXCR4 that have been widely characterized in peripheral tissues and delineate their main functions in the CNS. Extensive evidence supports CXCL12 as a key regulator for early development of the CNS. In the mature CNS, CXCL12 modulates neurotransmission, neurotoxicity and neuroglial interactions. CXCL12 has crucial roles in the formation of multiple organ systems during embryogenesis and in the regulation of bone marrow haematopoiesis and immune function in the postnatal organism. Although considered an important factor in normal bone metabolism, recent studies implicate CXCL12 in the pathogenesis of several diseases involving the skeleton, including rheumatoid arthritis and cancers that metastasize to bone. The CXCL12/CXCR4 axis is involved in tumor progression, angiogenesis, metastasis, and survival. Pathologically enhanced CXCL12 signaling may promote the formation of new vessels through recruiting circulating endothelial progenitor cells or directly enhancing the migration/growth of endothelial cells. Therefore, CXCL12 signaling represents an important mechanism that regulates brain tumor angiogenesis/vasculogenesis and may provide potential targets for anti-angiogenic therapy in malignant gliomas.
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TMPY-02820 | SDF-1 Protein, Human, Recombinant (isoform a) | Human | E. coli | ||
The human stromal cell-derived factor-1 (SDF1), also known as CXCL12, is a small (8 kDa) cytokine highly conserved chemotactic cytokine belonging to the large family of CXC chemokines. SDF1 is expressed in two isoforms from a single gene that encodes two splice variants, SDF1α and SDF1β, which are identical except for the four residues present in the C-terminus of SDF1β but absent from SDF1α. The chemokine CXCL12 [stromal cell-derived factor-1 (SDF-1)] binds primarily to CXC receptor 4 (CXCR4; CD184). The binding of CXCL12 to CXCR4 induces intracellular signaling through several divergent pathways initiating signals related to chemotaxis, cell survival and/or proliferation, increase in intracellular calcium, and gene transcription. CXCL12 and CXCR4 that have been widely characterized in peripheral tissues and delineate their main functions in the CNS. Extensive evidence supports CXCL12 as a key regulator for early development of the CNS. In the mature CNS, CXCL12 modulates neurotransmission, neurotoxicity and neuroglial interactions. CXCL12 has crucial roles in the formation of multiple organ systems during embryogenesis and in the regulation of bone marrow haematopoiesis and immune function in the postnatal organism. Although considered an important factor in normal bone metabolism, recent studies implicate CXCL12 in the pathogenesis of several diseases involving the skeleton, including rheumatoid arthritis and cancers that metastasize to bone. The CXCL12/CXCR4 axis is involved in tumor progression, angiogenesis, metastasis, and survival. Pathologically enhanced CXCL12 signaling may promote the formation of new vessels through recruiting circulating endothelial progenitor cells or directly enhancing the migration/growth of endothelial cells. Therefore, CXCL12 signaling represents an important mechanism that regulates brain tumor angiogenesis/vasculogenesis and may provide potential targets for anti-angiogenic therapy in malignant gliomas.
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TMPY-05053 | ANGPTL2 Protein, Human, Recombinant (His) | Human | HEK293 | ||
The angiopoietin-like protein (ANGPTL) family is homologous to angiopoietins but does not bind to the Tie2 receptor. The function of ANGPTLs has been elucidated largely in the context of angiogenesis and lipid metabolism. Morinaga et al. demonstrated that genetic depletion of Angptl2 confers amelioration of the mouse kidney fibrosis induced by a unilateral ureteral obstruction, implicating that ANGPTL2, predominantly in the renal tubular compartments, activates the transforming growth factor-β signaling and vice versa through miR-221. Angiopoietin-like protein 2 (ANGPTL2) maintains tissue homeostasis by inducing inflammation and angiogenesis. It is produced in infiltrating immune cells or resident cells, such as adipocytes, vascular endothelial cells, and tumor cells. The classic sequential cascade of P. gingivalis LPS → inflammatory cytokine induction is well established. However, in the current study, we reveal a novel cascade comprising sequential P. gingivalis LPS → ANGPTL2 → integrin α5β1 → inflammatory cytokine induction, which might be responsible for inducing potent periodontal disorganization activity in gingival epithelial cells. Via this pathway, ANGPTL2 functions in the pathogenesis of periodontitis and contributes to prolonging chronic inflammation in patients with systemic disease. That MAC-3-positive immune cells, including infiltrating bone marrow-derived macrophages and activated microglia, express abundant angiopoietin-like protein (ANGPTL) 2 in ischemic mouse brain in a transient middle cerebral artery occlusion (MCAO) model. Both neurological deficits and infarct volume decreased in transient MCAO model mice established in Angptl2 knockout (KO) relative to wild-type mice. Acute brain inflammation after ischemia-reperfusion, as estimated by expression levels of pro-inflammatory cytokines such as interleukin (IL)-1β and tumor necrosis factor alpha (TNF)-α, was significantly suppressed in Angptl2 KO compared to control mice.
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TMPY-02614 | NGFR/p75NTR Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Nerve growth factor receptors (NGFRs) belong to a large growth factor receptor family. NGFR includes two types of receptors: high-affinity nerve growth factor receptor and low-affinity nerve growth factor receptor. The high-affinity nerve growth factor receptor is also referred to as the Trk family whose members are bound by some neurotrophins with high affinity.Nerve growth factorbinds with TrkA after being released from target cells, the NGF / TrkA complex is subsequently trafficked back to the cell body. The Low-affinity nerve growth factor receptor also named p75 which binds with all kinds of neurotrophins with low affinity. All four kinds of neurotrophins, including Nerve growth factor, Brain-derived neurotrophic factor, Neurotrophin-3, and Neurotrophin-4 bind to the p75. Studies have proved that NGFR acts as a molecular signal switch that determines cell death or survival by three steps. First, pro-nerve growth factor (prNGF) triggers cell apoptosis by its high-affinity binding to p75NTR, while NGF induces neuronal survival with low-affinity binding. Second, p75NTR mediates cell death by combining with co-receptor Sortilin, whereas it promotes neuronal survival through combination with proNGF. Third, the release of the intracellular domain chopper or cleavage short p75 NTR can independently initiate neuronal apoptosis.
