目录号 | 产品详情 | 靶点 | |
---|---|---|---|
T9282 | Others | ||
DBCO-(CH2)3-Acid 是一种用于抗体-药物偶联物的 Click Chemistry 中间体,可用以合成 ADC linker。 | |||
T14184 | Others PROTAC Linker | ||
Alkynyl myristic acid (13-Tetradecyn-1-oic acid) 是一种基于烷基链的 PROTAC 接头。 | |||
T6873 | Others Endogenous Metabolite Antibacterial | ||
Lauric Acid (Dodecylic acid) 是一种有抗菌活性的中链脂肪酸,对P. acnes,S.aureus 和S. epidermidis 的 EC50值分别为 2,6,4 μg/mL。 | |||
T19124 | Endogenous Metabolite | ||
3-Oxocholic acid(3-Ketocholic acid) 是胆汁酸的代谢产物,也是产气荚膜梭菌在肠道中由胆汁降解的主要产物。33-Oxocholic acid 是一种主要存在于哺乳动物的胆汁中类固醇酸。 | |||
T3379 | GluR iGluR | ||
Decanoic Acid (Caprynic acid) 是中链甘油三酯中的成分,是非竞争性和可透过血脑屏障的 AMPA 受体抑制剂,具有抗癫痫作用。 | |||
T30355 | Others | ||
Benzeneboronic acid (Phenylboronic acid) 是一种用于Mizuroki Heck 和Suzuki Miyaura 偶联反应的硼酸。 | |||
T3391 | FAK Autophagy | ||
Corosolic acid (Colosic acid) 是从大花紫薇中提取的一种天然产物,具有抗肿瘤活性。 | |||
T5291 | Others | ||
Malonic acid (propanedioic acid) 是竞争性抑制剂的典型例子:它作用于呼吸电子传递链中的琥珀酸脱氢酶(复合物 II)。发现丙二酸与丙二酰辅酶A 脱羧酶缺乏有关,这是一种先天性代谢错误。 | |||
T2877 | Others Endogenous Metabolite | ||
Mucic Acid (Tetrahydroxyadipic acid) 是内源性代谢产物的一种。 | |||
T2P2923 | Phosphatase Endogenous Metabolite | ||
Stearic acid (Cetylacetic acid) 是长链饱和脂肪酸,存在于许多动植物油脂中。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
---|---|---|---|---|---|
TMPY-02131 | Acid Phosphatase/ACP1 Protein, Human, Recombinant (GST) | Human | E. coli | ||
The low molecular weight phosphotyrosine phosphatase (LMW-PTP), also known as Acid phosphatase 1 (ACP1), belongs to the low molecular weight phosphotyrosine protein phosphatase family are involved in the regulation of important physiological functions, including stress resistance and synthesis of the polysaccharide capsule. ACP1/LMW-PTP is an enzyme involved in platelet-derived growth factor-induced mitogenesis and cytoskeleton rearrangement. LMW-PTP is able to specifically bind and dephosphorylate activated PDGF receptor, thus modulating PDGF-induced mitogenesis. In vitro, LMW-PTP was found to efficiently dephosphorylate activated FcgammaRIIA and LAT, but not Syk or phospholipase Cgamma2. The overexpression of LMW-PTP inhibited activation of Syk downstream of FcgammaRIIA and reduced intracellular Ca(2+) mobilization. It been demonstrated that LMW-PTP is responsible for FcgammaRIIA dephosphorylation, and is implicated in the down-regulation of cell activation mediated by this ITAM-bearing immunoreceptor. In addition, ACP1 is a highly polymorphic phosphatase that is especially abundant in the central nervous system and is known to be involved in several signal transduction pathways.
|
|||||
TMPY-02155 | Prostatic Acid Phosphatase Protein, Human, Recombinant (His) | Human | HEK293 | ||
Prostatic acid phosphatase (PAP, or ACPP), also known as prostatic specific acid phosphatase (PSAP), is an enzyme produced by the prostate. As a non-specific phosphomonoesterase, Prostatic acid phosphatase is synthesized and secreted into seminal plasma under androgenic control. The enzyme is a dimer of molecular weight around 100 kDa. Prostatic acid phosphatase is a clinically important protein for its relevance as a biomarker of prostate carcinoma. Furthermore, it has a potential role in fertilization. The major action of PAP is to dephosphorylate macromolecules with the help of catalytic residues (His(12) and Asp(258)) that are located in the cleft between two domains. Cellular prostatic acid phosphatase (cPAcP), an authentic tyrosine phosphatase, is proposed to function as a negative growth regulator of prostate cancer (PCa) cells in part through its dephosphorylation of ErbB-2. cPAcP functions as a neutral protein tyrosine phosphatase (PTP) in prostate cancer cells and dephosphorylates HER-2/ErbB-2/Neu (HER-2: human epidermal growth factor receptor-2) at the phosphotyrosine (p-Tyr) residues. Injection of the secretory isoform of PAP has potent antinociceptive effects in mouse models of chronic pain. This enzyme exhibits ecto-5'-nucleotidase activity, is widely distributed, and implicated in the formation of chronic pain. Additionally, PAP could be a target molecule in specific immunotherapy for patients with nonprostate adenocarcinomas including colon and gastric cancers.
