目录号 | 产品详情 | 靶点 | |
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T65978 | |||
Boc-Glycine 是一种有用的有机化合物,可用于生命科学领域的相关研究。其产品编号为 T65978,CAS号为 4530-20-5。 | |||
T65459 | |||
(2,2,2-Trifluoroacetyl)glycine 是一种有用的有机化合物,可用于生命科学领域的相关研究。其产品编号为 T65459,CAS号为 383-70-0。 | |||
T23864 | |||
CCPG is an agonist of excitatory Amino Acid. | |||
T40016 | Ligand for E3 Ligase | ||
Thalidomide-NH-CH2-COOH ((2-(2,6-Dioxopiperidin-3-yl)-1,3-dioxoisoindolin-4-yl)glycine) 是一种基于 Thalidomide 的 Cereblon 配体,可用于募集 CRBN 蛋白。它能够利用 linker 与靶蛋白配体连接,得到 PROTAC 分子。 | |||
T65548 | |||
Diphenylmethylene-glycine benzyl ester 是一种有用的有机化合物,可用于生命科学领域的相关研究。其产品编号为 T65548,CAS号为 81477-91-0。 | |||
T11908 | GlyT | ||
LY2365109 hydrochloride 是高选择性GlyT1抑制剂,抑制过表达 hGlyT1 细胞摄取谷氨酸的IC50值为 15.8 nM. | |||
T64666 | |||
10× Tris-Glycine Transfer Buffer 是一种有用的有机化合物,可用于生命科学领域的相关研究,其产品编号为 T64666。 | |||
T83673 | |||
4-Hydroxyphenylpropionylglycine是一种由条件必需氨基酸酪氨酸代谢形成的代谢产物。通过芳香族氨基酸转氨酶、酪氨酸转氨酶以及肠道微生物作用后,结合甘氨酸共轭生成。此外,4-Hydroxyphenylpropionylglycine也是酚类化合物phloretin的代谢产物。 | |||
T65237 | |||
Glycine 7-amido-4-methylcoumarin hydrobromide 是一种有用的有机化合物,可用于生命科学领域的相关研究。其产品编号为 T65237,CAS号为 113728-13-5。 | |||
T9626 | NMDAR | ||
Cycloleucine 是 NMDA 受体相关甘氨酸受体的拮抗剂,Ki 为 600 μM。Cycloleucine 也是 S-腺苷甲硫氨酸介导的甲基化的竞争性抑制剂,具有抗焦虑和细胞抑制作用。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPJ-01118 | GNMT Protein, Human, Recombinant (His) | Human | E. coli | ||
Glycine N-Methyltransferase (GNMT) is a tetrameric cytosolic protein. GNMT catalyzes the synthesis of N-methylglycine from glycine using S-adenosylmethionine (AdoMet) as the methyl donor. It can affects DNA methylation by regulating the ratio of S-adenosylmethionine to S-adenosylhomocystine, playing an important role in maintaining normal AdoMet levels. GNMT is highly expressed in liver. As a major folate-binding protein, GNMT takes part in the detoxification pathway. Defects in GNMT are the cause of hypermethioninemia. the patients with this deficiency are mild hepatomegaly and chronic elevation of serum transaminases.
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TMPJ-00484 | SHMT1 Protein, Human, Recombinant (His) | Human | Human Cells | ||
Serine Hydroxymethyltransferase Cytosolic (SHMT1) is a member of the SHMT family. SHMT1 is a cytoplasmic protein and exists as a homotetramer. SHMT1 catalyzes the reversible conversion of serine and tetrahydrofolate to glycine and 5,10-methylene tetrahydrofolate. This reaction provides one carbon unit for the synthesis of methionine, thymidylate, and purines in the cytoplasm. A reduction in SHMT1 levels would result in less glycine that could affect the nervous system by acting as an agonist to the NMDA receptor and this could be a mechanism behind Smith-Magenis syndrome.