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TMPY-01084 | TrkA Protein, Human, Recombinant (His) | Human | HEK293 | ||
TRKA is a member of the neurotrophic tyrosine kinase receptor (NTKR) family. It is a membrane-bound receptor that, upon neurotrophin binding, phosphorylates itself and members of the MAPK pathway. Isoform TrkA-III promotes angiogenesis and has oncogenic activity when overexpressed. Isoform TrkA-I is found in most non-neuronal tissues. Isoform TrkA-II is primarily expressed in neuronal cells. TrkA-III is specifically expressed by the pluripotent neural stem and neural crest progenitors. The presence of NTRK1 leads to cell differentiation and may play a role in specifying sensory neuron subtypes. Mutations in the TRKA gene have been associated with congenital insensitivity to pain, anhidrosis, self-mutilating behavior, mental retardation, and cancer. It was originally identified as an oncogene as it is commonly mutated in cancers, particularly colon and thyroid carcinomas. TRKA is required for high-affinity binding tonerve growth factor (NGF), neurotrophin-3 and neurotrophin-4/5 but not brain-derived neurotrophic factor (BDNF). Known substrates for the Trk receptors are SHC1, PI 3-kinase, and PLC-gamma-1. NTRK1 has a crucial role in the development and function of the nociceptive reception system as well as the establishment of thermal regulation via sweating. It also activates ERK1 by either SHC1- or PLC-gamma-1-dependent signaling pathway. Defects in NTRK1 are a cause of congenital insensitivity to pain with anhidrosis and thyroid papillary carcinoma.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPH-02241 | TMEM158 Protein, Human, Recombinant (His) | Human | in vitro E. coli expression system | ||
Receptor for brain injury-derived neurotrophic peptide (BINP), a synthetic 13-mer peptide.
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TMPH-02980 | Aquaporin-4/AQP4 Protein, Mouse, Recombinant (His) | Mouse | Yeast | ||
Forms a water-specific channel. Plays an important role in brain water homeostasis and in glymphatic solute transport. Required for a normal rate of water exchange across the blood brain interface. Required for normal levels of cerebrospinal fluid influx into the brain cortex and parenchyma along paravascular spaces that surround penetrating arteries, and for normal drainage of interstitial fluid along paravenous drainage pathways. Thereby, it is required for normal clearance of solutes from the brain interstitial fluid, including soluble beta-amyloid peptides derived from APP. Plays a redundant role in urinary water homeostasis and urinary concentrating ability.
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TMPJ-01408 | HDGFRP3 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Hepatoma-Derived Growth Factor-Related Protein 3 (HDGFRP3) belongs to the HDGF family. HDGFRP3 can be found in testis, heart, spinal cord and brain. HDGFRP3 localizes to the nucleus and contains one PWWP domain. HDGFRP3 enhances DNA synthesis and may have a role in cell proliferation.
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TMPY-00438 | CNTN4 Protein, Mouse, Recombinant (His) | Mouse | Baculovirus-Insect Cells | ||
Contactin-4, abbreviated as CNTN4, is a brain-derived protein belonging to the immunoglobulin superfamily. It has been found high expression in testes, thyroid, small intestine, uterus and brain. This protein is an neuronal membrane protein that functions as an glycosylphosphatidylinositol- anchored cell adhesion molecule. Contactin-4 is considered as a candidate protein responsible for the differentiation potential of human neuroblastoma cells and it has been implicated in some cases of autism and spinocerebellar ataxia type 16. Studies of the cantactin family have revealed a complex pattern of hemophilic and heterophilic interactions that are required for axon growth and pathfinding. Such studies demonstrate that these essential functions are mediated by the combination and juxtaposition of multiple Ig and FNIII domains. Second, these neuronal adhesion molecules demonstrate highly regulated temporal and spatial expression patterns in the CNS. For this reason, the disruption of the regulatory region of the predominant brain-expressed isoform reasonable would be expected to have significant functional consequences.
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TMPY-01916 | CDNF Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Cerebral Dopamine Neurotrophic Factor (CDNF), also known as ARMETL1 (ARMET-like protein 1), is a secreted protein with eight conserved cysteine residues, predicting a unique protein fold and defining a new, evolutionarily conserved protein family. CDNF is a novel neurotrophic factor with strong trophic activity on dopaminergic neurons comparable to that of glial cell line-derived neurotrophic factor (GDNF). CDNF/ARMETL1 is a evolutionary conserved protein which can protect and restore the function of dopaminergic neurons in the rat model of Parkinson's disease, suggesting that CDNF might be beneficial for the treatment of Parkinson's disease. CDNF is widely expressed in neurons in several brain regions including cerebral cortex, hippocampus, substantia nigra, striatum and cerebellum. Human CDNF is glycosylated and secreted from transiently transfected cells. CDNF promotes the survival, growth, and function of dopamine-specific neurons and is expressed in brain regions that undergo cocaine-induced neuroplasticity.
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TMPY-00188 | CDNF Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Cerebral Dopamine Neurotrophic Factor (CDNF), also known as ARMETL1 (ARMET-like protein 1), is a secreted protein with eight conserved cysteine residues, predicting a unique protein fold and defining a new, evolutionarily conserved protein family. CDNF is a novel neurotrophic factor with strong trophic activity on dopaminergic neurons comparable to that of glial cell line-derived neurotrophic factor (GDNF). CDNF/ARMETL1 is a evolutionary conserved protein which can protect and restore the function of dopaminergic neurons in the rat model of Parkinson's disease, suggesting that CDNF might be beneficial for the treatment of Parkinson's disease. CDNF is widely expressed in neurons in several brain regions including cerebral cortex, hippocampus, substantia nigra, striatum and cerebellum. Human CDNF is glycosylated and secreted from transiently transfected cells. CDNF promotes the survival, growth, and function of dopamine-specific neurons and is expressed in brain regions that undergo cocaine-induced neuroplasticity.