|
|||||
TMPY-02585 | Acid sphingomyelinase/SMPD1 Protein, Mouse, Recombinant (His) | Mouse | Baculovirus-Insect Cells | ||
Sphingomyelin phosphodiesterase 1 (SMPD1) , also known as ASM ( acid sphingomyelinase ), is a member of the acid sphingomyelinase family of enzymes. Three isoforms have been identified, isoform 1 is 631 amino acids (aa) in length as the pro form, while Isoform 2 and isoform 3 have lost catalytic activity. The active SMPD1 isoform 1 contains one saposin B-type domain that likely interacts with sphingomyelin, and a catalytic region. Human SMPD1 is 86% aa identical to mouse SMPD1. SMPD1 is a monomeric lysosomal enzyme that converts sphingomyelin (a plasma membrane lipid ) into ceramide through the removal of phosphorylcholine. This generates second messenger components that participate in signal transduction. Defects in SMPD1 are the cause of Niemann-Pick disease type A (NPA) and type B (NPB), also known as Niemann-Pick disease classical infantile form and Niemann-Pick disease visceral form. Niemann-Pick disease is a clinically and genetically heterogeneous recessive disorder. NPB has little if any neurologic involvement and patients may survive into adulthood.
|
|||||
TMPY-02672 | Prostatic Acid Phosphatase Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Prostatic acid phosphatase (PAP, or ACPP), also known as prostatic specific acid phosphatase (PSAP), is an enzyme produced by the prostate. As a non-specific phosphomonoesterase, Prostatic acid phosphatase is synthesized and secreted into seminal plasma under androgenic control. The enzyme is a dimer of molecular weight around 100 kDa. Prostatic acid phosphatase is a clinically important protein for its relevance as a biomarker of prostate carcinoma. Furthermore, it has a potential role in fertilization. The major action of PAP is to dephosphorylate macromolecules with the help of catalytic residues (His(12) and Asp(258)) that are located in the cleft between two domains. Cellular prostatic acid phosphatase (cPAcP), an authentic tyrosine phosphatase, is proposed to function as a negative growth regulator of prostate cancer (PCa) cells in part through its dephosphorylation of ErbB-2. cPAcP functions as a neutral protein tyrosine phosphatase (PTP) in prostate cancer cells and dephosphorylates HER-2/ErbB-2/Neu (HER-2: human epidermal growth factor receptor-2) at the phosphotyrosine (p-Tyr) residues. Injection of the secretory isoform of PAP has potent antinociceptive effects in mouse models of chronic pain. This enzyme exhibits ecto-5'-nucleotidase activity, is widely distributed, and implicated in the formation of chronic pain. Additionally, PAP could be a target molecule in specific immunotherapy for patients with nonprostate adenocarcinomas including colon and gastric cancers.
|
|||||
TMPY-05526 | Siglec-15 Protein, Human, Recombinant (His) | Human | HEK293 | ||
|
|||||
TMPY-05658 | Siglec-10 Protein, Human, Recombinant (His) | Human | HEK293 | ||
|
|||||
TMPY-01938 | CD98 Protein, Human, Recombinant (His) | Human | HEK293 | ||
4F2 cell-surface antigen heavy chain, also known as 4F2 heavy chain antigen, Lymphocyte activation antigen 4F2 large subunit, CD98, SLC3A2 and MDU1, is a single-pass type I I membrane protein that belongs to the SLC3A transporter family. SLC3A2 / MDU1 is expressed ubiquitously in all tissues tested with highest levels detected in kidney, placenta and testis and weakest level in thymus. During gestation, expression in the placenta is significantly stronger at full-term than at the mid-trimester stage. SLC3A2 / MDU1 is expressed in HUVECS and at low levels in resting peripheral blood T-lymphocytes and quiescent fibroblasts. It is expressed in fetal liver and in the astrocytic process of primary astrocytic gliomas. SLC3A2 / MDU1 is also expressed in retinal endothelial cells and in the intestinal epithelial cell line Caco2-BBE. SLC3A2 / MDU1 is required for the function of light chain amino-acid transporters. It is involved in sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan. SLC3A2 / MDU1 is involved in guiding and targeting of LAT1 and LAT2 to the plasma membrane. When associated with SLC7A6 or SLC7A7, SLC3A2 / MDU1 acts as an arginine/glutamine exchanger, following an antiport mechanism for amino acid transport, influencing arginine release in exchange for extracellular amino acids. SLC3A2 / MDU1 plays a role in nitric oxide synthesis in human umbilical vein endothelial cells (HUVECs) via transport of L-arginine. It is required for normal and neoplastic cell growth. When associated with SLC7A5/LAT1, SLC3A2 / MDU1 is also involved in the transport of L-DOPA across the blood-brain barrier, and that of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane in tissues such as placenta.
|
|||||
TMPY-05099 | GBA/glucocerebrosidase Protein, Human, Recombinant (His) | Human | HEK293 | ||
Mutations in the GBA gene, encoding the lysosomal hydrolase glucocerebrosidase (GCase), are the most common known genetic risk factor for Parkinson's disease (PD) and dementia with Lewy bodies (DLB). ASAH1 (acid ceramidase 1) and GBA2 (glucocerebrosidase 2) enzymes that mediate glucosylsphingosine production and metabolism are attractive therapeutic targets for treating mutant GBA-associated PD.
|
|||||
TMPY-02358 | CD98 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
4F2 cell-surface antigen heavy chain, also known as 4F2 heavy chain antigen, Lymphocyte activation antigen 4F2 large subunit, CD98, SLC3A2 and MDU1, is a single-pass type I I membrane protein that belongs to the SLC3A transporter family. SLC3A2 / MDU1 is expressed ubiquitously in all tissues tested with highest levels detected in kidney, placenta and testis and weakest level in thymus. During gestation, expression in the placenta is significantly stronger at full-term than at the mid-trimester stage. SLC3A2 / MDU1 is expressed in HUVECS and at low levels in resting peripheral blood T-lymphocytes and quiescent fibroblasts. It is expressed in fetal liver and in the astrocytic process of primary astrocytic gliomas. SLC3A2 / MDU1 is also expressed in retinal endothelial cells and in the intestinal epithelial cell line Caco2-BBE. SLC3A2 / MDU1 is required for the function of light chain amino-acid transporters. It is involved in sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan. SLC3A2 / MDU1 is involved in guiding and targeting of LAT1 and LAT2 to the plasma membrane. When associated with SLC7A6 or SLC7A7, SLC3A2 / MDU1 acts as an arginine/glutamine exchanger, following an antiport mechanism for amino acid transport, influencing arginine release in exchange for extracellular amino acids. SLC3A2 / MDU1 plays a role in nitric oxide synthesis in human umbilical vein endothelial cells (HUVECs) via transport of L-arginine. It is required for normal and neoplastic cell growth. When associated with SLC7A5/LAT1, SLC3A2 / MDU1 is also involved in the transport of L-DOPA across the blood-brain barrier, and that of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane in tissues such as placenta.
