目录号 | 产品详情 | 靶点 | |
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T8549 | Others | ||
HEPES 是两性离子化学缓冲剂,在 pH 值为 6.8 至 8.2 时为有效的缓冲液,广泛应用于细胞培养。它是溶酶体生物发生的有效诱导剂。 | |||
T3478 | GluR | ||
Ro 67-7476 是mGluR1的正变位调节剂,能增强表达 rat mGluR1a 的 HEK293 细胞中谷氨酸诱导的钙释放,EC50为 60.1 nM。它是 P-ERK1/2 激动剂,可以在外源添加谷氨酸的情况下激活 ERK1/2 磷酸化 (EC50=163.3 nM)。 | |||
T2A2476 | Endogenous Metabolite | ||
L-Hydroxyproline (L-Hydroxyprolin) 是羟脯氨酸的异构体之一,是药物生产中有用的手性结构单元。 | |||
T2431 | DYRK | ||
ID-8 是 DYRK 抑制剂,长时间培养能够维持胚胎干细胞的自我更新。 | |||
T38509 | Others | ||
MOPS (Morpholinopropane sulfonic acid), a widely employed biological buffering agent, effectively regulates the pH of mammalian cell culture media. | |||
T14181 | Others | ||
Alizarin Red S sodium (ARS sodium) 是一种蒽醌类染料,在检测细胞培养中的钙沉积具有广泛的应用。 | |||
T39007 | Others | ||
3,4-Dimethoxybenzamide 是分离自Streptoverticillium morookaense 固体培养物的酰胺。它是制备盐酸伊托必利的起始原料。 | |||
T67854 | Others | ||
BAS 00489700是一种N-UTR 相互作用抑制剂。BAS 00489700抑制培养细胞中的病毒复制。 | |||
T4915 | Phosphatase Endogenous Metabolite | ||
β-Glycerophosphate disodium salt hydrate 是一种磷酸酶抑制剂,是内源性代谢产物的一种。 | |||
T4S1521 | HIV Protease | ||
1,4-Dicaffeoylquinic acid 是一种苯丙素类物质,从苍耳子中获得,可以减少 LPS 诱导的 TNF-α 的生成,具有抗炎活性。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-00210 | FGF-2 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Basic fibroblast growth factor (bFGF), also known as FGF2, is a member of the fibroblast growth factor (FGF) family. It is a highly specific chemotactic and mitogenic factor for many cell types, appears to be involved in remodeling damaged tissue, such as ulcer healing, vascular repair, traumatic brain injury (TBI). bFGF is a critical component of human embryonic stem cell culture medium. In addition, bFGF protein is a heparin-binding cationic protein involved in a variety of pathological conditions including angiogenesis and solid tumour growth. Thus, bFGF is regarded as a target for cancers chemopreventive and therapeutic strategies.bFGF/FGF2 Protein & Antibody Products
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TMPY-00749 | FGF-2 Protein, Human, Recombinant | Human | E. coli | ||
Basic fibroblast growth factor (bFGF), also known as FGF2, is a member of the fibroblast growth factor (FGF) family. It is a highly specific chemotactic and mitogenic factor for many cell types, appears to be involved in remodeling damaged tissue, such as ulcer healing, vascular repair, traumatic brain injury (TBI). bFGF is a critical component of human embryonic stem cell culture medium. In addition, bFGF protein is a heparin-binding cationic protein involved in a variety of pathological conditions including angiogenesis and solid tumour growth. Thus, bFGF is regarded as a target for cancers chemopreventive and therapeutic strategies.bFGF/FGF2 Protein & Antibody Products
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TMPY-00539 | GSTA1 Protein, Human, Recombinant (His) | Human | HEK293 | ||
GSTA1 (Glutathione S-Transferase Alpha 1) is a Protein Coding gene. This gene encodes a member of a family of enzymes that function to add glutathione to target electrophilic compounds. Glutathione S-transferases (GSTs) are involved in the detoxification of carcinogens and may be linked to carcinogenesis. As a vital component of GSTs, GSTA1 plays an important role in carcinogenesis. GSTA1 expression may be a target molecule in the early diagnosis and treatment of lung cancer. Human colonic adenocarcinoma (Caco-2) cells in culture undergo spontaneous differentiation into mature enterocytes in association with progressive increases in expression of glutathione S-transferase alpha-1 (GSTA1). GSTA1 levels may play a role in modulating enterocyte proliferation but do not influence differentiation or apoptosis. GSTA1 may play a key role during pregnancy.
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TMPJ-01065 | Noggin/NOG Protein, Mouse, Recombinant (His) | Mouse | Human Cells | ||
Noggin is a secreted homodimeric glycoprotein that is an antagonist of bone morphogenetic proteins (BMPs). Mouse Noggin cDNA encodes a 232 amino acid (aa) residue precursor protein with 19 aa residue putative signal peptide that is cleaved to generate the 213 aa residue mature protein which is secreted as a homodimeric glycoprotein. Secreted Noggin probably remains close to the cell surface due to its binding of heparin-containing proteoglycans. Noggin binds some BMPs such as BMP4 with high affinity and others such as BMP7 with lower affinity. It antagonizes BMP bioactivities by blocking epitopes on BMPs that are needed for binding to both type I and type II receptors. Noggin is expressed in defined areas of the adult central nervous system and peripheral tissues such as lung, skeletal muscle and skin. During culture of human embryonic stem cells (hESC) or neural stem cells under certain conditions, addition of Noggin to antagonize BMP activity may allow stem cells to proliferate while maintaining their undifferentiated state, or alternatively, to differentiate into dopaminergic neurons.