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TMPY-02593 | CNTN4 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
Contactin-4, abbreviated as CNTN4, is a brain-derived protein belonging to the immunoglobulin superfamily. It has been found high expression in testes, thyroid, small intestine, uterus and brain. This protein is an neuronal membrane protein that functions as an glycosylphosphatidylinositol- anchored cell adhesion molecule. Contactin-4 is considered as a candidate protein responsible for the differentiation potential of human neuroblastoma cells and it has been implicated in some cases of autism and spinocerebellar ataxia type 16. Studies of the cantactin family have revealed a complex pattern of hemophilic and heterophilic interactions that are required for axon growth and pathfinding. Such studies demonstrate that these essential functions are mediated by the combination and juxtaposition of multiple Ig and FNIII domains. Second, these neuronal adhesion molecules demonstrate highly regulated temporal and spatial expression patterns in the CNS. For this reason, the disruption of the regulatory region of the predominant brain-expressed isoform reasonable would be expected to have significant functional consequences.
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TMPY-00568 | CDNF Protein, Human, Recombinant (His) | Human | HEK293 | ||
Cerebral Dopamine Neurotrophic Factor (CDNF), also known as ARMETL1 (ARMET-like protein 1), is a secreted protein with eight conserved cysteine residues, predicting a unique protein fold and defining a new, evolutionarily conserved protein family. CDNF is a novel neurotrophic factor with strong trophic activity on dopaminergic neurons comparable to that of glial cell line-derived neurotrophic factor (GDNF). CDNF/ARMETL1 is a evolutionary conserved protein which can protect and restore the function of dopaminergic neurons in the rat model of Parkinson's disease, suggesting that CDNF might be beneficial for the treatment of Parkinson's disease. CDNF is widely expressed in neurons in several brain regions including cerebral cortex, hippocampus, substantia nigra, striatum and cerebellum. Human CDNF is glycosylated and secreted from transiently transfected cells. CDNF promotes the survival, growth, and function of dopamine-specific neurons and is expressed in brain regions that undergo cocaine-induced neuroplasticity.
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TMPY-01118 | SLC27A4/FATP4 Protein, Human, Recombinant (His) | Human | HEK293 | ||
SLC27A4/ATG4B complex might act as a new potential therapeutic target of lung tumor chemotherapy. The solute carrier 27A (SLC27A) gene family encodes fatty acid transport proteins (FATPs) and includes 6 members. Autism spectrum disorders (ASD) are now recognized as disorders caused by impaired early brain development, it is possible that functional abnormalities of SLC27A genes may contribute to the pathogenesis of ASD. The expression of SLC27A3 and SLC27A4 in human neural stem cells derived from human induced pluripotent stem cells, which suggested their involvement in the developmental stage of the central nervous system.
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TMPY-00028 | ARMET/MANF Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Mesencephalic astrocyte-derived neurotrophic factor, also known as Protein ARMET, Arginine-rich protein, MANF, and ARMET, is a secreted protein that belongs to the ARMET family. ARMET selectively promotes the survival of dopaminergic neurons of the ventral midbrain. It modulates GABAergic transmission to the dopaminergic neurons of the substantia nigra. ARMET enhances spontaneous, as well as evoked, GABAergic inhibitory postsynaptic currents in dopaminergic neurons. ARMET inhibits cell proliferation and endoplasmic reticulum (ER) stress-induced cell death. The N-terminal region of ARMET may be responsible for neurotrophic activity while the C-terminal region may play a role in the ER stress response. MANF reduces endoplasmic reticulum (ER) stress and has neurotrophic effects on dopaminergic neurons. Intracortical delivery of recombinant MANF protein protects tissue from ischemic brain injury. MANF has been described as a survival factor for dopaminergic neurons. MANF expression was widespread in the nervous system and non-neuronal tissues. In the brain, relatively high MANF levels were detected in the cerebral cortex, hippocampus, and cerebellar Purkinje cells. The widespread expression of MANF together with its evolutionary conserved nature and regulation by brain insults suggests that it has important functions both under normal and pathological conditions in many tissue types.
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TMPY-01678 | ARMET/MANF Protein, Human, Recombinant (His) | Human | HEK293 | ||
Mesencephalic astrocyte-derived neurotrophic factor, also known as Protein ARMET, Arginine-rich protein, MANF, and ARMET, is a secreted protein that belongs to the ARMET family. ARMET selectively promotes the survival of dopaminergic neurons of the ventral midbrain. It modulates GABAergic transmission to the dopaminergic neurons of the substantia nigra. ARMET enhances spontaneous, as well as evoked, GABAergic inhibitory postsynaptic currents in dopaminergic neurons. ARMET inhibits cell proliferation and endoplasmic reticulum (ER) stress-induced cell death. The N-terminal region of ARMET may be responsible for neurotrophic activity while the C-terminal region may play a role in the ER stress response. MANF reduces endoplasmic reticulum (ER) stress and has neurotrophic effects on dopaminergic neurons. Intracortical delivery of recombinant MANF protein protects tissue from ischemic brain injury. MANF has been described as a survival factor for dopaminergic neurons. MANF expression was widespread in the nervous system and non-neuronal tissues. In the brain, relatively high MANF levels were detected in the cerebral cortex, hippocampus, and cerebellar Purkinje cells. The widespread expression of MANF together with its evolutionary conserved nature and regulation by brain insults suggests that it has important functions both under normal and pathological conditions in many tissue types.