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TMPY-03503 | GCSH Protein, Human, Recombinant (His) | Human | E. coli | ||
Degradation of glycine is brought about by the glycine cleavage system, which is composed of four mitochondrial protein components: P protein (a pyridoxal phosphate-dependent glycine decarboxylase), H protein (a lipoic acid-containing protein), T protein (a tetrahydrofolate-requiring enzyme), and L protein (a lipoamide dehydrogenase). GCSH is the H protein, which transfers the methylamine group of glycine from the P protein to the T protein. Defects in GCSH gene are a cause of nonketotic hyperglycinemia (NKH). Two transcript variants, one protein-coding and the other probably not protein-coding,have been found for GCSH gene. Also, several transcribed and non-transcribed pseudogenes of GCSH gene exist throughout the genome.
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TMPH-00774 | SAM22 Protein, Glycine max, Recombinant (His) | Glycine max | Yeast | ||
Involved in disease resistance.
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TMPH-00770 | 2S albumin Protein, Glycine max, Recombinant (His) | Glycine max | Yeast | ||
This is a 2S seed storage protein.; binds to mammalian chromatin, preventing the normal formation of the kinetochore complex in the centromere and leading to the disruption of mitosis.
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TMPH-00772 | Leghemoglobin C2 Protein, Glycine max, Recombinant (His) | Glycine max | E. coli | ||
Provides oxygen to the bacteroids. This role is essential for symbiotic nitrogen fixation.
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TMPY-02235 | CSRP1 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Cysteine and glycine-rich protein 1, also known as Cysteine-rich protein 1, CSRP1 and CSRP, is a member of the CSRP family which may be involved in regulatory processes important for development and cellular differentiation. CSRP1 contains twoLIM zinc-binding domains. The LIM / double zinc-finger motif found in CSRP1 is found in a group of proteins with critical functions in gene regulation, cell growth, and somatic differentiation. Zebrafish CSRP1 is expressed in the mesendoderm and its derivatives. CSRP1 interacts with Dishevelled 2 (Dvl2) and Diversin (Div), which control cell morphology and other dynamic cell behaviors via the noncanonical Wnt and JNK pathways. When CSRP1 message is knocked down, abnormal convergent extension cell movement is induced, resulting in severe deformities in midline structures. In addition, cardiac bifida is induced as a consequence of defects in cardiac mesoderm cell migration. CSRP1 acts as a key molecule of the noncanonical Wnt pathway, which orchestrates cell behaviors during dynamic morphogenetic movements of tissues and organs.
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TMPJ-01410 | LSM4 Protein, Human, Recombinant (His) | Human | E. coli | ||
U6 snRNA-associated Sm-like protein LSm4 (LSM4) is a member of the snRNP Sm proteins family. Sm-like proteins contain the Sm sequence motif and are thought to form a stable heteromer present in tri-snRNP particles, which are important for pre-mRNA splicing. LSM4 forms a heteromer with a donut shape. The complexes are involved in various steps of RNA metabolism. LSM4 binds specifically to the 3-terminal U-tract of U6 snRNA. LSM4 contributes RNA protein interactions and structural changes which are essential during ribosomal subunit assembly.
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TMPH-00166 | Glycine oxidase Protein, Bacillus subtilis, Recombinant (His & SUMO) | Bacillus subtilis | E. coli | ||
Glycine oxidase Protein, Bacillus subtilis, Recombinant (His & SUMO) is expressed in E. coli.
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TMPH-00771 | Ferritin-2 Protein, Glycine max, Recombinant (His & SUMO) | Glycine max | E. coli | ||
Stores iron in a soluble, non-toxic, readily available form. Important for iron homeostasis. Has ferroxidase activity. Iron is taken up in the ferrous form and deposited as ferric hydroxides after oxidation.