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TMPY-02412 | ENO1 Protein, Human, Recombinant (His) | Human | E. coli | ||
The ENO1 gene encodes a multifunctional enzyme that has been identified as a key component of the glycolytic pathway. ENO1 overexpression and post-translational modifications could be of diagnostic and prognostic value in many cancer types. The results of the ENO1 expression profiling of ovarian follicles suggest that ENO1 may play an important dual role in the progress of follicular development, where ENO1 acts as a glycolytic enzyme and also mediates apoptosis. ENO1 overexpression could make the primary culture follicle granulosa cells in vitro improve progesterone secretion. The over-expression of ENO1 protein can enhance the abilities of proliferation and migration in gastric cancer cells of AGS, which indicates that ENO1 may be an important potential tumor-marker associated with the development of gastric cancer. ENO1 and GPI can be used as markers of human sperm freezability before starting the cryopreservation procedure. The inhibition of ENO1 expression may be a novel strategy for therapy for NHLs patients, and it may be a target for drug resistance.
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TMPY-00841 | IL-13RA2 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Interleukin-13 receptor subunit alpha-2 (IL13RA2/IL-13RA2) is also known as cluster of differentiation 213A2 (CD213A2), IL-13 receptor subunit alpha-2, IL-13R subunit alpha-2, and IL-13RA2. The IL13RA2 is often overexpressed in brain tumors, making Il13ra2 one of the vaccine targets for immunotherapy of glioma. IL13RA2/IL-13RA2 is a cancer-associated receptor that is present in greater than 80% of High-Grade Astrocytomas (HGA) and has recently been recognized as a cytokine that predisposes breast cancer cells to metastasize. Expression of IL13Rα2 was rapidly lost from the surface of transduced cells grown in culture. The loss appeared to be related to ligands present in fetal bovine serum in the medium. None of the malignant glioma cell lines cultivated in vitro and tested to date exhibited the IL13Rα2 receptor. A recombinant virus (R5111) enters cells via its interaction with the IL13Rα2 receptor in a manner that cannot be differentiated from the interaction of wild-type virus with its receptors.
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TMPY-01143 | N Cadherin Protein, Human, Recombinant (His) | Human | HEK293 | ||
Cadherins are calcium-dependent cell adhesion proteins, and they preferentially interact with themselves in a homophilic manner in connecting cells. Cadherin 2 (CDH2), also known as N-Cadherin (neuronal) (NCAD), is a single-pass transmembrane protein and a cadherin containing 5 cadherin domains. N-Cadherin displays a ubiquitous expression pattern but with different expression levels between endocrine cell types. CDH2 (NCAD) has been shown to play an essential role in normal neuronal development, which is implicated in an array of processes including neuronal differentiation and migration, and axon growth and fasciculation. In addition, N-Cadherin expression was upregulated in human HSC during activation in culture, and function or expression blocking of N-Cadherin promoted apoptosis. During apoptosis, N-Cadherin was cleaved into 20-100 kDa fragments. It may provide a novel target for therapies that are directed toward intimal proliferative disorders, including restenosis and vascular bypass graft failure. N-Cadherin is associated with tumor aggressiveness and metastatic potential and may contribute to tumor progression.
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TMPY-02792 | GDNF Protein, Human, Recombinant (HEK293) | Human | HEK293 | ||
Glial cell line-derived neurotrophic factor(GDNF) is an important member of the GDNF family of ligands(GFL). The GDNF family of ligands is comprised by four neurotrophic factors: glial cell line-derived neurotrophic factor (GDNF), neurturin (NRTN), artemin (ARTN), and persephin (PSPN). It has been found that GFLs play a role in a number of biological processes including cell survival, neurite outgrowth, cell differentiation and cell migration. As the founding member, GDNF plays a key role in the promotion of the survival of dopaminergic neurons. GDNF is a highly conserved neurotrophic factor. The recombinant form of this protein also promotes the survival and differentiation of dopaminergic neurons in culture, and was able to prevent apoptosis of motor neurons induced by axotomy. GDNF also regulates kidney development and spermatogenesis, and it affects alcohol consumption. It has been shown that GDNF results in two Parkinson's disease clinical trial and in a number of animal trials. It has been taken as a potent survival factor for central motoneurons.
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TMPY-00978 | Progranulin Protein, Human, Recombinant (His) | Human | HEK293 | ||
Granulins are a family of secreted, glycosylated peptides that are cleaved from a single precursor protein with 7.5 repeats of a highly conserved 12-cysteine granulin/epithelin motif. The precursor protein, progranulin, is also called Proepithelin and PC cell-derived growth factor. Cleavage of the signal peptide produces mature granulin which can be further cleaved into a variety of active, 6 kDa peptides. These smaller cleavage products are named granulin A, granulin B, granulin C, etc. Epithelins 1 and 2 are synonymous with granulins A and B, respectively. Both the peptides and intact granulin protein regulate cell growth. However, different members of the granulin protein family may act as inhibitors, stimulators, or have dual actions on cell growth. Granulin family members are important in normal development, wound healing, and tumorigenesis. Granulins have possible cytokine-like activity. They may play a role in inflammation, wound repair, and tissue remodeling. Granulin-4 promotes proliferation of the epithelial cell line A431 in culture while granulin-3 acts as an antagonist to granulin-4, inhibiting the growth. Granulin expression inhibited Tat transactivation, and tethering experiments showed that this effect was due, at least in part, to a direct action on cyclin T1 in the absence of Tat.
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TMPY-01062 | EGF Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
EGF is the founding member of the EGF-family of proteins. Members of this protein family have highly similar structural and functional characteristics. EGF contains 9 EGF-like domains and 9 LDL-receptor class B repeats. Human EGF is a 6045-Da protein with 53 amino acid residues and three intramolecular disulfide bonds. As a low-molecular-weight polypeptide, EGF was first purified from the mouse submandibular gland, but since then it was found in many human tissues including submandibular gland, parotid gland. It can also be found in human platelets, macrophages, urine, saliva, milk, and plasma. EGF is a growth factor that stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. It results in cellular proliferation, differentiation, and survival. Salivary EGF, which seems also regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. EGF acts by binding with high affinity to epidermal growth factor receptor on the cell surface and stimulating the intrinsic protein-tyrosine kinase activity of the receptor. The tyrosine kinase activity, in turn, initiates a signal transduction cascade that results in a variety of biochemical changes within the cell - a rise in intracellular calcium levels, increased glycolysis and protein synthesis, and increases in the expression of certain genes including the gene for EGFR - that ultimately lead to DNA synthesis and cell proliferation.