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TMPY-01879 | S100A14 Protein, Human, Recombinant (His) | Human | E. coli | ||
S100 protein is a family of low molecular weight protein found in vertebrates characterized by two EF-hand calcium-binding motifs. There are at least 21 different S100 proteins, and the name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are disulfide-linked homodimer, and is normally present in cells derived from theneural crest, chondrocytes, macrophages, dendritic cells, etc. S100 proteins have been implicated in a variety of intracellular and extracellular functions. They are involved in regulation of protein phosphorylation, transcription factors, the dynamics of cytoskeleton constituents, enzyme activities, cell growth and differentiation, and the inflammatory response. Protein S100-A14, also known as S100 calciumbinding protein A14, S114 and S100A14, is a cytoplasm protein which belongs to the S-100 family. It is expressed at highest levels in colon and at moderate levels in thymus, kidney, liver, small intestine, and lung. Low expression in heart and no expression is seen in brain, skeletal muscle, spleen, placenta and peripheral blood leukocytes.
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TMPY-03736 | REG1B Protein, Rhesus, Recombinant (hFc) | Rhesus | HEK293 | ||
Regenerating gene (Reg), first isolated from a regenerating islet cDNA library, encodes a secretory protein with a growth stimulating effect on pancreatic beta cells, and could be associated with fibrocalculous pancreatopathy. Reg and Reg-related genes which were expressed in various organs have been revealed to constitute a multigene family, the Reg family consisting of four subtypes (types I, II, III, IV) and are involved in cancers and neurodegenerative diseases. Regenerating islet-derived 1 beta (REG1B), also known as Lithostathine-1-beta and Pancreatic stone protein 2 (PSPS2), is a types I Reg protein and contains one typical C-type lectin domain. REG1B is a 166-amino acid protein that has 22 amino acid substitutions in comparison with the previously isolated human REG1A, and it is was expressed only in pancreas. REG1B Is normally found in the exocrine pancreas, whereas in other tissues it appears either only under pathological conditions, such as Alzheimer's disease (brain), cancer (colon), or during regeneration such as neuronal sprouting in brain and pancreas regeneration. REG1B might act as an inhibitor of spontaneous calcium carbonate precipitation. The REG1A and REG1B gene and proteins could play different roles in the pancreas.
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TMPY-01931 | S100A5 Protein, Human, Recombinant (His) | Human | E. coli | ||
S100 protein is a family of low molecular weight protein found in vertebrates characterized by two EF-hand calcium-binding motifs. There are at least 21 different S100 proteins, and the name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are disulfide-linked homodimer, and is normally present in cells derived from the?neural crest, chondrocytes, macrophages, dendritic cells, etc. S100 proteins have been implicated in a variety of intracellular and extracellular functions. They are involved in regulation of protein phosphorylation, transcription factors, the dynamics of cytoskeleton constituents, enzyme activities, cell growth and differentiation, and the inflammatory response. Protein S100-A5, also known as Protein S-100D, S100 calcium-binding protein A5, S100A5 and S100D, is a member of the S100 family which contains two EF-hand domains. S100A5 is also a novel member of the EF-hand superfamily of calcium-binding proteins that is poorly characterized at the protein level. It is expressed in very restricted regions of the adult brain. From birth onwards, S100A5 remained a neuronal-specific protein, only located in a subpopulation of neurons in the spiral ganglion.
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TMPY-02732 | ARMET/MANF Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Mesencephalic astrocyte-derived neurotrophic factor, also known as Protein ARMET, Arginine-rich protein, MANF, and ARMET, is a secreted protein that belongs to the ARMET family. ARMET selectively promotes the survival of dopaminergic neurons of the ventral midbrain. It modulates GABAergic transmission to the dopaminergic neurons of the substantia nigra. ARMET enhances spontaneous, as well as evoked, GABAergic inhibitory postsynaptic currents in dopaminergic neurons. ARMET inhibits cell proliferation and endoplasmic reticulum (ER) stress-induced cell death. The N-terminal region of ARMET may be responsible for neurotrophic activity while the C-terminal region may play a role in the ER stress response. MANF reduces endoplasmic reticulum (ER) stress and has neurotrophic effects on dopaminergic neurons. Intracortical delivery of recombinant MANF protein protects tissue from ischemic brain injury. MANF has been described as a survival factor for dopaminergic neurons. MANF expression was widespread in the nervous system and non-neuronal tissues. In the brain, relatively high MANF levels were detected in the cerebral cortex, hippocampus, and cerebellar Purkinje cells. The widespread expression of MANF together with its evolutionary conserved nature and regulation by brain insults suggests that it has important functions both under normal and pathological conditions in many tissue types.
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TMPY-03092 | REG1A Protein, Rat, Recombinant (hFc) | Rat | HEK293 | ||
Regenerating (reg) gene encodes protein that has been involved in pancreatic lithogenesis and the regeneration of islet cells and therefore the abnormality of reg genes could be associated with fibrocalculous pancreatopathy. REG I has been shown to be crucial for induction of ductal epithelial cells to differentiate into some cells. Lithostathine-1-alpha, also known as Pancreatic stone protein, Pancreatic thread protein, Regenerating islet-derived protein 1-alpha, REG1A, REG-1-alpha, and PSPS, is highly expressed in fetal and infant brains. REG1A contains one C-type lectin domain and is a known growth factor affecting pancreatic islet beta cells. REG1A may act as an inhibitor of spontaneous calcium carbonate precipitation. It may also be associated with neuronal sprouting in brain, and with brain and pancreas regeneration. REG1A has been reported to be expressed in human cancers, and it may be positively correlated with patient's prognosis. REG3A and REG1A proteins are both involved in liver and pancreatic regeneration and proliferation. High levels of REG1A expression by tumor cells are an independent predictor of a poor prognosis in patients with non-small cell lung cancer (NSCLC).