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TMPY-01562 | CSRP1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Cysteine and glycine-rich protein 1, also known as Cysteine-rich protein 1, CSRP1 and CSRP, is a member of the CSRP family which may be involved in regulatory processes important for development and cellular differentiation. CSRP1 contains twoLIM zinc-binding domains. The LIM / double zinc-finger motif found in CSRP1 is found in a group of proteins with critical functions in gene regulation, cell growth, and somatic differentiation. Zebrafish CSRP1 is expressed in the mesendoderm and its derivatives. CSRP1 interacts with Dishevelled 2 (Dvl2) and Diversin (Div), which control cell morphology and other dynamic cell behaviors via the noncanonical Wnt and JNK pathways. When CSRP1 message is knocked down, abnormal convergent extension cell movement is induced, resulting in severe deformities in midline structures. In addition, cardiac bifida is induced as a consequence of defects in cardiac mesoderm cell migration. CSRP1 acts as a key molecule of the noncanonical Wnt pathway, which orchestrates cell behaviors during dynamic morphogenetic movements of tissues and organs.
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TMPH-00773 | RuBisCO large subunit Protein, Glycine max, Recombinant (His & SUMO) | Glycine max | E. coli | ||
RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.
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TMPH-00769 | 2S albumin Protein, Glycine max, Recombinant (His & SUMO) | Glycine max | E. coli | ||
This is a 2S seed storage protein.; binds to mammalian chromatin, preventing the normal formation of the kinetochore complex in the centromere and leading to the disruption of mitosis.
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TMPH-01110 | CIRBP Protein, Human, Recombinant (GST) | Human | E. coli | ||
CIRBP Protein, Human, Recombinant (GST) is expressed in E. coli.
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TMPH-02587 | CIRBP Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Cold-inducible mRNA binding protein that plays a protective role in the genotoxic stress response by stabilizing transcripts of genes involved in cell survival. Promotes assembly of stress granules (SGs), when overexpressed. Seems to play an essential role in cold-induced suppression of cell proliferation. Acts as a translational repressor. Acts as a translational activator. Binds specifically to the 3'-untranslated regions (3'-UTRs) of stress-responsive transcripts RPA2 and TXN.
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TMPH-01176 | CSRP3 Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
CSRP3 Protein, Human, Recombinant (His & SUMO) is expressed in E. coli.
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TMPH-01596 | AADAT Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
Transaminase with broad substrate specificity. Has transaminase activity towards aminoadipate, kynurenine, methionine and glutamate. Shows activity also towards tryptophan, aspartate and hydroxykynurenine. Accepts a variety of oxo-acids as amino-group acceptors, with a preference for 2-oxoglutarate, 2-oxocaproic acid, phenylpyruvate and alpha-oxo-gamma-methiol butyric acid. Can also use glyoxylate as amino-group acceptor (in vitro).
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TMPY-02836 | MFGE8 Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
MFG-E8, also known as lactadherin and MFGE8, contains 1 EGF-like domain and 2 F5/8 type C domains. It also contains phosphatidylserine (PS) binding domain, as well as an Arginine-Glycine-Aspartic acid motif, which enables the binding to integrins. It binds PS, which is exposed on the surface of apoptotic cells. MFG-E8 is expressed in mammary epithelial cell surfaces and aortic media. Overexpression of MFG-E8 can be found in several carcinomas. MFG-E8 has opsonization of the apoptotic cells and binding to integrins on the surface of phagocytic cells. It also mediates the engulfment of the dead cell. MFG-E8 plays an important role in the maintenance of intestinal epithelial homeostasis and the promotion of mucosal healing. It promotes VEGF-dependent neovascularization and contributes to the phagocytic removal of apoptotic cells in many tissues. It also binds to phosphatidylserine-enriched cell surfaces in a receptor-independent manner.