|
|||||
TMPY-06686 | FASN Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
|
|||||
TMPJ-01073 | FABP5 Protein, Human, Recombinant (His) | Human | E. coli | ||
Fatty acid-binding protein 5 (FABP5) 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. FABP5 can be expressed in keratinocytes, and is highly expressed in psoriatic skin. FABP5 has been shown to be involved in keratinocyte differentiation. FABP5 has high specificity for fatty acids, the highest affinity for C18 chain length. FABP5 can decrease the chain length or introduce double bonds to reduce the affinity.
|
|||||
TMPJ-00520 | NANS Protein, Human, Recombinant (His) | Human | E. coli | ||
Sialic Acid Synthase (NANS) is an enzyme that contains one AFP-like domain. NANS is ubiquitous and plays a role in the biosynthetic pathways of sialic acids. NANS produces N-acetylneuraminic acid (Neu5Ac) and 2-keto-3-deoxy-D-glycero-D-galacto-nononic acid (KDN). It also can use N-acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of Neu5Ac and KDN, respectively.
|
|||||
TMPJ-00908 | LMW-PTP Protein, Human, Recombinant (His) | Human | E. coli | ||
Low Molecular Weight Phosphotyrosine Protein Phosphatase (LMW-PTP) is a member of the low molecular weight phosphotyrosine protein phosphatase family. LMW-PTP serves as an acid phosphatase and a protein tyrosine phosphatase (PTPase) by hydrolyzing protein tyrosine phosphate to protein tyrosine and orthophosphate. LMW-PTP can be detected in all human tissues, including adipocytes. LMW-PTP is a cytosolic enzyme that regulate cell proliferation and growth of leiomyomas during dephosphorylation of the PDGF receptor. In addition, LMW-PTP plays an important role in the regulation of physiological functions, such as stress resistance and synthesis of the polysaccharide capsule.
|
|||||
TMPJ-00785 | FABP3 Protein, Human, Recombinant (His) | Human | E. coli | ||
Fatty Acid Binding Protein 3 (FABP3) is a small cytoplasmic protein (15 kDa) that is released from cardiac myocytes following an ischemic episode. Like the nine other distinct FABPs that have been identified, FABP3 is involved in active fatty acid metabolism where it transports fatty acids from the cell membrane to mitochondria for oxidation. FABPs are divided into at least three distinct types, namely the hepatic-, intestinal- and cardiac-types. They form 14-15 kDa proteins and are thought to participate in the uptake, intracellular metabolism and/or transport of long-chain fatty acids. They may also be responsible in the modulation of cell growth and proliferation. The FABP3 gene contains four exons and its function is to arrest growth of mammary epithelial cells. This gene is also a candidate tumor suppressor gene for human breast cancer. FABP3 is a sensitive biomarker for myocardial infarction and can be detected in the blood within one to three hours of onset of pain.
|
|||||
TMPJ-00853 | DAO Protein, Human, Recombinant (His) | Human | E. coli | ||
D-Amino-Acid Oxidase (DAO) belongs to the DAMOX/DASOX family. DAO is a peroxisomal enzyme which founctions as a homodimer to oxidizes D-amino acids to the corresponding imino acids, producing ammonia and hydrogen peroxide. D-amino-acid oxidase regulates the level of the neuromodulator D-serine in the brain, has a high activity towards D-DOPA and contributes to dopamine synthesis. D-amino-acid oxidase could act as a detoxifying agent which removes D-amino acids accumulated during aging. It also acts on a variety of D-amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups.
|
|||||
TMPJ-00869 | GLB1 Protein, Human, Recombinant (His) | Human | Human Cells | ||
β Galactosidase is a lysosomal β Galactosidase that hydrolyzes the terminal β Galactose from Ganglioside and Keratan sulfate. In lysosome, the mature β Galactosidase protein associates with Cathepsin A and Neuraminidase 1 to form the lysosomal multienzyme complex . An alternative splicing at the RNA level of β Galactosidase results a catalytically inactive β Galactosidase that plays an important role in vascular development. Defects of β-galactosidase (GLB1) are the cause of diseases like GM1-gangliosidosis which is a lysosomal storage disease and Morquio Syndrome B that cause patients to have abnormal elastic fibers. More than 100 mutations have been identified for β Galactosidase, which result in different residual activities of the mutant enzymes and a spectrum of symptoms in the two related diseases.