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TMPY-03639 | REG1A Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 | ||
Regenerating (reg) gene encodes protein that has been involved in pancreatic lithogenesis and the regeneration of islet cells and therefore the abnormality of reg genes could be associated with fibrocalculous pancreatopathy. REG I has been shown to be crucial for induction of ductal epithelial cells to differentiate into some cells. Lithostathine-1-alpha, also known as Pancreatic stone protein, Pancreatic thread protein, Regenerating islet-derived protein 1-alpha, REG1A, REG-1-alpha, and PSPS, is highly expressed in fetal and infant brains. REG1A contains one C-type lectin domain and is a known growth factor affecting pancreatic islet beta cells. REG1A may act as an inhibitor of spontaneous calcium carbonate precipitation. It may also be associated with neuronal sprouting in brain, and with brain and pancreas regeneration. REG1A has been reported to be expressed in human cancers, and it may be positively correlated with patient's prognosis. REG3A and REG1A proteins are both involved in liver and pancreatic regeneration and proliferation. High levels of REG1A expression by tumor cells are an independent predictor of a poor prognosis in patients with non-small cell lung cancer (NSCLC).
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TMPY-00782 | ECE2 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
Endothelin-converting enzyme 2, also known as ECE-2, is a metalloprotease that possesses many properties consistent with it being a neuropeptide-processing enzyme. Endothelin-converting enzymes (ECEs) are the key enzymes in the endothelin (ET) biosynthesis that catalyze the conversion of big ET, the biologically inactive precursor of mature ET. Two enzymes, termed ECE-1 and ECE-2, have been molecularly identified. ECE-2 is found primarily in neural tissues, with high levels of expression in midbrain, cerebellum, hypothalamus, frontal cortex and spinal cord and moderate levels in hippocampus and striatum. ECE-2 is strongly down-regulated in inferior parietal lobe from Alzheimer disease patients (at protein level). ECE-2 converts big endothelin-1 to endothelin-1. It is involved in the processing of various neuroendocrine peptides, including neurotensin, angiotensin I, substance P, proenkephalin-derived peptides, and prodynorphin-derived peptides. ECE-2 may limit beta-amyloid peptide accumulation in brain. It may also have methyltransferase activity. A comparison of residues around the cleavage site revealed that ECE-2 exhibits a unique cleavage site selectivity that is related to but distinct from that of ECE-1.
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TMPY-01891 | ECE2 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Endothelin-converting enzyme 2, also known as ECE-2, is a metalloprotease that possesses many properties consistent with it being a neuropeptide-processing enzyme. Endothelin-converting enzymes (ECEs) are the key enzymes in the endothelin (ET) biosynthesis that catalyze the conversion of big ET, the biologically inactive precursor of mature ET. Two enzymes, termed ECE-1 and ECE-2, have been molecularly identified. ECE-2 is found primarily in neural tissues, with high levels of expression in midbrain, cerebellum, hypothalamus, frontal cortex and spinal cord and moderate levels in hippocampus and striatum. ECE-2 is strongly down-regulated in inferior parietal lobe from Alzheimer disease patients (at protein level). ECE-2 converts big endothelin-1 to endothelin-1. It is involved in the processing of various neuroendocrine peptides, including neurotensin, angiotensin I, substance P, proenkephalin-derived peptides, and prodynorphin-derived peptides. ECE-2 may limit beta-amyloid peptide accumulation in brain. It may also have methyltransferase activity. A comparison of residues around the cleavage site revealed that ECE-2 exhibits a unique cleavage site selectivity that is related to but distinct from that of ECE-1.
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TMPY-05474 | REG1A Protein, Human, Recombinant (His), Biotinylated | Human | HEK293 | ||
Regenerating (reg) gene encodes protein that has been involved in pancreatic lithogenesis and the regeneration of islet cells and therefore the abnormality of reg genes could be associated with fibrocalculous pancreatopathy. REG I has been shown to be crucial for induction of ductal epithelial cells to differentiate into some cells. Lithostathine-1-alpha, also known as Pancreatic stone protein, Pancreatic thread protein, Regenerating islet-derived protein 1-alpha, REG1A, REG-1-alpha, and PSPS, is highly expressed in fetal and infant brains. REG1A contains one C-type lectin domain and is a known growth factor affecting pancreatic islet beta cells. REG1A may act as an inhibitor of spontaneous calcium carbonate precipitation. It may also be associated with neuronal sprouting in brain, and with brain and pancreas regeneration. REG1A has been reported to be expressed in human cancers, and it may be positively correlated with patient's prognosis. REG3A and REG1A proteins are both involved in liver and pancreatic regeneration and proliferation. High levels of REG1A expression by tumor cells are an independent predictor of a poor prognosis in patients with non-small cell lung cancer (NSCLC).
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TMPY-01335 | REG1A Protein, Human, Recombinant (His) | Human | HEK293 | ||
Regenerating (reg) gene encodes protein that has been involved in pancreatic lithogenesis and the regeneration of islet cells and therefore the abnormality of reg genes could be associated with fibrocalculous pancreatopathy. REG I has been shown to be crucial for induction of ductal epithelial cells to differentiate into some cells. Lithostathine-1-alpha, also known as Pancreatic stone protein, Pancreatic thread protein, Regenerating islet-derived protein 1-alpha, REG1A, REG-1-alpha, and PSPS, is highly expressed in fetal and infant brains. REG1A contains one C-type lectin domain and is a known growth factor affecting pancreatic islet beta cells. REG1A may act as an inhibitor of spontaneous calcium carbonate precipitation. It may also be associated with neuronal sprouting in brain, and with brain and pancreas regeneration. REG1A has been reported to be expressed in human cancers, and it may be positively correlated with patient's prognosis. REG3A and REG1A proteins are both involved in liver and pancreatic regeneration and proliferation. High levels of REG1A expression by tumor cells are an independent predictor of a poor prognosis in patients with non-small cell lung cancer (NSCLC).