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TMPY-06984 | EGF Protein, Mouse, Recombinant (Yeast) | Mouse | Yeast | ||
EGF is the founding member of the EGF-family of proteins. Members of this protein family have highly similar structural and functional characteristics. EGF contains 9 EGF-like domains and 9 LDL-receptor class B repeats. Human EGF is a 6045-Da protein with 53 amino acid residues and three intramolecular disulfide bonds. As a low-molecular-weight polypeptide, EGF was first purified from the mouse submandibular gland, but since then it was found in many human tissues including submandibular gland, parotid gland. It can also be found in human platelets, macrophages, urine, saliva, milk, and plasma. EGF is a growth factor that stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. It results in cellular proliferation, differentiation, and survival. Salivary EGF, which seems also regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. EGF acts by binding with high affinity to epidermal growth factor receptor on the cell surface and stimulating the intrinsic protein-tyrosine kinase activity of the receptor. The tyrosine kinase activity, in turn, initiates a signal transduction cascade that results in a variety of biochemical changes within the cell - a rise in intracellular calcium levels, increased glycolysis and protein synthesis, and increases in the expression of certain genes including the gene for EGFR - that ultimately lead to DNA synthesis and cell proliferation.
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TMPY-02170 | SCF Protein, Human, Recombinant (aa 1-189, His) | Human | Baculovirus-Insect Cells | ||
Similar to Kit ligand precursor (C-kit ligand), also known as Stem cell factor (SCF), Mast cell growth factor (MGF), or Hematopoietic growth factor KL. SCF/C-kit ligand is the ligand of the tyrosine-kinase receptor encoded by the KIT locus. This ligand is a pleiotropic factor that acts in utero in germ cell and neural cell development, and hematopoiesis, all believed to reflect a role in cell migration. In adults, it functions pleiotropically, while mostly noted for its continued requirement in hematopoiesis. SCF/C-kit ligand stimulates the proliferation of mast cells. This protein can augment the proliferation of both myeloid and lymphoid hematopoietic progenitors in bone marrow culture. It may act synergistically with other cytokines, probably interleukins SCF/C-kit ligand is the ligand for the tyrosine kinase receptor c-kit, which is expressed on both primitive and mature hematopoietic progenitor cells. In vitro, SCF/C-kit ligand synergizes with other growth factors, such as granulocyte colony-stimulating factor (G-CSF), granulocyte-macrophage colony-stimulating factor, and interleukin-3 to stimulate the proliferation and differentiation of cells of the lymphoid, myeloid, erythroid, and megakaryocytic lineages. In vivo, SCF/C-kit also synergizes with other growth factors and has been shown to enhance the mobilization of peripheral blood progenitor cells in combination with G-CSF. In phase I/II clinical studies administration of the combination of SCF and G-CSF resulted in a two- to threefold increase in cells that express the CD34 antigen compared with G-CSF alone.
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TMPY-02105 | SCF Protein, Mouse, Recombinant (His) | Mouse | Baculovirus-Insect Cells | ||
Similar to Kit ligand precursor (C-kit ligand), also known as Stem cell factor (SCF), Mast cell growth factor (MGF), or Hematopoietic growth factor KL. SCF/C-kit ligand is the ligand of the tyrosine-kinase receptor encoded by the KIT locus. This ligand is a pleiotropic factor that acts in utero in germ cell and neural cell development, and hematopoiesis, all believed to reflect a role in cell migration. In adults, it functions pleiotropically, while mostly noted for its continued requirement in hematopoiesis. SCF/C-kit ligand stimulates the proliferation of mast cells. This protein can augment the proliferation of both myeloid and lymphoid hematopoietic progenitors in bone marrow culture. It may act synergistically with other cytokines, probably interleukins SCF/C-kit ligand is the ligand for the tyrosine kinase receptor c-kit, which is expressed on both primitive and mature hematopoietic progenitor cells. In vitro, SCF/C-kit ligand synergizes with other growth factors, such as granulocyte colony-stimulating factor (G-CSF), granulocyte-macrophage colony-stimulating factor, and interleukin-3 to stimulate the proliferation and differentiation of cells of the lymphoid, myeloid, erythroid, and megakaryocytic lineages. In vivo, SCF/C-kit also synergizes with other growth factors and has been shown to enhance the mobilization of peripheral blood progenitor cells in combination with G-CSF. In phase I/II clinical studies administration of the combination of SCF and G-CSF resulted in a two- to threefold increase in cells that express the CD34 antigen compared with G-CSF alone.
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TMPY-01560 | EGF Protein, Human, Recombinant | Human | E. coli | ||
EGF is the founding member of the EGF-family of proteins. Members of this protein family have highly similar structural and functional characteristics. EGF contains 9 EGF-like domains and 9 LDL-receptor class B repeats. Human EGF is a 6045-Da protein with 53 amino acid residues and three intramolecular disulfide bonds. As a low-molecular-weight polypeptide, EGF was first purified from the mouse submandibular gland, but since then it was found in many human tissues including submandibular gland, parotid gland. It can also be found in human platelets, macrophages, urine, saliva, milk, and plasma. EGF is a growth factor that stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. It results in cellular proliferation, differentiation, and survival. Salivary EGF, which seems also regulated by dietary inorganic iodine, also plays an important physiological role in the maintenance of oro-esophageal and gastric tissue integrity. EGF acts by binding with high affinity to epidermal growth factor receptor on the cell surface and stimulating the intrinsic protein-tyrosine kinase activity of the receptor. The tyrosine kinase activity, in turn, initiates a signal transduction cascade that results in a variety of biochemical changes within the cell - a rise in intracellular calcium levels, increased glycolysis and protein synthesis, and increases in the expression of certain genes including the gene for EGFR - that ultimately lead to DNA synthesis and cell proliferation.