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TMPY-01288 | Osteopontin Protein, Human, Recombinant (His) | Human | HEK293 | ||
Osteopontin, also known as Secreted phosphoprotein 1, Bone sialoprotein 1, BSP-1, OPN, and SPP1, is a member of the osteopontin family and a SIBLING glycoprotein. Osteopontin has been classified as T-helper 1 cytokine and thus believed to exacerbate inflammation in several chronic inflammatory diseases, including atherosclerosis. Besides proinflammatory functions, physiologically Osteopontin is a potent inhibitor of mineralization, it prevents ectopic calcium deposits and is a potent inducible inhibitor of vascular calcification. Osteopontin is expressed and secreted by various cells, and has a role in cell adhesion, chemotaxis, prevention of apoptosis, invasion, migration and anchorage-independent growth of tumor cells. Osteopontin recruitment functions of inflammatory cells are thought to be mediated through its adhesive domains, especially the arginine-glycine-aspartate (RGD) sequence that interacts with several integrin heterodimers. Osteopontin has emerged as a potential biomarker and mediator in cardiovascular disease. In the context of atherosclerosis, OPN is generally regarded as a proinflammatory and proatherogenic molecule. However, the role of OPN in vascular calcification (VC), which is closely related to chronic and active inflammation, is that of a negative regulator because it is an inhibitor of calcification and an active inducer of decalcification. Extensive research has demonstrated the pivotal participation of Osteopontin in the regulation of cell signaling which controls neoplastic and malignant transformation. The elevated expression of Osteopontin has been observed in a variety of cancers. It has been linked with tumor metastasis and signifies a poor prognosis for the patient.
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TMPY-06988 | Osteopontin Protein, Human, Recombinant (aa 17-166, His) | Human | HEK293 | ||
Osteopontin, also known as Secreted phosphoprotein 1, Bone sialoprotein 1, BSP-1, OPN, and SPP1, is a member of the osteopontin family and a SIBLING glycoprotein. Osteopontin has been classified as T-helper 1 cytokine and thus believed to exacerbate inflammation in several chronic inflammatory diseases, including atherosclerosis. Besides proinflammatory functions, physiologically Osteopontin is a potent inhibitor of mineralization, it prevents ectopic calcium deposits and is a potent inducible inhibitor of vascular calcification. Osteopontin is expressed and secreted by various cells, and has a role in cell adhesion, chemotaxis, prevention of apoptosis, invasion, migration and anchorage-independent growth of tumor cells. Osteopontin recruitment functions of inflammatory cells are thought to be mediated through its adhesive domains, especially the arginine-glycine-aspartate (RGD) sequence that interacts with several integrin heterodimers. Osteopontin has emerged as a potential biomarker and mediator in cardiovascular disease. In the context of atherosclerosis, OPN is generally regarded as a proinflammatory and proatherogenic molecule. However, the role of OPN in vascular calcification (VC), which is closely related to chronic and active inflammation, is that of a negative regulator because it is an inhibitor of calcification and an active inducer of decalcification. Extensive research has demonstrated the pivotal participation of Osteopontin in the regulation of cell signaling which controls neoplastic and malignant transformation. The elevated expression of Osteopontin has been observed in a variety of cancers. It has been linked with tumor metastasis and signifies a poor prognosis for the patient.
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TMPH-03535 | Dihydrofolate reductase Protein, S. aureus, Recombinant (His & Myc) | Staphylococcus aureus | E. coli | ||
Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
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TMPH-02331 | GLRA1 Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
Glycine receptors are ligand-gated chloride channels. Channel opening is triggered by extracellular glycine. Channel opening is also triggered by taurine and beta-alanine. Channel characteristics depend on the subunit composition; heteropentameric channels are activated by lower glycine levels and display faster desensitization. Plays an important role in the down-regulation of neuronal excitability. Contributes to the generation of inhibitory postsynaptic currents. Channel activity is potentiated by ethanol. Potentiation of channel activity by intoxicating levels of ethanol contribute to the sedative effects of ethanol.
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TMPH-00608 | Dihydrofolate reductase Protein, E. coli, Recombinant (His) | E. coli | E. coli | ||
Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
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TMPH-03581 | Dihydrofolate reductase Protein, S. epidermidis, Recombinant (His) | Staphylococcus epidermidis | E. coli | ||
Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis.
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TMPH-01224 | Dihydrofolate reductase Protein, Human, Recombinant (His) | Human | E. coli | ||
Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Binds its own mRNA and that of DHFR2.
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TMPH-01394 | GRIN1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+). Sensitivity to glutamate and channel kinetics depend on the subunit composition.