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TMPY-01394 | REG1B Protein, Human, Recombinant (His) | Human | HEK293 | ||
Regenerating gene (Reg), first isolated from a regenerating islet cDNA library, encodes a secretory protein with a growth stimulating effect on pancreatic beta cells, and could be associated with fibrocalculous pancreatopathy. Reg and Reg-related genes which were expressed in various organs have been revealed to constitute a multigene family, the Reg family consisting of four subtypes (types I, II, III, IV) and are involved in cancers and neurodegenerative diseases. Regenerating islet-derived 1 beta (REG1B), also known as Lithostathine-1-beta and Pancreatic stone protein 2 (PSPS2), is a types I Reg protein and contains one typical C-type lectin domain. REG1B is a 166-amino acid protein that has 22 amino acid substitutions in comparison with the previously isolated human REG1A, and it is was expressed only in pancreas. REG1B Is normally found in the exocrine pancreas, whereas in other tissues it appears either only under pathological conditions, such as Alzheimer's disease (brain), cancer (colon), or during regeneration such as neuronal sprouting in brain and pancreas regeneration. REG1B might act as an inhibitor of spontaneous calcium carbonate precipitation. The REG1A and REG1B gene and proteins could play different roles in the pancreas.
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TMPY-03478 | REG1B Protein, Rhesus, Recombinant (His) | Rhesus | HEK293 | ||
Regenerating gene (Reg), first isolated from a regenerating islet cDNA library, encodes a secretory protein with a growth stimulating effect on pancreatic beta cells, and could be associated with fibrocalculous pancreatopathy. Reg and Reg-related genes which were expressed in various organs have been revealed to constitute a multigene family, the Reg family consisting of four subtypes (types I, II, III, IV) and are involved in cancers and neurodegenerative diseases. Regenerating islet-derived 1 beta (REG1B), also known as Lithostathine-1-beta and Pancreatic stone protein 2 (PSPS2), is a types I Reg protein and contains one typical C-type lectin domain. REG1B is a 166-amino acid protein that has 22 amino acid substitutions in comparison with the previously isolated human REG1A, and it is was expressed only in pancreas. REG1B Is normally found in the exocrine pancreas, whereas in other tissues it appears either only under pathological conditions, such as Alzheimer's disease (brain), cancer (colon), or during regeneration such as neuronal sprouting in brain and pancreas regeneration. REG1B might act as an inhibitor of spontaneous calcium carbonate precipitation. The REG1A and REG1B gene and proteins could play different roles in the pancreas.
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TMPY-03684 | REG1A Protein, Cynomolgus, Recombinant (hFc) | Cynomolgus | HEK293 | ||
Regenerating (reg) gene encodes protein that has been involved in pancreatic lithogenesis and the regeneration of islet cells and therefore the abnormality of reg genes could be associated with fibrocalculous pancreatopathy. REG I has been shown to be crucial for induction of ductal epithelial cells to differentiate into some cells. Lithostathine-1-alpha, also known as Pancreatic stone protein, Pancreatic thread protein, Regenerating islet-derived protein 1-alpha, REG1A, REG-1-alpha, and PSPS, is highly expressed in fetal and infant brains. REG1A contains one C-type lectin domain and is a known growth factor affecting pancreatic islet beta cells. REG1A may act as an inhibitor of spontaneous calcium carbonate precipitation. It may also be associated with neuronal sprouting in brain, and with brain and pancreas regeneration. REG1A has been reported to be expressed in human cancers, and it may be positively correlated with patient's prognosis. REG3A and REG1A proteins are both involved in liver and pancreatic regeneration and proliferation. High levels of REG1A expression by tumor cells are an independent predictor of a poor prognosis in patients with non-small cell lung cancer (NSCLC).
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TMPY-02463 | S100A5 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
S100 protein is a family of low molecular weight protein found in vertebrates characterized by two EF-hand calcium-binding motifs. There are at least 21 different S100 proteins, and the name is derived from the fact that the protein is 100% soluble in ammonium sulfate at neutral pH. Most S100 proteins are disulfide-linked homodimer, and is normally present in cells derived from the?neural crest, chondrocytes, macrophages, dendritic cells, etc. S100 proteins have been implicated in a variety of intracellular and extracellular functions. They are involved in regulation of protein phosphorylation, transcription factors, the dynamics of cytoskeleton constituents, enzyme activities, cell growth and differentiation, and the inflammatory response. Protein S100-A5, also known as Protein S-100D, S100 calcium-binding protein A5, S100A5 and S100D, is a member of the S100 family which contains two EF-hand domains. S100A5 is also a novel member of the EF-hand superfamily of calcium-binding proteins that is poorly characterized at the protein level. It is expressed in very restricted regions of the adult brain. From birth onwards, S100A5 remained a neuronal-specific protein, only located in a subpopulation of neurons in the spiral ganglion.
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TMPY-01404 | CD200R4 Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
Cell surface glycoprotein CD2 receptor 4, also known as Cell surface glycoprotein OX2 receptor 4, CD2 cell surface glycoprotein receptor-like 4, CD2RLa, and CD2R4, is a single-pass type I membrane protein which belongs to theCD2R family. CD2 (OX2) is a cell surface glycoprotein that interacts with a structurally related receptor (CD2R) expressed mainly on myeloid cells and is involved in regulation of macrophage and mast cell function. In mouse there are up to five genes related to CD2R with conflicting data as to whether they bind CD2. CD2R4 contains oneIg-like C2-type (immunoglobulin-like) domain and one Ig-like V-type (immunoglobulin-like) domain. CD2R4 is highly expressed in monocytes, NK cells and a subset of NKT cells. It is weakly expressed in granulocytes and B cells (at protein level). CD2R4 is also expressed in brain, lung, testis, thymus, intestine and uterus. and in bone marrow derived-macrophage and dendritic cells and mast cells. CD2R4 is involved in the recruitment or surface expression of the TYROBP receptor.