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TMPK-00842 | CD21 Protein, Human, Recombinant (His) | Human | HEK293 | ||
CD21 mRNA expression, an EBV-entry receptor, was transiently detected in NK cells after exosome treatment, and levels decreased after further culture. CD21 protein expression was also transiently transferred to NK cells after co-culture with an EBV-positive Burkitt lymphoma cell line (Raji) via trogocytosis. However, EBV did not infect NK cells through CD21-mediated trogocytosis.
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TMPH-00252 | Bovine coronavirus (strain Mebus) Protein I (His) | BCoV | E. coli | ||
Structural protein that is not essential for the viral replication either in tissue culture or in its natural host.
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TMPH-00253 | Bovine coronavirus (strain 98TXSF-110-LUN) Protein I (His) | BCoV | E. coli | ||
Structural protein that is not essential for the viral replication either in tissue culture or in its natural host.
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TMPH-00255 | Bovine coronavirus (strain LSU-94LSS-051) Protein I (His) | BCoV | E. coli | ||
Structural protein that is not essential for the viral replication either in tissue culture or in its natural host.
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TMPH-00784 | Intimin Protein, Hafnia alvei, Recombinant (His & SUMO) | Hafnia alvei | E. coli | ||
Necessary for the production of attaching and effacing lesions on tissue culture cells.
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TMPJ-00039 | FGF-2 Protein, Human, Recombinant (K128N) | Human | E. coli | ||
Fibroblast growth factors (FGF) are a family of heparin-binding secreted proteins that stimulate cell proliferation and differentiation in a wide variety of tissues. FGFs play important roles in diverse biological functions both in vivo and in vitro, including mitogenesis, cellular migration, differentiation, angiogenesis, and wound healing. Human embryonic stem cell (hESC) cultures require FGF basic (also known as FGF-2 or bFGF) in cell culture media to remain in an undifferentiated and pluripotent state. Thermostable FGF basic was engineered for enhanced stability in culture media, without modification of its biological function. FGF basic is a required component of stem cell culture media for maintaining cells in an undifferentiated state. Because FGF basic is unstable, daily media changes are needed. The thermostable FGF basic that supports a 2-day media change schedule, so no media changes are required over a weekend. This thermostable FGF basic was more stable than FGF basic in biochemical studies, and maintained cell growth, pluripotency and differentiation potential with a 2-day feeding schedule.
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TMPH-00256 | Bovine coronavirus (strain LY-138) Protein I (His) | BCoV | E. coli | ||
Structural protein that is not essential for the viral replication either in tissue culture or in its natural host.
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TMPH-00254 | Bovine coronavirus (strain 98TXSF-110-ENT) Protein I (His) | BCoV | E. coli | ||
Structural protein that is not essential for the viral replication either in tissue culture or in its natural host.
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TMPJ-00040 | FGF-2 Protein, Human,Recombinant (Q65I, C96S, N111G) | Human | E. coli | ||
Fibroblast growth factors (FGF) are a family of heparin-binding secreted proteins that stimulate cell proliferation and differentiation in a wide variety of tissues. FGFs play important roles in diverse biological functions both in vivo and in vitro, including mitogenesis, cellular migration, differentiation, angiogenesis, and wound healing. Human embryonic stem cell (hESC) cultures require FGF basic (also known as FGF-2 or bFGF) in cell culture media to remain in an undifferentiated and pluripotent state. Thermostable FGF basic was engineered for enhanced stability in culture media, without modification of its biological function. FGF basic is a required component of stem cell culture media for maintaining cells in an undifferentiated state. Because FGF basic is unstable, daily media changes are needed. The thermostable FGF basic that supports a 2-day media change schedule, so no media changes are required over a weekend. This thermostable FGF basic was more stable than FGF basic in biochemical studies, and maintained cell growth, pluripotency and differentiation potential with a 2-day feeding schedule.
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TMPH-03247 | Artemin Protein, Rat, Recombinant (His & Myc) | Rat | E. coli | ||
Ligand for the GFR-alpha-3-RET receptor complex but can also activate the GFR-alpha-1-RET receptor complex. Supports the survival of sensory and sympathetic peripheral neurons in culture and also supports the survival of dopaminergic neurons of the ventral mid-brain. Strong attractant of gut hematopoietic cells thus promoting the formation Peyer's patch-like structures, a major component of the gut-associated lymphoid tissue.
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TMPK-01202 | CD93/C1qR1 Protein, Human, Recombinant (His&Avi), Biotinylated | Human | HEK293 | ||
CD93 has been shown critical roles in inflammatory and immune diseases. CD93 silencing increased IL-6 and TSLP, but not IL-33 levels in culture supernatants. HDM-induced asthma mice showed significant airway hyperresponsiveness and inflammation with Th2 cytokine activation, along with decreased CD93 expression in bronchial epithelial cells and lung homogenates but increased serum CD93 levels.
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TMPJ-00811 | IGFBP-1 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Insulin-like growth factor-binding protein 1 (IGFBP1) is encoded by 259 amino acid (aa) with 25 aa residue signal peptide that is processed to generate the 234 aa residue mature protein. IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Promotes cell migration. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
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TMPY-03185 | METRN Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
METRN (Meteorin, Glial Cell Differentiation Regulator) is a Protein Coding gene. The encoded protein belongs to the meteorin family. It is broadly expressed in the brain, kidney, and other tissues. Meteorin is a novel secreted protein that is expressed in undifferentiated neural progenitors and the astrocyte lineage, including radial glia. It plays important role in the differentiation of glial cells and also in axonal network formation during neurogenesis. Meteorin selectively promoted astrocyte formation from mouse cerebrocortical neurospheres in differentiation culture, whereas it induced cerebellar astrocytes to become radial glia. Meteorin also induced axonal extension in small and intermediate neurons of sensory ganglia by activating nearby satellite glia.
