目录号 | 产品详情 | 靶点 | |
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TN5050 | NADPH-oxidase VEGFR p38 MAPK ROS Akt PI3K mTOR p53 | ||
Sprengerinin C exerts anti-tumorigenic effects in hepatocellular carcinoma via inhibition of proliferation and angiogenesis and induction of apoptosis, it can strongly suppress tumor angiogenesis in human umbilical vein endothelial cells, it blocks vascul | |||
T69477 | |||
F81-1144b is a matrix metalloproteinase inhibitor which reduces secretion of very low density lipoprotein-triacylglycerol, thereby lowering TAG levels in serum and the liver. F81-1144b also lowers VLDL-TAG secretion, de novo FA synthesis in the liver, and serum levels of insulin and glucose. | |||
T38378 | |||
Dnp-PLAYWAR is a fluorogenic substrate for matrix metalloproteinase-8 (MMP-8) and MMP-26. The activity of MMP-8 and MMP-26 can be quantified by measuring tryptophan fluorescence that is unquenched upon peptide hydrolysis that removes the N-terminal dinitrophenol (Dnp) group. | |||
T16291 | COX | ||
NF157 significantly decreases the expression of metalloproteinase (MMP)-3, MMP-13, which can be used in the treatment of osteoarthritis (OA). NF157 is a highly selective nanomolar P2Y11 antagonist (pKi: 7.35). The IC50s are 463 nM, 1811 µM, 170 µM for P2Y | |||
T37025 | |||
Mca-PLAC(p-OMeBz)-WAR(Dpa)-NH2 is a fluorogenic substrate for matrix metalloproteinase-14 (MMP-14). Upon cleavage by MMP-14, 7-methoxycoumarin-4-acetyl (Mca) is released and its fluorescence can be used to quantify MMP activity. Mca displays excitation/emission maxima of 328/420 nm, respectively. | |||
T71995 | |||
Decanoyl Chloride is used in the synthesis of an effective metalloproteinase inhibitor. Also acts as a reagent in the synthesis of reversible α-ketoheterocycle inhibitors of fatty acid amide hydrolase as potnetial analgesics. | |||
T76009 | |||
Thermolysin 是由革兰氏阳性菌 Bacillus thermoproteolyticus 分泌的耐热的中性金属蛋白酶。Thermolysin 可催化含有疏水残基的肽键水解。 | |||
T36360 | |||
Dnp-P-Cha-G-Cys(Me)-HA-K(Nma)-NH2 is a fluorogenic substrate for matrix metalloproteinase-1 (MMP-1) and MMP-9. Upon cleavage by MMP-1 or MMP-9, N-methylanthranilic acid (Nma) is unquenched and its fluorescence can be used to quantify MMP activity. Nma displays excitation/emission spectra of 340/440 nm, respectively. | |||
T36962 | |||
MMP inhibitor I is a peptide inhibitor of matrix metalloproteinase-1 (MMP-1), MMP-2, and MMP-3 (IC50s = 1.3, 30, and 150 μM, respectively). It is selective for MMP-1, MMP-2, and MMP-3 over the proteases thermolysin, urease, trypsin, α-chymotrypsin, plasmin, and elastase at concentrations up to 4 mM. | |||
TN1832 | Others NF-κB Tyrosinase | ||
Kanzonol C has antimicrobial activity, it also shows potent PTP1B inhibitory activity (IC50 value of 0.31-0.97uM). Kanzonol C has chemopreventive activity,it shows the inhibition of matrix metalloproteinase (MMP)-2 secretion from brain tumor-derived glioblastoma cells. |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPJ-00916 | TIMP-2 Protein, Mouse, Recombinant (His) | Mouse | HEK293 Cells | ||
Mouse Metalloproteinase inhibitor 2(TIMP-2), belongs to a family of proteins that regulate the activation and proteolytic activity of matrix metalloproteinases (MMPs). There are four mammalian members of the family; TIMP‑1, TIMP‑2, TIMP‑3, and TIMP‑4. The TIMP-2 is detected in testis, retina, hippocampus and cerebral cortex. The function of TIMP 2 protein is to inhibit MMPs non covalently by the formation of binary complexes. Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor.And the interaction with MMP-14 facilitates the activation of pro-MMP-2.It has been shown that the binding of TIMP 2 to a3b1 integrin results in the inhibition of endothelial cell proliferation and angiogenesis.