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TMPY-02917 | TrkB Protein, Rat, Recombinant (hFc) | Rat | HEK293 | ||
TrkB receptor also known as TrkB tyrosine kinase or BDNF/NT-3 growth factors receptor or neurotrophic tyrosine kinase, receptor, type 2 (NTRK2) is a single transmembrane catalytic receptor with intracellular tyrosine kinase activity. TrkB/NTRK2 is a member of the neurotrophic tyrosine receptor kinase (NTRK) family. TrkB tyrosine kinase (TrkB) or NTRK2 is coupled to the Ras, Cdc42/Rac/RhoG, MAPK, PI3-K, and PLCgamma signaling pathways. There are four members of the Trk family; TrkA, TrkB, and TrkC and a related p75NTR receptor. Each family member binds different neurotrophins with varying affinities. TrkB/NTRK has the highest affinity for brain-derived neurotrophic factor (BDNF) and is involved in neuronal plasticity, long-term potentiation, and apoptosis of CNS neurons. Other neurotrophins includenerve growth factor(NGF), neurotrophin-3 and neurotrophin-4. TrkB/NTRK is a membrane-bound receptor that, upon neurotrophin binding, phosphorylates itself and members of the MAPK pathway. Signaling through this kinase leads to cell differentiation. Mutations in TrkB/NTRK have been associated with obesity and mood disorders.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-03635 | TrkB Protein, Canine, Recombinant (His) | Canine | HEK293 | ||
TrkB receptor also known as TrkB tyrosine kinase or BDNF/NT-3 growth factors receptor or neurotrophic tyrosine kinase, receptor, type 2 (NTRK2) is a single transmembrane catalytic receptor with intracellular tyrosine kinase activity. TrkB/NTRK2 is a member of the neurotrophic tyrosine receptor kinase (NTRK) family. TrkB tyrosine kinase (TrkB) or NTRK2 is coupled to the Ras, Cdc42/Rac/RhoG, MAPK, PI3-K, and PLCgamma signaling pathways. There are four members of the Trk family; TrkA, TrkB, and TrkC and a related p75NTR receptor. Each family member binds different neurotrophins with varying affinities. TrkB/NTRK has the highest affinity for brain-derived neurotrophic factor (BDNF) and is involved in neuronal plasticity, long-term potentiation, and apoptosis of CNS neurons. Other neurotrophins includenerve growth factor(NGF), neurotrophin-3 and neurotrophin-4. TrkB/NTRK is a membrane-bound receptor that, upon neurotrophin binding, phosphorylates itself and members of the MAPK pathway. Signaling through this kinase leads to cell differentiation. Mutations in TrkB/NTRK have been associated with obesity and mood disorders.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-05509 | TrkB Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
TrkB receptor also known as TrkB tyrosine kinase or BDNF/NT-3 growth factors receptor or neurotrophic tyrosine kinase, receptor, type 2 (NTRK2) is a single transmembrane catalytic receptor with intracellular tyrosine kinase activity. TrkB/NTRK2 is a member of the neurotrophic tyrosine receptor kinase (NTRK) family. TrkB tyrosine kinase (TrkB) or NTRK2 is coupled to the Ras, Cdc42/Rac/RhoG, MAPK, PI3-K, and PLCgamma signaling pathways. There are four members of the Trk family; TrkA, TrkB, and TrkC and a related p75NTR receptor. Each family member binds different neurotrophins with varying affinities. TrkB/NTRK has the highest affinity for brain-derived neurotrophic factor (BDNF) and is involved in neuronal plasticity, long-term potentiation, and apoptosis of CNS neurons. Other neurotrophins includenerve growth factor(NGF), neurotrophin-3 and neurotrophin-4. TrkB/NTRK is a membrane-bound receptor that, upon neurotrophin binding, phosphorylates itself and members of the MAPK pathway. Signaling through this kinase leads to cell differentiation. Mutations in TrkB/NTRK have been associated with obesity and mood disorders.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-00228 | TrkB Protein, Canine, Recombinant (hFc) | Canine | HEK293 | ||
TrkB receptor also known as TrkB tyrosine kinase or BDNF/NT-3 growth factors receptor or neurotrophic tyrosine kinase, receptor, type 2 (NTRK2) is a single transmembrane catalytic receptor with intracellular tyrosine kinase activity. TrkB/NTRK2 is a member of the neurotrophic tyrosine receptor kinase (NTRK) family. TrkB tyrosine kinase (TrkB) or NTRK2 is coupled to the Ras, Cdc42/Rac/RhoG, MAPK, PI3-K, and PLCgamma signaling pathways. There are four members of the Trk family; TrkA, TrkB, and TrkC and a related p75NTR receptor. Each family member binds different neurotrophins with varying affinities. TrkB/NTRK has the highest affinity for brain-derived neurotrophic factor (BDNF) and is involved in neuronal plasticity, long-term potentiation, and apoptosis of CNS neurons. Other neurotrophins includenerve growth factor(NGF), neurotrophin-3 and neurotrophin-4. TrkB/NTRK is a membrane-bound receptor that, upon neurotrophin binding, phosphorylates itself and members of the MAPK pathway. Signaling through this kinase leads to cell differentiation. Mutations in TrkB/NTRK have been associated with obesity and mood disorders.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-03289 | SDF-1 Protein, Mouse, Recombinant | Mouse | E. coli | ||
The human stromal cell-derived factor-1 (SDF1), also known as CXCL12, is a small (8 kDa) cytokine highly conserved chemotactic cytokine belonging to the large family of CXC chemokines. SDF1 is expressed in two isoforms from a single gene that encodes two splice variants, SDF1α and SDF1β, which are identical except for the four residues present in the C-terminus of SDF1β but absent from SDF1α. The chemokine CXCL12 [stromal cell-derived factor-1 (SDF-1)] binds primarily to CXC receptor 4 (CXCR4; CD184). The binding of CXCL12 to CXCR4 induces intracellular signaling through several divergent pathways initiating signals related to chemotaxis, cell survival and/or proliferation, increase in intracellular calcium, and gene transcription. CXCL12 and CXCR4 that have been widely characterized in peripheral tissues and delineate their main functions in the CNS. Extensive evidence supports CXCL12 as a key regulator for early development of the CNS. In the mature CNS, CXCL12 modulates neurotransmission, neurotoxicity and neuroglial interactions. CXCL12 has crucial roles in the formation of multiple organ systems during embryogenesis and in the regulation of bone marrow haematopoiesis and immune function in the postnatal organism. Although considered an important factor in normal bone metabolism, recent studies implicate CXCL12 in the pathogenesis of several diseases involving the skeleton, including rheumatoid arthritis and cancers that metastasize to bone. The CXCL12/CXCR4 axis is involved in tumor progression, angiogenesis, metastasis, and survival. Pathologically enhanced CXCL12 signaling may promote the formation of new vessels through recruiting circulating endothelial progenitor cells or directly enhancing the migration/growth of endothelial cells. Therefore, CXCL12 signaling represents an important mechanism that regulates brain tumor angiogenesis/vasculogenesis and may provide potential targets for anti-angiogenic therapy in malignant gliomas.