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TMPJ-00164 | IGFBP-5 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | Human Cells | ||
Insulin-Like Growth Factor-Binding Protein 5 (IGFBP-5) is a secreted protein that belongs to the insulin-like growth factor (IGF) binding proteins superfamily. Members of this family prolong the half-life of the IGFs. They have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. IGFBP-5 contains one IGFBP N-terminal domain and one thyroglobulin type-1 domain. IGFBP-5 is expressed by fibroblasts, myoblasts and Osteosarcoma. It is also present at lower levels in liver, kidney, and brain.
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TMPY-02441 | alanyl-tRNA synthetase Protein, Mouse, Recombinant (His) | Mouse | Baculovirus-Insect Cells | ||
Alanyl-tRNA synthetase (AARS) belongs to the family of ligases, specifically those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. This enzyme participates in alanine and aspartate metabolism and aminoacyl-tRNA biosynthesis. Alanyl-tRNA synthetase (AlaRS) catalyzes synthesis of Ala-tRNA (Ala) and hydrolysis of mis-acylated Ser- and Gly-tRNA (Ala) at 2 different catalytic sites. Their role is not confined to catalyze the attachment of amino acids to transfer RNAs and thereby establish the rules of genetic code by virtue of matching the nucleotide triplet of anticodon with cognate amino acid. Under apoptotic conditions in cell culture, the full-length enzyme is secreted, and the two cytokine activities can be generated by leukocyte elastase, an extracellular protease. Secretion of this tRNA synthetase may contribute to apoptosis both by arresting translation and producing needed cytokines. This protein could be an attractive target of drugs against bacterial, fungal and parasitic infections.
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TMPY-03821 | IL-13RA2 Protein, Canine, Recombinant (hFc) | Canine | HEK293 | ||
Interleukin-13 receptor subunit alpha-2 (IL13RA2/IL-13RA2) is also known as cluster of differentiation 213A2 (CD213A2), IL-13 receptor subunit alpha-2, IL-13R subunit alpha-2, and IL-13RA2. The IL13RA2 is often overexpressed in brain tumors, making Il13ra2 one of the vaccine targets for immunotherapy of glioma. IL13RA2/IL-13RA2 is a cancer-associated receptor that is present in greater than 80% of High-Grade Astrocytomas (HGA) and has recently been recognized as a cytokine that predisposes breast cancer cells to metastasize. Expression of IL13Rα2 was rapidly lost from the surface of transduced cells grown in culture. The loss appeared to be related to ligands present in fetal bovine serum in the medium. None of the malignant glioma cell lines cultivated in vitro and tested to date exhibited the IL13Rα2 receptor. A recombinant virus (R5111) enters cells via its interaction with the IL13Rα2 receptor in a manner that cannot be differentiated from the interaction of wild-type virus with its receptors.
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TMPJ-01082 | IGFBP-5 Protein, Mouse, Recombinant (His) | Mouse | Human Cells | ||
Mouse Insulin-like growth factor-binding protein 5(IGFBP-5) belongs to the superfamily of insulin-like growth factor (IGF) binding proteins. It contains 1 IGFBP N-terminal domain and 1 thyroglobulin type-1 domain. Mouse IGFBP-5 shows 97% aa sequence identity with those of human and rat IGFBP-5. It is expressed mostly in kidney, uterus and gastrocnemius muscle. It also expressed by fibroblasts, myoblasts and osteoblasts, making it the predominant IGFBP found in bone extracts. IGFBP-5 has a strong affinity for hydroxyapatite, allowing it to bind to bone cells. When bound to extracelluar matrix, IGFBP-5 is protected from proteolysis and potentiates IGF activity, but when it is soluble, IGFBP-5 is cleaved to a biologically inactive 21 kDa fragment. IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors.
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TMPY-00080 | IGFBP-1 Protein, Canine, Recombinant (His) | Canine | HEK293 | ||
IGFBP1, also known as IGFBP-1 and insulin-like growth factor-binding protein 1, is a member of the insulin-like growth factor-binding protein family. IGF binding proteins (IGFBPs) are proteins of 24 to 45 kDa. All six IGFBPs share 50% homology and have binding affinities for IGF-I and IGF-II at the same order of magnitude as the ligands have for the IGF-IR. IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth-promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. IGFBP1 has an IGFBP domain and a thyroglobulin type-I domain. It binds both insulin-like growth factors (IGFs) I and II and circulates in the plasma. The binding of this protein prolongs the half-life of the IGFs and alters their interaction with cell surface receptors.
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TMPY-00842 | IL-13RA2 Protein, Human, Recombinant (His & hFc) | Human | HEK293 | ||
Interleukin-13 receptor subunit alpha-2 (IL13RA2/IL-13RA2) is also known as cluster of differentiation 213A2 (CD213A2), IL-13 receptor subunit alpha-2, IL-13R subunit alpha-2, and IL-13RA2. The IL13RA2 is often overexpressed in brain tumors, making Il13ra2 one of the vaccine targets for immunotherapy of glioma. IL13RA2/IL-13RA2 is a cancer-associated receptor that is present in greater than 80% of High-Grade Astrocytomas (HGA) and has recently been recognized as a cytokine that predisposes breast cancer cells to metastasize. Expression of IL13Rα2 was rapidly lost from the surface of transduced cells grown in culture. The loss appeared to be related to ligands present in fetal bovine serum in the medium. None of the malignant glioma cell lines cultivated in vitro and tested to date exhibited the IL13Rα2 receptor. A recombinant virus (R5111) enters cells via its interaction with the IL13Rα2 receptor in a manner that cannot be differentiated from the interaction of wild-type virus with its receptors.