|
|||||
TMPY-00960 | ACP5 Protein, Human, Recombinant (His) | Human | HEK293 | ||
Tartrate-resistant acid phosphatase (TRACP) or acid phosphatase 5, tartrate resistant (ACP5 or TRAP) is a glycosylated monomeric metalloenzyme expressed in mammals. TRACP is associated with osteoblast migration to bone resorption sites, and, once there, TRACP is believed to initiate osteoblast differentiation, activation, and proliferation. TRACP once considered to be just a histochemical marker of osteoclasts is now recognised to be a molecule of widespread occurrence with functions in both the skeleton and the immune system. Two forms of TRACP circulate in human blood, TRACP 5a derived from macrophages and dendritic cells, and TRACP-5b derived from osteoclasts. Recent data have demonstrated the utility of TRACP-5b as a marker of osteoclast number and bone resorption, and serum TRACP-5a as a marker of inflammatory conditions. TRACP is expressed by osteoclasts, macrophages, dendritic cells and a number of other cell types. It has a critical role in many biological processes including skeletal development, collagen synthesis and degradation, the mineralisation of bone, cytokine production by macrophages and dendritic cells, macrophage recruitment, dendritic cell maturation and a role in the development of Th1 responses.
|
|||||
TMPY-06683 | FASN Protein, Human, Recombinant (His) | Human | E. coli | ||
|
|||||
TMPY-01414 | ACP5 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Tartrate-resistant acid phosphatase (TRACP) or acid phosphatase 5, tartrate resistant (ACP5 or TRAP) is a glycosylated monomeric metalloenzyme expressed in mammals. TRACP is associated with osteoblast migration to bone resorption sites, and, once there, TRACP is believed to initiate osteoblast differentiation, activation, and proliferation. TRACP once considered to be just a histochemical marker of osteoclasts is now recognised to be a molecule of widespread occurrence with functions in both the skeleton and the immune system. Two forms of TRACP circulate in human blood, TRACP 5a derived from macrophages and dendritic cells, and TRACP-5b derived from osteoclasts. Recent data have demonstrated the utility of TRACP-5b as a marker of osteoclast number and bone resorption, and serum TRACP-5a as a marker of inflammatory conditions. TRACP is expressed by osteoclasts, macrophages, dendritic cells and a number of other cell types. It has a critical role in many biological processes including skeletal development, collagen synthesis and degradation, the mineralisation of bone, cytokine production by macrophages and dendritic cells, macrophage recruitment, dendritic cell maturation and a role in the development of Th1 responses.
|
|||||
TMPY-00190 | ULBP-6 Protein, Human, Recombinant (hFc) | Human | HEK293 | ||
ULBP6/RAET1L, is a polymorphic locus that expresses a functional transcript. ULBP6 had a more restricted expression profile in cell lines and primary human tissues than other NKG2D ligands, but expression was detected in several human papillomavirus-positive cervical carcinoma cell lines and was inducible on infection with human CMV. Expression of ULBP6 on target cells induced a significant increase in NK-cell killing.
|
|||||
TMPY-05678 | Siglec-15 Protein, Cynomolgus, Recombinant (hFc) | Cynomolgus | HEK293 | ||
|
|||||
TMPY-01060 | DOPA Decarboxylase/DDC Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
Dopa Decarboxylase (DDC), also known as AADC and Aromatic-L-amino acid decarboxylase, is a 54 kDa member of the group II decarboxylase family of proteins.It is a vitamin B6-dependent homodimeric enzyme that catalyzes the decarboxylation of both L-3,4-dihydroxyphenylalanine (L-DOPA) and L-5-hydroxytryptophan to dopamine and serotonin, respectively, which are major mammalian neurotransmitters and hormones belonging to catecholamines and indoleamines. Since L-DOPA is regularly used to treat the symptoms of Parkinson's disease, the catalytic pathway is of particular research interest. Defects of DDC are associated with severe developmental delay, oculogyric crises (OGC), as well as autosomal recessive disorder AADC deficiency, an early onset inborn error in neurotransmitter metabolism which can lead to catecholamine and serotonin deficiency.
|
|||||
TMPY-00575 | ULBP-6 Protein, Human, Recombinant (His) | Human | HEK293 | ||
ULBP6/RAET1L, is a polymorphic locus that expresses a functional transcript. ULBP6 had a more restricted expression profile in cell lines and primary human tissues than other NKG2D ligands, but expression was detected in several human papillomavirus-positive cervical carcinoma cell lines and was inducible on infection with human CMV. Expression of ULBP6 on target cells induced a significant increase in NK-cell killing.
|
|||||
TMPY-02472 | DOPA Decarboxylase/DDC Protein, Mouse, Recombinant (His) | Mouse | Baculovirus-Insect Cells | ||
Dopa Decarboxylase (DDC), also known as AADC and Aromatic-L-amino acid decarboxylase, is a 54 kDa member of the group II decarboxylase family of proteins.It is a vitamin B6-dependent homodimeric enzyme that catalyzes the decarboxylation of both L-3,4-dihydroxyphenylalanine (L-DOPA) and L-5-hydroxytryptophan to dopamine and serotonin, respectively, which are major mammalian neurotransmitters and hormones belonging to catecholamines and indoleamines. Since L-DOPA is regularly used to treat the symptoms of Parkinson's disease, the catalytic pathway is of particular research interest. Defects of DDC are associated with severe developmental delay, oculogyric crises (OGC), as well as autosomal recessive disorder AADC deficiency, an early onset inborn error in neurotransmitter metabolism which can lead to catecholamine and serotonin deficiency.
|
|||||
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.
|
|||||
TMPY-03278 | SMPDL3A Protein, Human, Recombinant (His) | Human | HEK293 | ||
SMPDL3A gene is a novel liver X receptor (LXR) -regulated gene, with an LXR response element within its promoter. The induction of SMPDL3A is LXR-dependent and is restricted to human blood cells with no induction observed in mouse cellular systems. LXR α and LXRβ function as physiological sensors of cholesterol metabolites (oxysterols), regulating key genes involved in cholesterol and lipid metabolism. LXRs have been extensively studied in both human and rodent cell systems, revealing their potential therapeutic value in the contexts of atherosclerosis and inflammatory diseases. The LXR genome landscape has been investigated in murine macrophages but not in human THP-1 cells, which represent one of the frequently used monocyte/macrophage cell systems to study immune responses.