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TMPY-01348 | CD200R4 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Cell surface glycoprotein CD2 receptor 4, also known as Cell surface glycoprotein OX2 receptor 4, CD2 cell surface glycoprotein receptor-like 4, CD2RLa, and CD2R4, is a single-pass type I membrane protein which belongs to theCD2R family. CD2 (OX2) is a cell surface glycoprotein that interacts with a structurally related receptor (CD2R) expressed mainly on myeloid cells and is involved in regulation of macrophage and mast cell function. In mouse there are up to five genes related to CD2R with conflicting data as to whether they bind CD2. CD2R4 contains oneIg-like C2-type (immunoglobulin-like) domain and one Ig-like V-type (immunoglobulin-like) domain. CD2R4 is highly expressed in monocytes, NK cells and a subset of NKT cells. It is weakly expressed in granulocytes and B cells (at protein level). CD2R4 is also expressed in brain, lung, testis, thymus, intestine and uterus. and in bone marrow derived-macrophage and dendritic cells and mast cells. CD2R4 is involved in the recruitment or surface expression of the TYROBP receptor.
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TMPY-03162 | TrkB Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
TrkB receptor also known as TrkB tyrosine kinase or BDNF/NT-3 growth factors receptor or neurotrophic tyrosine kinase, receptor, type 2 (NTRK2) is a single transmembrane catalytic receptor with intracellular tyrosine kinase activity. TrkB/NTRK2 is a member of the neurotrophic tyrosine receptor kinase (NTRK) family. TrkB tyrosine kinase (TrkB) or NTRK2 is coupled to the Ras, Cdc42/Rac/RhoG, MAPK, PI3-K, and PLCgamma signaling pathways. There are four members of the Trk family; TrkA, TrkB, and TrkC and a related p75NTR receptor. Each family member binds different neurotrophins with varying affinities. TrkB/NTRK has the highest affinity for brain-derived neurotrophic factor (BDNF) and is involved in neuronal plasticity, long-term potentiation, and apoptosis of CNS neurons. Other neurotrophins includenerve growth factor(NGF), neurotrophin-3 and neurotrophin-4. TrkB/NTRK is a membrane-bound receptor that, upon neurotrophin binding, phosphorylates itself and members of the MAPK pathway. Signaling through this kinase leads to cell differentiation. Mutations in TrkB/NTRK have been associated with obesity and mood disorders.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-03580 | SDF-1 Protein, Canine, Recombinant | Canine | E. coli | ||
The human stromal cell-derived factor-1 (SDF1), also known as CXCL12, is a small (8 kDa) cytokine highly conserved chemotactic cytokine belonging to the large family of CXC chemokines. SDF1 is expressed in two isoforms from a single gene that encodes two splice variants, SDF1α and SDF1β, which are identical except for the four residues present in the C-terminus of SDF1β but absent from SDF1α. The chemokine CXCL12 [stromal cell-derived factor-1 (SDF-1)] binds primarily to CXC receptor 4 (CXCR4; CD184). The binding of CXCL12 to CXCR4 induces intracellular signaling through several divergent pathways initiating signals related to chemotaxis, cell survival and/or proliferation, increase in intracellular calcium, and gene transcription. CXCL12 and CXCR4 that have been widely characterized in peripheral tissues and delineate their main functions in the CNS. Extensive evidence supports CXCL12 as a key regulator for early development of the CNS. In the mature CNS, CXCL12 modulates neurotransmission, neurotoxicity and neuroglial interactions. CXCL12 has crucial roles in the formation of multiple organ systems during embryogenesis and in the regulation of bone marrow haematopoiesis and immune function in the postnatal organism. Although considered an important factor in normal bone metabolism, recent studies implicate CXCL12 in the pathogenesis of several diseases involving the skeleton, including rheumatoid arthritis and cancers that metastasize to bone. The CXCL12/CXCR4 axis is involved in tumor progression, angiogenesis, metastasis, and survival. Pathologically enhanced CXCL12 signaling may promote the formation of new vessels through recruiting circulating endothelial progenitor cells or directly enhancing the migration/growth of endothelial cells. Therefore, CXCL12 signaling represents an important mechanism that regulates brain tumor angiogenesis/vasculogenesis and may provide potential targets for anti-angiogenic therapy in malignant gliomas.
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