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TMPY-05305 | alanyl-tRNA synthetase Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
Alanyl-tRNA synthetase (AARS) belongs to the family of ligases, specifically those forming carbon-oxygen bonds in aminoacyl-tRNA and related compounds. This enzyme participates in alanine and aspartate metabolism and aminoacyl-tRNA biosynthesis. Alanyl-tRNA synthetase (AlaRS) catalyzes synthesis of Ala-tRNA (Ala) and hydrolysis of mis-acylated Ser- and Gly-tRNA (Ala) at 2 different catalytic sites. Their role is not confined to catalyze the attachment of amino acids to transfer RNAs and thereby establish the rules of genetic code by virtue of matching the nucleotide triplet of anticodon with cognate amino acid. Under apoptotic conditions in cell culture, the full-length enzyme is secreted, and the two cytokine activities can be generated by leukocyte elastase, an extracellular protease. Secretion of this tRNA synthetase may contribute to apoptosis both by arresting translation and producing needed cytokines. This protein could be an attractive target of drugs against bacterial, fungal and parasitic infections.
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TMPY-02920 | IGFBP-1 Protein, Rhesus, Recombinant (His) | Rhesus | HEK293 | ||
IGFBP1, also known as IGFBP-1 and insulin-like growth factor-binding protein 1, is a member of the insulin-like growth factor-binding protein family. IGF binding proteins (IGFBPs) are proteins of 24 to 45 kDa. All six IGFBPs share 50% homology and have binding affinities for IGF-I and IGF-II at the same order of magnitude as the ligands have for the IGF-IR. IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth-promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. IGFBP1 has an IGFBP domain and a thyroglobulin type-I domain. It binds both insulin-like growth factors (IGFs) I and II and circulates in the plasma. The binding of this protein prolongs the half-life of the IGFs and alters their interaction with cell surface receptors.
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TMPY-05783 | IL-13RA2 Protein, Mouse, Recombinant (mFc) | Mouse | HEK293 | ||
Interleukin-13 receptor subunit alpha-2 (IL13RA2/IL-13RA2) is also known as cluster of differentiation 213A2 (CD213A2), IL-13 receptor subunit alpha-2, IL-13R subunit alpha-2, and IL-13RA2. The IL13RA2 is often overexpressed in brain tumors, making Il13ra2 one of the vaccine targets for immunotherapy of glioma. IL13RA2/IL-13RA2 is a cancer-associated receptor that is present in greater than 80% of High-Grade Astrocytomas (HGA) and has recently been recognized as a cytokine that predisposes breast cancer cells to metastasize. Expression of IL13Rα2 was rapidly lost from the surface of transduced cells grown in culture. The loss appeared to be related to ligands present in fetal bovine serum in the medium. None of the malignant glioma cell lines cultivated in vitro and tested to date exhibited the IL13Rα2 receptor. A recombinant virus (R5111) enters cells via its interaction with the IL13Rα2 receptor in a manner that cannot be differentiated from the interaction of wild-type virus with its receptors.
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TMPY-01018 | IL-13RA2 Protein, Mouse, Recombinant (His & hFc) | Mouse | HEK293 | ||
Interleukin-13 receptor subunit alpha-2 (IL13RA2/IL-13RA2) is also known as cluster of differentiation 213A2 (CD213A2), IL-13 receptor subunit alpha-2, IL-13R subunit alpha-2, and IL-13RA2. The IL13RA2 is often overexpressed in brain tumors, making Il13ra2 one of the vaccine targets for immunotherapy of glioma. IL13RA2/IL-13RA2 is a cancer-associated receptor that is present in greater than 80% of High-Grade Astrocytomas (HGA) and has recently been recognized as a cytokine that predisposes breast cancer cells to metastasize. Expression of IL13Rα2 was rapidly lost from the surface of transduced cells grown in culture. The loss appeared to be related to ligands present in fetal bovine serum in the medium. None of the malignant glioma cell lines cultivated in vitro and tested to date exhibited the IL13Rα2 receptor. A recombinant virus (R5111) enters cells via its interaction with the IL13Rα2 receptor in a manner that cannot be differentiated from the interaction of wild-type virus with its receptors.
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TMPY-03692 | N Cadherin Protein, Human, Recombinant (His & hFc) | Human | HEK293 | ||
Cadherins are calcium-dependent cell adhesion proteins, and they preferentially interact with themselves in a homophilic manner in connecting cells. Cadherin 2 (CDH2), also known as N-Cadherin (neuronal) (NCAD), is a single-pass transmembrane protein and a cadherin containing 5 cadherin domains. N-Cadherin displays a ubiquitous expression pattern but with different expression levels between endocrine cell types. CDH2 (NCAD) has been shown to play an essential role in normal neuronal development, which is implicated in an array of processes including neuronal differentiation and migration, and axon growth and fasciculation. In addition, N-Cadherin expression was upregulated in human HSC during activation in culture, and function or expression blocking of N-Cadherin promoted apoptosis. During apoptosis, N-Cadherin was cleaved into 20-100 kDa fragments. It may provide a novel target for therapies that are directed toward intimal proliferative disorders, including restenosis and vascular bypass graft failure. N-Cadherin is associated with tumor aggressiveness and metastatic potential and may contribute to tumor progression.
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TMPY-06970 | GDNF Protein, Human, Recombinant | Human | E. coli | ||
Glial cell line-derived neurotrophic factor(GDNF) is an important member of the GDNF family of ligands(GFL). The GDNF family of ligands is comprised by four neurotrophic factors: glial cell line-derived neurotrophic factor (GDNF), neurturin (NRTN), artemin (ARTN), and persephin (PSPN). It has been found that GFLs play a role in a number of biological processes including cell survival, neurite outgrowth, cell differentiation and cell migration. As the founding member, GDNF plays a key role in the promotion of the survival of dopaminergic neurons. GDNF is a highly conserved neurotrophic factor. The recombinant form of this protein also promotes the survival and differentiation of dopaminergic neurons in culture, and was able to prevent apoptosis of motor neurons induced by axotomy. GDNF also regulates kidney development and spermatogenesis, and it affects alcohol consumption. It has been shown that GDNF results in two Parkinson's disease clinical trial and in a number of animal trials. It has been taken as a potent survival factor for central motoneurons.