|
|||||
TMPY-01878 | L-FABP Protein, Human, Recombinant (His) | Human | E. coli | ||
Fatty acid-binding protein, liver, also known as Fatty acid-binding protein 1, Liver-type fatty acid-binding protein, FABP1 and FABPL,is a cytoplasm protein which belongs to thecalycin superfamily and Fatty-acid binding protein (FABP) family. Fatty acid binding proteins are a family of small, highly conserved, cytoplasmic proteins that bind long-chain fatty acids and other hydrophobic ligands. FABP1 and FABP6 (the ileal fatty acid binding protein) are also able to bind bile acids. It is thought that FABPs roles include fatty acid uptake, transport, and metabolism. FABP1 / FABPL binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. It forms a beta-barrel structure that accommodates hydrophobic ligands in its interior. FABP1 / FABPL may be involved in intracellular lipid transport.
|
|||||
TMPJ-00426 | Siglec-5 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | Human Cells | ||
Sialic acid-binding Ig-like lectin 5 is a protein that in Cynomolgus is encoded by the SIGLEC5 gene, Cynomolgus SIGLEC5 cDNA encodes 551 amino acids (aa) that include a 16 aa signal sequence, a 439aa extracellular domain (ECD) with three Ig-like domains, a transmembrane region and a cytoplasma tail. No Siglec has been shown to recognized any cell surface ligand other than sialic acids, suggesting that interactions with glycans containing this carbohydrate are important in mediating the biological functions of Siglecs. Siglec5 to 11 share a high degree of sequence similarity with CD33/Siglec3 both in their extracellular and intracellular regions. Putative adhesion molecule that mediates sialic-acid dependent binding to cells. Binds equally to alpha-2,3-linked and alpha-2,6-linked sialic acid. The sialic acid recognition site may be masked by cis interactions with sialic acids on the same cell surface.
|
|||||
TMPY-00367 | Chemerin/RARRES2 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Retinoic acid receptor responder protein 2 (RARRES2) is a small secreted protein involved in multiple cancers, including adrenocortical carcinoma (ACC). Serum RARRES2 may be used as a novel prognostic marker for ACC. Retinoic acid receptor responder 2 (RARRES2) is transcriptionally downregulated in multiple cancer types. Previous studies suggested that it can serve as an immune-dependent tumor suppressor by acting as a chemoattractant to recruit anticancer immune cells expressing its receptor, the chemerin chemokine receptor 1 (CMKLR1), to sites of tumor. Mechanistically, RARRES2 overexpression in ACC cells inhibited Wnt/beta-catenin pathway activity by promoting beta-catenin phosphorylation and degradation, it also inhibited the phosphorylation of p38 mitogen-activated protein kinase. Thus RARRES2 is a novel tumor suppressor for ACC, which can function through an immune-independent mechanism.
|
|||||
TMPY-01549 | CRABP2 Protein, Human, Recombinant (His) | Human | E. coli | ||
Cellular retinoic acid-binding protein 2, also known as Cellular retinoic acid-binding protein II, CRABP-II and CRABP2, is a protein which belongs to thecalycin superfamily and Fatty-acid binding protein (FABP) family. Cellular retinoic acid binding proteins (CRABP) are low molecular weight proteins whose precise function remains unknown. The predicted amino acid sequences of human CRABP1 and CRABP2 demonstrated a 99.3% and 93.5% identity to mouse CRABP1 and CRABP2, respectively. CRABP2 forms a beta-barrel structure that accommodates hydrophobic ligands in its interior. Expression of CRABP2, but not CRABP1 mRNA, was markedly increased (greater than 15-fold) by retinoic acid treatment of fibroblasts cultured from human skin, whereas no significant induction of CRABP2 mRNA was observed in human lung fibroblasts. CRABP2 transports retinoic acid to the nucleus. It regulates the access of retinoic acid to the nuclear retinoic acid receptors. CRABP2 is necessary for elastin induction by All-trans retinoic acid (ATRA) in MRC-5 cells. It is expressed at low levels in emphysema fibroblasts. This alteration in the retinoic acid signalling pathway in lung fibroblasts may contribute to the defect of alveolar repair in human pulmonary emphysema.
|
|||||
TMPY-04623 | PRRG2 Protein, Human, Recombinant (mFc) | Human | HEK293 | ||
The genes encoding a family of proteins termed proline-rich gamma-carboxyglutamic acid (PRRG) proteins were identified and characterized more than a decade ago. These novel membrane proteins have an extracellular gamma-carboxyglutamic acid (Gla) protein domain and cytosolic WW binding motifs. Several of the PRRG-interacting proteins are essential for a variety of physiologic processes.
|
|||||
TMPY-04143 | Chemerin/RARRES2 Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
Retinoic acid receptor responder protein 2 (RARRES2) is a small secreted protein involved in multiple cancers, including adrenocortical carcinoma (ACC). Serum RARRES2 may be used as a novel prognostic marker for ACC. Retinoic acid receptor responder 2 (RARRES2) is transcriptionally downregulated in multiple cancer types. Previous studies suggested that it can serve as an immune-dependent tumor suppressor by acting as a chemoattractant to recruit anticancer immune cells expressing its receptor, the chemerin chemokine receptor 1 (CMKLR1), to sites of tumor. Mechanistically, RARRES2 overexpression in ACC cells inhibited Wnt/beta-catenin pathway activity by promoting beta-catenin phosphorylation and degradation, it also inhibited the phosphorylation of p38 mitogen-activated protein kinase. Thus RARRES2 is a novel tumor suppressor for ACC, which can function through an immune-independent mechanism.