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TMPH-03166 | Elastase Protein, Pseudomonas aeruginosa, Recombinant (His & SUMO) | Pseudomonas aeruginosa | E. coli | ||
Cleaves host elastin, collagen, IgG, and several complement components as well as endogenous pro-aminopeptidase. Autocatalyses processing of its pro-peptide. Processes the pro-peptide of pro-chitin-binding protein (cbpD). Involved in the pathogenesis of P.aeruginosa infections. Elastase Protein, Pseudomonas aeruginosa, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 49.1 kDa and the accession number is P14756.
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TMPJ-00942 | MMP-12 Protein, Mouse, Recombinant (His) | Mouse | HEK293 Cells | ||
Matrix metalloproteinase-12(MMP12) is a secreted protein.It contains 4 hemopexin repeats and belongs to the peptidase M10A family. MMP12 may be involved in tissue injury and remodeling and have significant elastolytic activity. It can accept large and small amino acids at the P1' site, but has a preference for leucine. Aromatic or hydrophobic residues are preferred at the P1 site, with small hydrophobic residues (preferably alanine) occupying P3.
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TMPH-02402 | Zinc metalloproteinase Protein, Legionella pneumophila, Recombinant (His) | Legionella pneumophila | E. coli | ||
Cleaves collagen, gelatin, casein, alpha-1-antitrypsin, and bovine insulin. May play a role in the pathogenesis of legionnaires disease.
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TMPJ-01289 | TIMP-4 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
Metalloproteinase inhibitor 4 is an enzyme that in humans is encoded by the TIMP4 gene, belongs to the protease inhibitor I35 (TIMP) family. The protein complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7 and MMP-9.
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TMPH-01234 | ADAM33 Protein, Human, Recombinant (His) | Human | Baculovirus Insect Cells | ||
ADAM33 Protein, Human, Recombinant (His) is expressed in Baculovirus with C-terminal 6xHis tag. The predicted molecular weight is 78.0 kDa. Accession number: Q9BZ11
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TMPH-02629 | ADAM12 Protein, Mouse, Recombinant (His & Myc) | Mouse | Baculovirus Insect Cells | ||
Involved in skeletal muscle regeneration, specifically at the onset of cell fusion. Also involved in macrophage-derived giant cells (MGC) and osteoclast formation from mononuclear precursors. ADAM12 Protein, Mouse, Recombinant (His & Myc) is expressed in Baculovirus insect cells with N-10xHis and C-Myc tag. The predicted molecular weight is 58.4 kDa and the accession number is Q61824.
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TMPH-03580 | Zinc metalloproteinase aureolysin Protein, S. aureus, Recombinant (His & Myc) | Staphylococcus aureus | E. coli | ||
Zinc metalloproteinase aureolysin Protein, S. aureus, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 40.2 kDa and the accession number is P81177.
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TMPJ-00447 | MMP-3 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
MMP3 is a member of the matrix metalloproteinase (MMP) family whose members are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, tissue remodeling, and disease processes including arthritis and metastasis. The MMP-3 enzyme degrades collagen types II, III, IV, IX, and X, proteoglycans, fibronectin, laminin, and elastin. In addition, MMP-3 can also activate other MMPs such as MMP-1, MMP-7, and MMP-9, rendering MMP-3 crucial in connective tissue remodeling.[3] The enzyme is thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation.
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TMPJ-00101 | TIMP-2 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
Tissue inhibitors of metalloproteinases or TIMPs are a family of proteins that regulate the activation and proteolytic activity of the zinc enzymes known as matrix metalloproteinases (MMPs). There are four members of the family, TIMP-1, TIMP-2, TIMP-3, and TIMP-4. Tissue Inhibitor of Metalloproteinases 2 (TIMP-2) is a non N-glycosylated protein with a molecular mass of 22 kDa. It produced by a wide range of cell types, which inhibits MMPs non-covalently by the formation of binary complexes and irreversibly inactivates them by binding to their catalytic zinc cofactor. TIMP-2 also has erythroid‑potentiating and cell growth promoting activities.