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TMPY-03772 | IL-13RA2 Protein, Canine, Recombinant (His) | Canine | HEK293 | ||
Interleukin-13 receptor subunit alpha-2 (IL13RA2/IL-13RA2) is also known as cluster of differentiation 213A2 (CD213A2), IL-13 receptor subunit alpha-2, IL-13R subunit alpha-2, and IL-13RA2. The IL13RA2 is often overexpressed in brain tumors, making Il13ra2 one of the vaccine targets for immunotherapy of glioma. IL13RA2/IL-13RA2 is a cancer-associated receptor that is present in greater than 80% of High-Grade Astrocytomas (HGA) and has recently been recognized as a cytokine that predisposes breast cancer cells to metastasize. Expression of IL13Rα2 was rapidly lost from the surface of transduced cells grown in culture. The loss appeared to be related to ligands present in fetal bovine serum in the medium. None of the malignant glioma cell lines cultivated in vitro and tested to date exhibited the IL13Rα2 receptor. A recombinant virus (R5111) enters cells via its interaction with the IL13Rα2 receptor in a manner that cannot be differentiated from the interaction of wild-type virus with its receptors.
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TMPY-01172 | CDH12 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Classic Cadherins represent a family of calcium-dependent homophilic cell-cell adhesion molecules. They confer strong adhesiveness to animal cells when they are anchored to the actin cytoskeleton via their cytoplasmic binding partners, catenins. The cadherin/catenin adhesion system plays key roles in the morphogenesis and function of the vertebrate and invertebrate nervous systems. Furthermore, this system is involved in synaptic plasticity. Recent studies on the role of individual cadherin subtypes at synapses indicate that individual cadherin subtypes play their own unique role to regulate synaptic activities. Type II (atypical) cadherins are defined based on their lack of an HAV cell adhesion recognition sequence specific to type I cadherins. It has been observed that cells containing a specific cadherin subtype tend to cluster together to the exclusion of other types, both in cell culture and during development. Cadherin-12 also known as CDH12, is a type II classical cadherin from the cadherin superfamily of integral membrane proteins that mediate calcium-dependent cell-cell adhesion. Cadherin-12 appears to be expressed specifically in the brain and its temporal pattern of expression would be consistent with a role during a critical period of neuronal development, perhaps specifically during synaptogenesis.
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TMPY-06506 | IL-13RA2 Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
Interleukin-13 receptor subunit alpha-2 (IL13RA2/IL-13RA2) is also known as cluster of differentiation 213A2 (CD213A2), IL-13 receptor subunit alpha-2, IL-13R subunit alpha-2, and IL-13RA2. The IL13RA2 is often overexpressed in brain tumors, making Il13ra2 one of the vaccine targets for immunotherapy of glioma. IL13RA2/IL-13RA2 is a cancer-associated receptor that is present in greater than 80% of High-Grade Astrocytomas (HGA) and has recently been recognized as a cytokine that predisposes breast cancer cells to metastasize. Expression of IL13Rα2 was rapidly lost from the surface of transduced cells grown in culture. The loss appeared to be related to ligands present in fetal bovine serum in the medium. None of the malignant glioma cell lines cultivated in vitro and tested to date exhibited the IL13Rα2 receptor. A recombinant virus (R5111) enters cells via its interaction with the IL13Rα2 receptor in a manner that cannot be differentiated from the interaction of wild-type virus with its receptors.
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TMPY-05334 | IL-13RA2 Protein, Human, Recombinant (His), Biotinylated | Human | HEK293 | ||
Interleukin-13 receptor subunit alpha-2 (IL13RA2/IL-13RA2) is also known as cluster of differentiation 213A2 (CD213A2), IL-13 receptor subunit alpha-2, IL-13R subunit alpha-2, and IL-13RA2. The IL13RA2 is often overexpressed in brain tumors, making Il13ra2 one of the vaccine targets for immunotherapy of glioma. IL13RA2/IL-13RA2 is a cancer-associated receptor that is present in greater than 80% of High-Grade Astrocytomas (HGA) and has recently been recognized as a cytokine that predisposes breast cancer cells to metastasize. Expression of IL13Rα2 was rapidly lost from the surface of transduced cells grown in culture. The loss appeared to be related to ligands present in fetal bovine serum in the medium. None of the malignant glioma cell lines cultivated in vitro and tested to date exhibited the IL13Rα2 receptor. A recombinant virus (R5111) enters cells via its interaction with the IL13Rα2 receptor in a manner that cannot be differentiated from the interaction of wild-type virus with its receptors.
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TMPH-02346 | Influenza A H1N1 (strain A/USA:Iowa/1943) Matrix protein 1 (His & Myc) | H1N1 | E. coli | ||
Plays critical roles in virus replication, from virus entry and uncoating to assembly and budding of the virus particle. M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit viral transcription. Interaction of viral NEP with M1-RNP is thought to promote nuclear export of the complex, which is targeted to the virion assembly site at the apical plasma membrane in polarized epithelial cells. Interactions with NA and HA may bring M1, a non-raft-associated protein, into lipid rafts. Forms a continuous shell on the inner side of the lipid bilayer in virion, where it binds the RNP. During virus entry into cell, the M2 ion channel acidifies the internal virion core, inducing M1 dissociation from the RNP. M1-free RNPs are transported to the nucleus, where viral transcription and replication can take place.; Determines the virion's shape: spherical or filamentous. Clinical isolates of influenza are characterized by the presence of significant proportion of filamentous virions, whereas after multiple passage on eggs or cell culture, virions have only spherical morphology. Filamentous virions are thought to be important to infect neighboring cells, and spherical virions more suited to spread through aerosol between hosts organisms.