|
|||||
TMPY-02051 | FABP2 Protein, Human, Recombinant (His) | Human | E. coli | ||
Fatty acid binding protein (FABP) is one of the intracellular proteins, with a low molecular weight of approximately 15 kDa, that plays important roles in the transportation and metabolism of long-chain fatty acids. FABP family proteins could be used as tissue specific injury marker based on the following characteristics of FABP. The intestinal fatty acid binding protein (I-FABP), or fatty acid-binding protein 2 (FABP2), an intracellular protein expressed only in the intestine, involved in the absorption and intracellular transport of dietary long chain fatty acids. The FABP2 gene is proposed as a candidate gene for diabetes because the protein it codes is involved in fatty acid (FA) absorption and metabolism. Numerous studies have assessed FABP2 gene variants. A transition of G to A at codon 54 of FABP2 results in an amino acid substitution (Ala54 to Thr54), which is common in diverse populations and results in increased FA absorption in vivo. Some evidence indicates that this variant may be associated with type 2 diabetes. This polymorphism was associated with some cardiovascular risk factors. The cytosolic human intestinal fatty acid binding protein (hFABP2) is proposed to be involved in intestinal absorption of long-chain fatty acids. FABP2 may also help maintain energy homeostasis by functioning as a lipid sensor.
|
|||||
TMPY-02189 | CRABP2 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Cellular retinoic acid-binding protein 2, also known as Cellular retinoic acid-binding protein II, CRABP-II and CRABP2, is a protein which belongs to thecalycin superfamily and Fatty-acid binding protein (FABP) family. Cellular retinoic acid binding proteins (CRABP) are low molecular weight proteins whose precise function remains unknown. The predicted amino acid sequences of human CRABP1 and CRABP2 demonstrated a 99.3% and 93.5% identity to mouse CRABP1 and CRABP2, respectively. CRABP2 forms a beta-barrel structure that accommodates hydrophobic ligands in its interior. Expression of CRABP2, but not CRABP1 mRNA, was markedly increased (greater than 15-fold) by retinoic acid treatment of fibroblasts cultured from human skin, whereas no significant induction of CRABP2 mRNA was observed in human lung fibroblasts. CRABP2 transports retinoic acid to the nucleus. It regulates the access of retinoic acid to the nuclear retinoic acid receptors. CRABP2 is necessary for elastin induction by All-trans retinoic acid (ATRA) in MRC-5 cells. It is expressed at low levels in emphysema fibroblasts. This alteration in the retinoic acid signalling pathway in lung fibroblasts may contribute to the defect of alveolar repair in human pulmonary emphysema.
|
|||||
TMPY-02952 | SIAE Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
Sialate O-acetylesterase belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. It is widely expressed with high expression in the testis, prostate, and colon. The systematic name of this enzyme class is N-acyl-O-acetylneuraminate O-acetylhydrolase. Other names in common use include N-acetylneuraminate acetyltransferase, sialate 9(4)-O-acetylesterase, and sialidase. Sialate O-acetylesterase catalyzes the removal of O-acetyl ester groups from position 9 of the parent sialic acid, N-acetylneuraminic acid. Defects in Sialate O-acetylesterase are a cause of autoimmune disease type 6 (AIS6). Individuals manifesting susceptibility to autoimmune disease type 6 can suffer from juvenile idiopathic arthritis, rheumatoid arthritis, multiple sclerosis, Sjogren syndrome, systemic lupus erythematosus, type 1 diabetes, ulcerative colitis, and Crohn disease.
|
|||||
TMPY-04631 | CD98 Protein, Rat, Recombinant (hFc) | Rat | HEK293 | ||
4F2 cell-surface antigen heavy chain, also known as 4F2 heavy chain antigen, Lymphocyte activation antigen 4F2 large subunit, CD98, SLC3A2 and MDU1, is a single-pass type I I membrane protein that belongs to the SLC3A transporter family. SLC3A2 / MDU1 is expressed ubiquitously in all tissues tested with highest levels detected in kidney, placenta and testis and weakest level in thymus. During gestation, expression in the placenta is significantly stronger at full-term than at the mid-trimester stage. SLC3A2 / MDU1 is expressed in HUVECS and at low levels in resting peripheral blood T-lymphocytes and quiescent fibroblasts. It is expressed in fetal liver and in the astrocytic process of primary astrocytic gliomas. SLC3A2 / MDU1 is also expressed in retinal endothelial cells and in the intestinal epithelial cell line Caco2-BBE. SLC3A2 / MDU1 is required for the function of light chain amino-acid transporters. It is involved in sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan. SLC3A2 / MDU1 is involved in guiding and targeting of LAT1 and LAT2 to the plasma membrane. When associated with SLC7A6 or SLC7A7, SLC3A2 / MDU1 acts as an arginine/glutamine exchanger, following an antiport mechanism for amino acid transport, influencing arginine release in exchange for extracellular amino acids. SLC3A2 / MDU1 plays a role in nitric oxide synthesis in human umbilical vein endothelial cells (HUVECs) via transport of L-arginine. It is required for normal and neoplastic cell growth. When associated with SLC7A5/LAT1, SLC3A2 / MDU1 is also involved in the transport of L-DOPA across the blood-brain barrier, and that of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane in tissues such as placenta.