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TMPH-00868 | ADAMTS7 Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
Metalloprotease that may play a role in the degradation of COMP. ADAMTS7 Protein, Human, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 52.1 kDa and the accession number is Q9UKP4.
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TMPJ-00957 | MMP-9 Protein, Mouse, Recombinant (His) | Mouse | HEK293 Cells | ||
Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-9 (gelatinase B) can degrade a broad range of substrates including gelatin, collagen types IV and V, elastin and proteoglycan core protein. It is believed to act synergistically with interstitial collagenase (MMP1) in the degradation of fibrillar collagens as it degrades their denatured gelatin forms. MMP-9 is produced by keratinocytes, monocytes, macrophages and PMN leukocytes. MMP-9 is present in most cases of inflammatory responses. Structurally, MMP-9 may be divided into five distinct domains: a prodomain which is cleaved upon activation, a gelatinbinding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a prolinerich linker region, and a carboxyl terminal hemopexinlike domain.
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TMPH-00866 | ADAMTS14 Protein, Human, Recombinant (His) | Human | E. coli | ||
Has aminoprocollagen type I processing activity in the absence of ADAMTS2. Seems to be synthesized as a latent enzyme that requires activation to display aminoprocollagen peptidase activity. Cleaves lysyl oxidase LOX at a site downstream of its propeptide cleavage site to produce a short LOX form. ADAMTS14 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 40.2 kDa and the accession number is Q8WXS8.
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TMPJ-00362 | MMP-2 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
72 kDa type IV collagenase also known as matrix metalloproteinase-2 (MMP-2) and gelatinase A is an enzyme that in humans is encoded by the MMP2 gene.It belongs to the matrix metalloproteinase (MMP) family. Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade components of the extracellular matrix (ECM) and play essential roles in various physiological processes such as morphogenesis, differentiation, angiogenesis and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases and tumor invasion. MMP-2 is ubiquitinous metalloproteinase that is involved in diverse functions such as remodeling of the vasculature, angiogenesis, tissue repair, tumor invasion, inflammation, atherosclerotic plaque rupture, as well as degrading extracellular matrix proteins. MMP-2 can also act on several nonmatrix proteins such as big endothelial 1 and beta-type CGRP promoting vasoconstriction. MMP-2 cleaves KISS at a Gly-|-Leu bond and appears to have a role in myocardial cell death pathways.
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TMPH-00867 | ADAMTS4 Protein, Human, Recombinant (GST) | Human | E. coli | ||
Cleaves aggrecan, a cartilage proteoglycan, and may be involved in its turnover. May play an important role in the destruction of aggrecan in arthritic diseases. Could also be a critical factor in the exacerbation of neurodegeneration in Alzheimer disease. Cleaves aggrecan at the '392-Glu-|-Ala-393' site. ADAMTS4 Protein, Human, Recombinant (GST) is expressed in E. coli expression system with N-GST tag. The predicted molecular weight is 39.0 kDa and the accession number is O75173.
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TMPH-02493 | ADAMDEC1 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
May play an important role in the control of the immune response and during pregnancy. ADAMDEC1 Protein, Mouse, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 34.9 kDa and the accession number is Q9R0X2.
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TMPH-00869 | ADAMTS7 Protein, Human, Recombinant (His) | Human | P. pastoris (Yeast) | ||
Metalloprotease that may play a role in the degradation of COMP. ADAMTS7 Protein, Human, Recombinant (His) is expressed in yeast with N-6xHis tag. The predicted molecular weight is 41.1 kDa and the accession number is Q9UKP4.
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TMPJ-00665 | ADAMDEC1 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
ADAM DEC1 protein is expressed highly in the small intestine and appendix, moderately in lymph node, mucosal lining of the colon, thymus, spleen and very weakly in the bone marrow. ADAM DEC1 is induced during DC maturation and up-regulated in response to T-cell signals. It may play an important role in the control of the immune response and during pregnancy.
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TMPH-00998 | CD147 Protein, Human, Recombinant (aa 138-323, hFc) | Human | HEK293 Cells | ||
CD147 Protein, Human, Recombinant (aa 138-323, hFc) is expressed in HEK293.
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TMPH-02485 | ADAMTS5 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
ADAMTS5 Protein, Mouse, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 77.8 kDa and the accession number is Q9R001.