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TMPY-01800 | NEGR1 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Neuronal Growth Regulator 1, NEGR1, also known as neurotractin, or KILON, belongs to the immunoglobulin superfamily, IgLON family. This GPI-linked cell surface glycoprotein NEGR1 is composed of three Ig-like domains and belongs to the IgLON subgroup of neural IgSF members. It is expressed in two isoforms with apparent molecular masses of 50 and 37 kD, termed L-form and S-form, respectively. NEGR1/Neurotractin participates in the regulation of neurite outgrowth in the developing brain and is expressed on the neurites of primary hippocampal neurons. Neurotractin/KILON is a trans-neural growth-promoting factor for outgrowing axons following hippocampal denervation. KILON (kindred of IgLON) and opioid-binding cell adhesion molecule, together with the limbic system-associated membrane protein and neurotrophin, belong to the IgLON subgroup of immunoglobulin superfamily. The alteration of the modulatory function of KILON/NEGR1 for the number of dendritic synapses concomitant with changes in its localization and detergent solubility during neuronal culture development. In addition to its reported role in the brain, NEGR1 is also expressed in subcutaneous adipose tissue and acts as a central 'hub' in an obesity-related transcript network.
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TMPY-02997 | IL-13RA2 Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
Interleukin-13 receptor subunit alpha-2 (IL13RA2/IL-13RA2) is also known as cluster of differentiation 213A2 (CD213A2), IL-13 receptor subunit alpha-2, IL-13R subunit alpha-2, and IL-13RA2. The IL13RA2 is often overexpressed in brain tumors, making Il13ra2 one of the vaccine targets for immunotherapy of glioma. IL13RA2/IL-13RA2 is a cancer-associated receptor that is present in greater than 80% of High-Grade Astrocytomas (HGA) and has recently been recognized as a cytokine that predisposes breast cancer cells to metastasize. Expression of IL13Rα2 was rapidly lost from the surface of transduced cells grown in culture. The loss appeared to be related to ligands present in fetal bovine serum in the medium. None of the malignant glioma cell lines cultivated in vitro and tested to date exhibited the IL13Rα2 receptor. A recombinant virus (R5111) enters cells via its interaction with the IL13Rα2 receptor in a manner that cannot be differentiated from the interaction of wild-type virus with its receptors.
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TMPY-00073 | ENO1 Protein, Rat, Recombinant (His) | Rat | E. coli | ||
The ENO1 gene encodes a multifunctional enzyme that has been identified as a key component of the glycolytic pathway. ENO1 overexpression and post-translational modifications could be of diagnostic and prognostic value in many cancer types. The results of the ENO1 expression profiling of ovarian follicles suggest that ENO1 may play an important dual role in the progress of follicular development, where ENO1 acts as a glycolytic enzyme and also mediates apoptosis. ENO1 overexpression could make the primary culture follicle granulosa cells in vitro improve progesterone secretion. The over-expression of ENO1 protein can enhance the abilities of proliferation and migration in gastric cancer cells of AGS, which indicates that ENO1 may be an important potential tumor-marker associated with the development of gastric cancer. ENO1 and GPI can be used as markers of human sperm freezability before starting the cryopreservation procedure. The inhibition of ENO1 expression may be a novel strategy for therapy for NHLs patients, and it may be a target for drug resistance.
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TMPY-02911 | GDNF Protein, Rat, Recombinant (His) | Rat | Baculovirus-Insect Cells | ||
Glial cell line-derived neurotrophic factor(GDNF) is an important member of the GDNF family of ligands(GFL). The GDNF family of ligands is comprised by four neurotrophic factors: glial cell line-derived neurotrophic factor (GDNF), neurturin (NRTN), artemin (ARTN), and persephin (PSPN). It has been found that GFLs play a role in a number of biological processes including cell survival, neurite outgrowth, cell differentiation and cell migration. As the founding member, GDNF plays a key role in the promotion of the survival of dopaminergic neurons. GDNF is a highly conserved neurotrophic factor. The recombinant form of this protein also promotes the survival and differentiation of dopaminergic neurons in culture, and was able to prevent apoptosis of motor neurons induced by axotomy. GDNF also regulates kidney development and spermatogenesis, and it affects alcohol consumption. It has been shown that GDNF results in two Parkinson's disease clinical trial and in a number of animal trials. It has been taken as a potent survival factor for central motoneurons.
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TMPY-04535 | GDNF Protein, Canine, Recombinant (hFc) | Canine | HEK293 | ||
Glial cell line-derived neurotrophic factor(GDNF) is an important member of the GDNF family of ligands(GFL). The GDNF family of ligands is comprised by four neurotrophic factors: glial cell line-derived neurotrophic factor (GDNF), neurturin (NRTN), artemin (ARTN), and persephin (PSPN). It has been found that GFLs play a role in a number of biological processes including cell survival, neurite outgrowth, cell differentiation and cell migration. As the founding member, GDNF plays a key role in the promotion of the survival of dopaminergic neurons. GDNF is a highly conserved neurotrophic factor. The recombinant form of this protein also promotes the survival and differentiation of dopaminergic neurons in culture, and was able to prevent apoptosis of motor neurons induced by axotomy. GDNF also regulates kidney development and spermatogenesis, and it affects alcohol consumption. It has been shown that GDNF results in two Parkinson's disease clinical trial and in a number of animal trials. It has been taken as a potent survival factor for central motoneurons.
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TMPY-03703 | N Cadherin Protein, Mouse, Recombinant | Mouse | HEK293 | ||
Cadherins are calcium-dependent cell adhesion proteins, and they preferentially interact with themselves in a homophilic manner in connecting cells. Cadherin 2 (CDH2), also known as N-Cadherin (neuronal) (NCAD), is a single-pass transmembrane protein and a cadherin containing 5 cadherin domains. N-Cadherin displays a ubiquitous expression pattern but with different expression levels between endocrine cell types. CDH2 (NCAD) has been shown to play an essential role in normal neuronal development, which is implicated in an array of processes including neuronal differentiation and migration, and axon growth and fasciculation. In addition, N-Cadherin expression was upregulated in human HSC during activation in culture, and function or expression blocking of N-Cadherin promoted apoptosis. During apoptosis, N-Cadherin was cleaved into 20-100 kDa fragments. It may provide a novel target for therapies that are directed toward intimal proliferative disorders, including restenosis and vascular bypass graft failure. N-Cadherin is associated with tumor aggressiveness and metastatic potential and may contribute to tumor progression.
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