|
|||||
TMPY-03307 | CD98 Protein, Rat, Recombinant (His) | Rat | HEK293 | ||
4F2 cell-surface antigen heavy chain, also known as 4F2 heavy chain antigen, Lymphocyte activation antigen 4F2 large subunit, CD98, SLC3A2 and MDU1, is a single-pass type I I membrane protein that belongs to the SLC3A transporter family. SLC3A2 / MDU1 is expressed ubiquitously in all tissues tested with highest levels detected in kidney, placenta and testis and weakest level in thymus. During gestation, expression in the placenta is significantly stronger at full-term than at the mid-trimester stage. SLC3A2 / MDU1 is expressed in HUVECS and at low levels in resting peripheral blood T-lymphocytes and quiescent fibroblasts. It is expressed in fetal liver and in the astrocytic process of primary astrocytic gliomas. SLC3A2 / MDU1 is also expressed in retinal endothelial cells and in the intestinal epithelial cell line Caco2-BBE. SLC3A2 / MDU1 is required for the function of light chain amino-acid transporters. It is involved in sodium-independent, high-affinity transport of large neutral amino acids such as phenylalanine, tyrosine, leucine, arginine and tryptophan. SLC3A2 / MDU1 is involved in guiding and targeting of LAT1 and LAT2 to the plasma membrane. When associated with SLC7A6 or SLC7A7, SLC3A2 / MDU1 acts as an arginine/glutamine exchanger, following an antiport mechanism for amino acid transport, influencing arginine release in exchange for extracellular amino acids. SLC3A2 / MDU1 plays a role in nitric oxide synthesis in human umbilical vein endothelial cells (HUVECs) via transport of L-arginine. It is required for normal and neoplastic cell growth. When associated with SLC7A5/LAT1, SLC3A2 / MDU1 is also involved in the transport of L-DOPA across the blood-brain barrier, and that of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane in tissues such as placenta.
|
|||||
TMPY-05835 | Siglec-15 Protein, Mouse, Recombinant (rFc) | Mouse | HEK293 | ||
|
|||||
TMPY-01579 | GBA3 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
Cytosolic beta-glucosidase, also known as Cytosolic beta-glucosidase-like protein 1, GBA3, CBG and CBGL1 is a cytoplasm protein which belongs to theglycosyl hydrolase 1 family and Klotho subfamily. GBA3 / CBGL1 is a glycosidase probably involved in the intestinal absorption and metabolism of dietary flavonoid glycosides. GBA3 / CBGL1 is present in small intestine (at protein level). GBA3 / CBGL1 is expressed in liver, small intestine, colon, spleen and kidney. GBA3 / CBGL1 is down-regulated in renal cell carcinomas and hepatocellular carcinomas. GBA3 / CBGL1 is able to hydrolyze a broad variety of glycosides including phytoestrogens, flavonols, flavones, flavanones and cyanogens. GBA3 / CBGL1 possesses beta-glycosylceramidase activity and may be involved in a nonlysosomal catabolic pathway of glycosylceramide.
|
|||||
TMPJ-00938 | 4HPPD Protein, Human, Recombinant (His) | Human | E. coli | ||
4-Hydroxyphenylpyruvate Dioxygenase (4HPPD) belongs to the 4HPPD family. 4HPPD is a key enzyme in the degradation of tyrosine, which catalyzes the second reaction in the catabolism of tyrosine the conversation of 4-hydroxyphenylpyruvate to homogentisate. 4HPPD exists in homodimer forms, which uses zinc as a cofactor to catalyze the third step in the conversion of L-phenylalanine to fumarate and acetoacetic acid. When the active 4HPPD enzyme concentration is low in the human body, it results in high levels of tyrosine concentration in the blood, which can cause mild mental retardation at birth, and degradation in vision as a patient grows older.
|
|||||
TMPY-04512 | SMPDL3A Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
SMPDL3A gene is a novel liver X receptor (LXR) -regulated gene, with an LXR response element within its promoter. The induction of SMPDL3A is LXR-dependent and is restricted to human blood cells with no induction observed in mouse cellular systems. LXR α and LXRβ function as physiological sensors of cholesterol metabolites (oxysterols), regulating key genes involved in cholesterol and lipid metabolism. LXRs have been extensively studied in both human and rodent cell systems, revealing their potential therapeutic value in the contexts of atherosclerosis and inflammatory diseases. The LXR genome landscape has been investigated in murine macrophages but not in human THP-1 cells, which represent one of the frequently used monocyte/macrophage cell systems to study immune responses.
|
|||||
TMPY-03864 | CRABP1 Protein, Human, Recombinant | Human | E. coli | ||
CRABP1 is a specific binding protein for a vitamin A family member. It is thought that CRABP1 plays an important role in retinoic acid-mediated differentiation and proliferation processes. CRABP1 is structurally similar to the cellular retinol-binding proteins, but binds only retinoic acid at specific sites within the nucleus, which may contribute to vitamin A-directed differentiation in epithelial tissue. It forms a beta-barrel structure which accommodates hydrophobic ligands in its interior.
|
|||||
TMPY-01482 | FABP4 Protein, Mouse, Recombinant (His) | Mouse | HEK293 | ||
Fatty acid-binding protein, adipocyte, also known as Adipocyte-type fatty acid-binding protein, Fatty acid-binding protein 4, Adipocyte lipid-binding protein, and FABP4, is a cytoplasm protein which belongs to thecalycin superfamily and Fatty-acid binding protein (FABP) family. In familial combined hyperlipidemia (FCHL), FABP4 correlated to body mass index (BMI), waist circumference and homeostasis model assessment (HOMA) index.FABP4 levels were associated with triglyceride-rich lipoproteins. In humans serum FABP4 levels correlate significantly with features of PCOS. It appears to be a determinant of atherogenic dyslipidemia. FABP4 pathway mediates the sebaceous gland hyperplasia in keratinocyte-specific Pten-null mice. FABP4 concentration significantly increased with an increasing of MS features and was strongly correlated with body-mass index, triglycerides, HDL-cholesterol concentrations and blood pressure. Patients in the highest quartile of FABP4 presented a six-fold increased odds ratio for MS and a three-fold increased odds for LD, adjusted by age, sex, body-mass index and the antiretroviral therapy. FABP4 is a strong plasma marker of metabolic disturbances in HIV-infected patients, and therefore, could serve to guide therapeutic intervention in this group of patients.