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TMPY-02979 | HMGN3 Protein, Human, Recombinant (His) | Human | E. coli | ||
HMGN3 belongs to the HMGN family and is expressed in the kidney, lung, pancreas, testis, skeletal muscle, heart, thyroid gland, pituitary gland, prostate, and uterus. Members of the HMGN family bind to nucleosomes without any specificity for the underlying DNA sequence. They affect the global and local structure of chromatin, as well as the levels of histone modifications, and thus play a role in epigenetic regulation of gene expression. HMGN3 regulates the expression of the glucose transporter SLC2A2 by binding specifically to its promoter region and recruiting PDX1 and additional transcription factors. It also regulates the expression of SLC6A9, a glycine transporter that regulates the glycine concentration in synaptic junctions in the central nervous system, by binding to its transcription start site. Both insulin and glucagon levels can be affected by HMGN3. HMGN3 may play a role in ocular development and astrocyte function. It also modulates the expression of pancreatic genes involved in insulin secretion.
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TMPH-01570 | KLHDC3 Protein, Human, Recombinant (E. coli, His & Myc) | Human | E. coli | ||
Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. The CRL2(KLHDC3) complex specifically recognizes proteins with a glycine (Gly) at the C-terminus, leading to their ubiquitination and degradation: recognizes the C-terminal -Arg-(Xaa)n-Arg-Gly, -Arg-(Xaa)n-Lys-Gly, and -Arg-(Xaa)n-Gln-Gly degrons. The CRL2(KLHDC3) complex mediates ubiquitination and degradation of truncated SELENOV and SEPHS2 selenoproteins produced by failed UGA/Sec decoding, which end with a glycine. May be involved in meiotic recombination process.
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TMPH-01569 | KLHDC3 Protein, Human, Recombinant (His & Myc) | Human | Baculovirus | ||
Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. The CRL2(KLHDC3) complex specifically recognizes proteins with a glycine (Gly) at the C-terminus, leading to their ubiquitination and degradation: recognizes the C-terminal -Arg-(Xaa)n-Arg-Gly, -Arg-(Xaa)n-Lys-Gly, and -Arg-(Xaa)n-Gln-Gly degrons. The CRL2(KLHDC3) complex mediates ubiquitination and degradation of truncated SELENOV and SEPHS2 selenoproteins produced by failed UGA/Sec decoding, which end with a glycine. May be involved in meiotic recombination process.
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TMPK-00191 | PILRA Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 | ||
Alzheimer's disease (AD) is a neurodegenerative disease characterized by a progressive decline in cognitive performance; Mild Cognitive Impairment (MCI) is instead an objective decline in cognitive performance that does not reach pathology. Paired immunoglobulin-like type 2 receptor alpha (PILRA) is a cell surface inhibitory receptor that was recently suggested to be involved in AD pathogenesis. In particular, the arginine-to-glycine substitution in position 78 (R78, rs1859788) was shown to be protective against AD.
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TMPK-00150 | FOLR1 Protein, Human, Recombinant (His & Avi) | Human | HEK293 | ||
Folate Receptor 1 (FOLR1), also known as Folate Receptor alpha and Folate Binding Protein (FBP), is a 37 - 42 kDa protein that mediates the cellular uptake of folic acid and reduced folates. Dietary folates are required for many key metabolic processes including nucleotide and methionine synthesis, the interconversion of glycine and serine, and histidine breakdown. FOLR1 binds to folate and reduced folic acid derivatives and mediates delivery of 5-methyltetrahydrofolate and folate analogs into the interior of cells. Has high affinity for folate and folic acid analogs at neutral pH.
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TMPH-03575 | Sortase A Protein, S. aureus, Recombinant (His) | Staphylococcus aureus | E. coli | ||
Transpeptidase that anchors surface proteins to the cell wall. Recognizes and modifies its substrate by proteolytic cleavage of a C-terminal sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the sortase and its substrate, which is then transferred and covalently attached to the cell wall. This sortase recognizes a Leu-Pro-x-Thr-Gly (LPXTG) motif, which is cleaved by the sortase between the threonine and glycine residues. Utilizes lipid II as the peptidoglycan substrate for the sorting reaction. Responsible for the display of important virulence factors. Important for interactions with the host and host colonization during infection.