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TMPJ-00160 | EMMPRIN/CD147 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
Extracellular Matrix Metalloproteinase Inducer (EMMPRIN) belongs to the immunoglobulin superfamily, which has the homology to both the immunoglobulin V domain and MHC class II antigen β-chain. EMMPRIN is a transmembrane glycoprotein with different forms, resulting from different modes of glycosylation and N-terminal sequence variants. EMMPRIN can be expressed in breast cancer, oral squamous cell carcinoma, glioma, lymphoma, lung, bladder, and melanoma carcinomas cells. EMMPRIN promotes invasion, metastasis, growth, and survival of malignants cells, serves as a receptor for extracellular cyclophilinthe, may play a role in signal transduction.
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TMPH-02484 | ADAMTS13 Protein, Mouse, Recombinant (His & Myc) | Mouse | E. coli | ||
Cleaves the vWF multimers in plasma into smaller forms thereby controlling vWF-mediated platelet thrombus formation. ADAMTS13 Protein, Mouse, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 32.7 kDa and the accession number is Q769J6.
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TMPY-05716 | Integrin alpha V beta 3 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
Integrin alpha-V & beta-3 (ITGAV/ITGB3) is a receptor for cytotactin, fibronectin, laminin, matrix metalloproteinase-2, osteopontin, osteomodulin, prothrombin, thrombospondin, vitronectin and von Willebrand factor.
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TMPY-02869 | MMP-12 Protein, Human, Recombinant (catalytic domain) | Human | E. coli | ||
Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases that degrade components of the extracellular matrix (ECM) and play essential roles in various physiological processes such as morphogenesis, differentiation, angiogenesis, and tissue remodeling, as well as pathological processes including inflammation, arthritis, cardiovascular diseases, pulmonary diseases, and tumor invasion. Macrophage Metalloelastase, also known as Matrix metalloproteinase-12, Macrophage elastase, MMP12, and MMP-12, is a secreted protein that belongs to the peptidase M1A family. MMP12 is a macrophage-secreted elastase that is highly induced in the liver and lung in response to S. mansoni eggs and contains four hemopexin-like domains. MMP12 is a proteolytic enzyme responsible for the cleavage of plasminogen to angiotensin, which has an angiostatic effect. It may be involved in tissue injury and remodeling and has significant elastolytic activity. It may be related to prognosis in breast cancer patients. MMP12 promotes fibrosis by limiting the expression of specific ECM-degrading MMPs. Like MMP12, MMP13 expression is highly dependent on IL-13 and type I I-IL-4 receptor signaling. MMP12 is a potent proinflammatory and oncogenic molecule. MMP12 up-regulation plays a critical role in emphysema to lung cancer transition that is facilitated by inflammation.
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TMPH-00216 | SVMP Protein, Bothrops jararaca, Recombinant (His & KSI) | Bothrops jararaca | E. coli | ||
Metalloproteinase that binds to von Willebrand factor (VWF) and induces its interaction with GPIb (GP1BA), resulting in platelet aggregation. SVMP Protein, Bothrops jararaca, Recombinant (His & KSI) is expressed in E. coli expression system with N-6xHis-KSI tag. The predicted molecular weight is 18.0 kDa and the accession number is P22028.
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TMPK-00553 | ADAM9 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 Cells | ||
A disintegrin and metalloproteinase 9 (ADAM9) is a member of the transmembrane ADAM family. It is expressed in different types of solid cancer and promotes tumor invasiveness. ADAM9 may be a prognostic marker for vestibular schwannomas (VS), and ADAM9 inhibition might have the potential as a systemic approach for the treatment of VS.
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TMPK-00367 | MMP-9 Protein, Human, Recombinant (His & Avi) | Human | HEK293 Cells | ||
Matrix metalloproteinase 9 (MMP9) contributes to this process and deficiencies in the MMP9 lead to impaired healing. Inappropriate expression of MMP9 also contributes to impaired re-epithelialization. Previously we demonstrated that FOXO1 was activated in wound healing but to higher levels in diabetic wounds. To address mechanisms of impaired re-epithelialization we examined MMP9 expression in vivo in full thickness dermal scalp wounds created in experimental K14. MMP-9 Protein, Human, Recombinant (His & Avi) is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 79.3 kDa and the accession number is P14780.