|
|||||
TMPY-01306 | DNMT2 Protein, Human, Recombinant (GST) | Human | Baculovirus-Insect Cells | ||
DNMT2, also known as tRNA (cytosine-5-)-methyltransferase, DNA methyltransferase homolog HsaIIP, and TRDMT1, is a member of the DNA methyltransferase family of enzymes. DNMT2 enzymes have been widely conserved during evolution and contain all of the signature motifs of DNA (cytosine-5)-methyltransferases. It contains all 10 sequence motifs that are conserved among m(5)C MTases, including the consensus S:-adenosyl-L-methionine-binding motifs and the active site ProCys dipeptide, and its structure is very similar to prokaryotic DNA methyltransferases. DNMT2 has close homologs in plants, insects and Schizosaccharomyces pombe, but no related sequence can be found in the genomes of Saccharomyces cerevisiae or Caenorhabditis elegans. While the biological function of DNMT2 is not yet known, the strong binding to DNA suggests that DNMT2 may mark specific sequences in the genome by binding to DNA through the specific target-recognizing motif. However, the DNA methyltransferase activity of these proteins is comparatively weak and their biochemical and functional properties remain enigmatic. Recent evidence now shows that Dnmt2 has a novel tRNA methyltransferase activity, raising the possibility that the biological roles of these proteins might be broader than previously thought.
|
|||||
TMPY-05736 | Siglec-15 Protein, Human, Recombinant (mFc) | Human | HEK293 | ||
|
|||||
TMPY-02239 | FABP3 Protein, Human, Recombinant | Human | E. coli | ||
Fatty acid binding protein 3 (FABP3, also termed heart-type fatty acid binding protein) is a member of the intracellular lipid-binding protein family that may be essential in fatty acid transport, cell growth, cellular signaling and gene transcription. Previously FABP3 was involved in apoptosis-associated congenital cardiac malformations. FABP3 knockdown exhibited significant toxic effects on cardiac development and mitochondrial function, which may be responsible for the knockdown of FABP3-induced apoptosis. FABP3 as a candidate gene underlying the etiology of congenital heart defects. Overexpression of FABP3 inhibited cell growth and proliferation via negative regulation of the cell cycle and down-regulation of cell growth factors, but enhances cell survival in hypoxic or ischemic conditions. FABPs are known to be carrier proteins for transporting fatty acids and other lipophilic substances from the cytoplasm to the nucleus, where these lipids are released to a group of nuclear receptors such as peroxisome proliferator-activated receptors (PPARs).
|
|||||
TMPJ-00529 | FABP6 Protein, Human, Recombinant (His) | Human | E. coli | ||
Fatty Acid-Binding Protein 6 (FABP6) is cytoplasmic protein that binds long-chain fatty acids and other hydrophobic ligands which belongs to the calycin superfamily. FABP6 expression is restricted in the small intestine to the ileum where it is involved in the enterohepatic circulation of bile acids. FABP6 forms a beta-barrel structure that accommodates the hydrophobic ligand in its interior. Isoform 2 is expressed in colorectal adenocarcinomas and their adjacent normal mucosa (at protein level). Isoform 1 is expressed in the jejunum, ileum, cecum and ascending colon intestine. FABP6 plays a role in fatty acid uptake, transport, and metabolism. FABP6 stimulates gastric acid and pepsinogen secretion. It seems to be able to bind to bile salts and bilirubins.
|
|||||
TMPY-05832 | Siglec-10 Protein, Human, Recombinant (mFc) | Human | HEK293 | ||
|
|||||
TMPJ-00217 | Siglec-15 Protein, Human, Recombinant (hFc & Avi), Biotinylated | Human | Human Cells | ||
Human Siglec-15 is a transmembrane glycoprotein in the Siglec family. Siglecs are type I transmembrane proteins where the NH3+-terminus is in the extracellular space and the COO−-terminus is cytosolic. Each Siglec contains an N-terminal V-type immunoglobulin domain (Ig domain) which acts as the binding receptor for sialic acid. These lectins are placed into the group of I-type lectins because the lectin domain is an immunoglobulin fold. All Siglecs are extended from the cell surface by C2-type Ig domains which have no binding activity. Siglecs differ in the number of these C2-type domains. Human Siglec-15 consists of a 244 amino acid (aa) extracellular domain (ECD) with two Ig-like domains, a 21 aa transmembrane segment, and a 44 aa cytoplasmic domain. Siglec-15 function is important for osteoclast formation and TRANCE/RANK Ligand signaling in osteoclasts.
|
|||||
TMPY-00605 | FABP3 Protein, Mouse, Recombinant | Mouse | E. coli | ||
Fatty acid binding protein 3 (FABP3, also termed heart-type fatty acid binding protein) is a member of the intracellular lipid-binding protein family that may be essential in fatty acid transport, cell growth, cellular signaling and gene transcription. Previously FABP3 was involved in apoptosis-associated congenital cardiac malformations. FABP3 knockdown exhibited significant toxic effects on cardiac development and mitochondrial function, which may be responsible for the knockdown of FABP3-induced apoptosis. FABP3 as a candidate gene underlying the etiology of congenital heart defects. Overexpression of FABP3 inhibited cell growth and proliferation via negative regulation of the cell cycle and down-regulation of cell growth factors, but enhances cell survival in hypoxic or ischemic conditions. FABPs are known to be carrier proteins for transporting fatty acids and other lipophilic substances from the cytoplasm to the nucleus, where these lipids are released to a group of nuclear receptors such as peroxisome proliferator-activated receptors (PPARs).
|