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TMPJ-00979 | GSH-S Protein, Human, Recombinant (His) | Human | E. coli | ||
Glutathione Synthetase belongs to the eukaryotic GSH synthase family. Glutathione Synthetase is the second enzyme in the glutathione biosynthesis pathway. It catalyses the condensation of gamma-glutamylcysteine and glycine to form glutathione. Glutathione play an important role in a variety of biological functions, including detoxification of xenobiotics, protection of cells from oxidative damage by free radicals, and membrane transport. The protein functions as a homodimer to catalyze the second step of glutathione biosynthesis, which is the ATP-dependent conversion of gamma-L-glutamyl-L-cysteine to glutathione. Defects in Glutathione Synthetase can also cause the glutathione synthetase deficiency of erythrocytes, which is a mild form causing hemolytic anemia.
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TMPJ-00304 | ALK-1 Protein, Mouse, Recombinant (hFc) | Mouse | Human Cells | ||
Activin Receptor-Like Kinase 1 (ALK-1) is a type I cell-surface receptor for the TGF-β superfamily of ligands, which mediates signaling of BMP9 (bone morphogenetic protein) and BMP10. ALK1 signaling is necessary for angiogenesis during embryogenesis, wound healing, and tumor growth. ALK-1 has a high degree of similarity in serine-threonine kinase subdomains, a glycine and serine rich region preceding the kinase-domain, and a C-terminal tail with other activin receptor-like kinase proteins. ALK-1 is mainly expressed in endothelial cells regulating proliferation and migration in vitro and angiogenesis in vivo. Mutations in ALK-1 as well as in endoglin are associated with hereditary hemorrhagic telangiectasia (HHT), suggesting ALK-1 plays a critical role for in the control of blood vessel development or repair.
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TMPY-02332 | UCHL3 Protein, Rat, Recombinant (His) | Rat | E. coli | ||
Ubiquitin carboxyl-terminal hydrolase isozyme L3, also known as UCH-L3, Ubiquitin thioesterase L3 and UCHL3, is a ubiquitin-protein hydrolase that belongs to the peptidase C12 family. It is involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. UCHL3 is highly expressed in heart, skeletal muscle, and testis. UCHL1 and UCHL3 are two of the deubiquitinating enzymes expressed in the brain. These phenotypes indicate the importance of UCHL1 and UCHL3 in the regulation of the central nervous system. UCHL3 functions as a de-ubiquitinating enzyme where lack of its hydrolase activity may result in the prominent accumulation of ubiquitinated proteins and subsequent induction of stress responses in skeletal muscle. UCHL3 has also been identified as a tumor-specific antigen in colon cancer.
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TMPY-05235 | MFGE8 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | Baculovirus-Insect Cells | ||
MFG-E8, also known as lactadherin and MFGE8, contains 1 EGF-like domain and 2 F5/8 type C domains. It also contains phosphatidylserine (PS) binding domain, as well as an Arginine-Glycine-Aspartic acid motif, which enables the binding to integrins. It binds PS, which is exposed on the surface of apoptotic cells. MFG-E8 is expressed in mammary epithelial cell surfaces and aortic media. Overexpression of MFG-E8 can be found in several carcinomas. MFG-E8 has opsonization of the apoptotic cells and binding to integrins on the surface of phagocytic cells. It also mediates the engulfment of the dead cell. MFG-E8 plays an important role in the maintenance of intestinal epithelial homeostasis and the promotion of mucosal healing. It promotes VEGF-dependent neovascularization and contributes to the phagocytic removal of apoptotic cells in many tissues. It also binds to phosphatidylserine-enriched cell surfaces in a receptor-independent manner.
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TMPY-02190 | UCHL3 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Ubiquitin carboxyl-terminal hydrolase isozyme L3, also known as UCH-L3, Ubiquitin thioesterase L3 and UCHL3, is a ubiquitin-protein hydrolase that belongs to the peptidase C12 family. It is involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. UCHL3 is highly expressed in heart, skeletal muscle, and testis. UCHL1 and UCHL3 are two of the deubiquitinating enzymes expressed in the brain. These phenotypes indicate the importance of UCHL1 and UCHL3 in the regulation of the central nervous system. UCHL3 functions as a de-ubiquitinating enzyme where lack of its hydrolase activity may result in the prominent accumulation of ubiquitinated proteins and subsequent induction of stress responses in skeletal muscle. UCHL3 has also been identified as a tumor-specific antigen in colon cancer.