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TMPK-01334 | EMMPRIN/CD147 Protein, Canine, Recombinant (His) | Canine | HEK293 Cells | ||
CD147, also known as extracellular matrix metalloproteinase inducer (EMMPRIN) or basigin, is expressed in a variety of cell types. It is involved in the regulation of extracellular matrix (ECM) remodeling during physiological and pathological processes including wound healing, inflammatory diseases, and cancer. CD147 is a diagnostic and therapeutic target in cancer and inflammatory diseases, either directly or indirectly, by targeting CD147 partners.
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TMPK-00933 | ADAM8/CD156a Protein, Mouse, Recombinant (His) | Mouse | HEK293 Cells | ||
A Disintegrin And Metalloproteinase (ADAM) proteases constitute a family of multifunctional, membrane-bound proteins with traditional sheddase functions. Their protumorigenic potential has been attributed to both, essential (ADAM10 and ADAM17) and 'dispensable' ADAM proteases (ADAM8, 9, 12, 15, and 19). Of specific interest in this review is the ADAM proteinase ADAM8 that has been identified as a significant player in aggressive malignancies including breast, pancreatic, and brain cancer. ADAM8/CD156a Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 71.7 kDa and the accession number is Q05910.
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TMPY-04671 | MCP-5 Protein, Mouse, Recombinant (His) | Mouse | P. pastoris (Yeast) | ||
Ccl12 prevented initiation of the reparative response by prolonging inflammation and inhibiting fibroblast conversion to myofibroblasts, resulting in diminished scar formation. Macrophage secretion of Ccl12 directly impaired fibronectin and collagen deposition and indirectly stimulated collagen degradation through upregulation of matrix metalloproteinase-2. In post-MI patients, circulating LPS levels strongly associated with the Ccl12 homologue monocyte chemotactic protein 1 (MCP-1). Both MCP-1 and MCP-5 are HIF-1 target genes and that HIF-1alpha is involved in transcriptional induction of these two chemokines in astrocytes by hypoxia.
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TMPK-00918 | ADAM8/CD156a Protein, Human, Recombinant (aa 17-655, His) | Human | HEK293 Cells | ||
A Disintegrin And Metalloproteinase (ADAM) proteases constitute a family of multifunctional, membrane-bound proteins with traditional sheddase functions. Their protumorigenic potential has been attributed to both, essential (ADAM10 and ADAM17) and 'dispensable' ADAM proteases (ADAM8, 9, 12, 15, and 19). Of specific interest in this review is the ADAM proteinase ADAM8 that has been identified as a significant player in aggressive malignancies including breast, pancreatic, and brain cancer. ADAM8/CD156a Protein, Human, Recombinant (aa 17-655, His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 70.9 kDa and the accession number is P78325.
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TMPH-00217 | SVMP Protein, Bothrops leucurus, Recombinant (His & Myc) | Bothrops leucurus | E. coli | ||
Non-hemorrhagic metalloproteinase that hydrolyzes the alpha chains of fibrinogen, as well as fibrin, fibronectin and casein. Beta and gamma chains are also hydrolyzed, but more slowly. Thrombolytic activity is also observed. Induces detachment of endothelial cells followed by death, and inhibits endothelial cell adhesion to fibronectin. Induces edema in mouse paw. Inhibits ADP-induced platelet aggregation on human platelet-rich plasma with an IC(50) of 2.8 uM. SVMP Protein, Bothrops leucurus, Recombinant (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 30.5 kDa and the accession number is P84907.
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TMPK-00368 | MMP-9 Protein, Human, Recombinant (His & Avi), Biotinylated | Human | HEK293 Cells | ||
Matrix metalloproteinase 9 (MMP9) contributes to this process and deficiencies in the MMP9 lead to impaired healing. Inappropriate expression of MMP9 also contributes to impaired re-epithelialization. Previously we demonstrated that FOXO1 was activated in wound healing but to higher levels in diabetic wounds. To address mechanisms of impaired re-epithelialization we examined MMP9 expression in vivo in full thickness dermal scalp wounds created in experimental K14. MMP-9 Protein, Human, Recombinant (His & Avi), Biotinylated is expressed in HEK293 mammalian cells with C-His-Avi tag. The predicted molecular weight is 79.3 kDa and the accession number is P14780.