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TMPH-01520 | HIV-1 (group M, subtype K, isolate 96CM-MP535) Protein Vpr (His & Myc) | HIV-1 | E. coli | ||
During virus replication, may deplete host UNG protein, and incude G2-M cell cycle arrest. Acts by targeting specific host proteins for degradation by the 26S proteasome, through association with the cellular CUL4A-DDB1 E3 ligase complex by direct interaction with host VPRPB/DCAF-1. Cell cycle arrest reportedly occurs within hours of infection and is not blocked by antiviral agents, suggesting that it is initiated by the VPR carried into the virion. Additionally, VPR induces apoptosis in a cell cycle dependent manner suggesting that these two effects are mechanistically linked. Detected in the serum and cerebrospinal fluid of AIDS patient, VPR may also induce cell death to bystander cells.; During virus entry, plays a role in the transport of the viral pre-integration (PIC) complex to the host nucleus. This function is crucial for viral infection of non-dividing macrophages. May act directly at the nuclear pore complex, by binding nucleoporins phenylalanine-glycine (FG)-repeat regions.
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TMPH-01519 | HIV-1 (group M, subtype C, isolate 92BR025) Protein Vpr (His & Myc) | HIV-1 | E. coli | ||
During virus replication, may deplete host UNG protein, and incude G2-M cell cycle arrest. Acts by targeting specific host proteins for degradation by the 26S proteasome, through association with the cellular CUL4A-DDB1 E3 ligase complex by direct interaction with host VPRPB/DCAF-1. Cell cycle arrest reportedly occurs within hours of infection and is not blocked by antiviral agents, suggesting that it is initiated by the VPR carried into the virion. Additionally, VPR induces apoptosis in a cell cycle dependent manner suggesting that these two effects are mechanistically linked. Detected in the serum and cerebrospinal fluid of AIDS patient, VPR may also induce cell death to bystander cells.; During virus entry, plays a role in the transport of the viral pre-integration (PIC) complex to the host nucleus. This function is crucial for viral infection of non-dividing macrophages. May act directly at the nuclear pore complex, by binding nucleoporins phenylalanine-glycine (FG)-repeat regions.
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TMPY-01548 | UCHL3 Protein, Human, Recombinant (His) | Human | E. coli | ||
Ubiquitin carboxyl-terminal hydrolase isozyme L3, also known as UCH-L3, Ubiquitin thioesterase L3 and UCHL3, is a ubiquitin-protein hydrolase that belongs to the peptidase C12 family. It is involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. UCHL3 is highly expressed in heart, skeletal muscle, and testis. UCHL1 and UCHL3 are two of the deubiquitinating enzymes expressed in the brain. These phenotypes indicate the importance of UCHL1 and UCHL3 in the regulation of the central nervous system. UCHL3 functions as a de-ubiquitinating enzyme where lack of its hydrolase activity may result in the prominent accumulation of ubiquitinated proteins and subsequent induction of stress responses in skeletal muscle. UCHL3 has also been identified as a tumor-specific antigen in colon cancer.
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TMPY-02840 | Ubiquitin Activating Enzyme E1/UBA1 Protein, Human, Recombinant (His & GST) | Human | Baculovirus-Insect Cells | ||
UBE1, also known as UBA1, belongs to the ubiquitin-activating E1 family. UBE1 gene complements an X-linked mouse temperature-sensitive defect in DNA synthesis, and thus may function in DNA repair. It is part of a gene cluster on chromosome Xp11.23. UBE1 catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation. It also catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP. Defects in UBA1 can cause spinal muscular atrophy X-linked type 2 (SMAX2), also known as X-linked lethal infantile spinal muscular atrophy, distal X-linked arthrogryposis multiplex congenita or X-linked arthrogryposis type 1 (AMCX1). Spinal muscular atrophy refers to a group of neuromuscular disorders characterized by degeneration of the anterior horn cells of the spinal cord, leading to symmetrical muscle weakness and atrophy. SMAX2 is a lethal infantile form presenting with hypotonia, areflexia, and multiple congenital contractures.
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TMPY-01547 | UCHL1 Protein, Human, Recombinant (His) | Human | E. coli | ||
Ubiquitin carboxyl-terminal hydrolase isozyme L1, also known as UCH-L1, Ubiquitin thioesterase L1, PGP9.5 and UCHL1, is a deubiqutinating enzyme with important functions in recycling of ubiquitin. Regulated proteolysis by the ubiquitin pathway has been implicated in control of the cell cycle, transcriptional activation, cell fate and growth, and synaptogenesis. The ubiquitin-proteasome system is involved in synaptic plasticity and is proposed to be part of a molecular switch that converts short-term synaptic potentiation to long-term changes in synaptic strength. UCHL1 is found in neuronal cell bodies and processes throughout the neocortex (at protein level). It is expressed in neurons and cells of the diffuse neuroendocrine system and their tumors. UCHL1 is weakly expressed in ovary. UCHL1 is a ubiquitin-protein hydrolase. It is involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. UCHL1 also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer of UCHL1 may have ATP-independent ubiquitin ligase activity. UCHL1 dysfunction has been associated with neurodegeneration in Parkinson's, Alzheimer's, and Huntington's disease patients. Reduced UCHL1 function may jeopardize the survival of CNS neurons.
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TMPY-02331 | UCHL1 Protein, Rat, Recombinant (His) | Rat | E. coli | ||
Ubiquitin carboxyl-terminal hydrolase isozyme L1, also known as UCH-L1, Ubiquitin thioesterase L1, PGP9.5 and UCHL1, is a deubiqutinating enzyme with important functions in recycling of ubiquitin. Regulated proteolysis by the ubiquitin pathway has been implicated in control of the cell cycle, transcriptional activation, cell fate and growth, and synaptogenesis. The ubiquitin-proteasome system is involved in synaptic plasticity and is proposed to be part of a molecular switch that converts short-term synaptic potentiation to long-term changes in synaptic strength. UCHL1 is found in neuronal cell bodies and processes throughout the neocortex (at protein level). It is expressed in neurons and cells of the diffuse neuroendocrine system and their tumors. UCHL1 is weakly expressed in ovary. UCHL1 is a ubiquitin-protein hydrolase. It is involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. UCHL1 also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer of UCHL1 may have ATP-independent ubiquitin ligase activity. UCHL1 dysfunction has been associated with neurodegeneration in Parkinson's, Alzheimer's, and Huntington's disease patients. Reduced UCHL1 function may jeopardize the survival of CNS neurons.
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TMPY-02175 | UCHL1 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Ubiquitin carboxyl-terminal hydrolase isozyme L1, also known as UCH-L1, Ubiquitin thioesterase L1, PGP9.5 and UCHL1, is a deubiqutinating enzyme with important functions in recycling of ubiquitin. Regulated proteolysis by the ubiquitin pathway has been implicated in control of the cell cycle, transcriptional activation, cell fate and growth, and synaptogenesis. The ubiquitin-proteasome system is involved in synaptic plasticity and is proposed to be part of a molecular switch that converts short-term synaptic potentiation to long-term changes in synaptic strength. UCHL1 is found in neuronal cell bodies and processes throughout the neocortex (at protein level). It is expressed in neurons and cells of the diffuse neuroendocrine system and their tumors. UCHL1 is weakly expressed in ovary. UCHL1 is a ubiquitin-protein hydrolase. It is involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. UCHL1 also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer of UCHL1 may have ATP-independent ubiquitin ligase activity. UCHL1 dysfunction has been associated with neurodegeneration in Parkinson's, Alzheimer's, and Huntington's disease patients. Reduced UCHL1 function may jeopardize the survival of CNS neurons.
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