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TMPK-00503 | MMP-9 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 Cells | ||
Matrix metalloproteinase 9 (MMP9) contributes to this process and deficiencies in the MMP9 lead to impaired healing. Inappropriate expression of MMP9 also contributes to impaired re-epithelialization. Previously we demonstrated that FOXO1 was activated in wound healing but to higher levels in diabetic wounds. To address mechanisms of impaired re-epithelialization we examined MMP9 expression in vivo in full thickness dermal scalp wounds created in experimental K14. MMP-9 Protein, Cynomolgus, Recombinant (His) is expressed in HEK293 mammalian cells with C-His tag. The predicted molecular weight is 77.44 kDa and the accession number is A0A2K5UU71.
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TMPY-02965 | MMP-19 Protein, Human, Recombinant | Human | E. coli | ||
MMP19, also known as RASI-1, is a member of the peptidase M1A family. It contains 4 hemopexin-like domains and is expressed in the mammary gland, placenta, lung, pancreas, ovary, small intestine, spleen, thymus, prostate, testis colon, heart, and blood vessel walls. It is a matrix metalloproteinase (MMP). Proteins of the MMP family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP19 may play a role in pathological processes participating in rheumatoid arthritis (RA)-associated joint tissue destruction. Autoantigen anti-MMP19 is frequent in RA patients.
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TMPJ-00277 | NgR3 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
Nogo-66 Receptor-Related Protein 3 (NgR3) has primary structures with NgR2 (NgRH1, NgRL3) and biochemical properties that are homologous to Nogo-66 receptor (NgR), and constitute a novel neuronal receptor protein family. NgR is GPI-anchored and contains eight leucine-rich repeats (LRR), it is the neuronal receptor for the myelin- associated proteins Nogo-A, OMgp (oligodendrocyte myelin glycoprotein), and MAG (myelin-associated glycoprotein) and mediates the inhibition of CNS axonal regeneration both in vitro and in vivo. NgR2 and NgR3 have similar structure and distinct but overlapping expression versus NgR. NgR2 can be metalloproteinase-cleaved to release a soluble ectodomain. NgR2 has also been shown to bind MAG, but ligands for NgR3 have not yet been determined. Mature huaman NgR3 shares 88%, 88%, 48% and 44% amino acid identity with mature mouse NgR3, rat NgR3, human NgRH1 and NgR, repectively.
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TMPY-02689 | MMP-3 Protein, Human, Recombinant | Human | E. coli | ||
Matrix metallopeptidase 3 (abbreviated as MMP3) is also known as stromelysin 1 and progelatinase. MMP3 is a member of the matrix metalloproteinase (MMP) family whose members are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, tissue remodeling, and disease processes including arthritis and metastasis. As a secreted zinc-dependent endopeptidase, MMP3 exerts its functions mainly in the extracellular matrix. This protein is activated by two major endogenous inhibitors: alpha2-macroglobulin and tissue inhibitors of metalloproteases (TIMPs). MMP3 plays a central role in degrading collagen types II, III, IV, IX, and X, proteoglycans, fibronectin, laminin, and elastin. Also, MMP3 can active other MMPs such as MMP1, MMP7, and MMP9, rendering MMP3 crucial in connective tissue remodeling. Dysregulation of MMPs has been implicated in many diseases including arthritis, chronic ulcers, encephalomyelitis, and cancer. Synthetic or natural inhibitors of MMPs result in inhibition of metastasis, while up-regulation of MMPs led to enhanced cancer cell invasion.
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TMPJ-00082 | NGAL/Lipocalin-2 Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 Cells | ||
Lipocalin-2, also known as Neutrophil Gelatinase-Associated Lipocalin (NGAL), is a secretory protein of the lipocalin superfamily. Lipocalin-2 contains a signal peptide that enables it to be secreted and form complexes with matrix metalloproteinase-9 (MMP-9) through disulfide bonds. Similar to other lipocalin family members, Lipocalin-2 is involved in diverse cellular processes, including the transport of small hydrophobic molecules, protection of MMP-9 from proteolytic degradation, and cell signaling. Furthermore, Lipocalin-2 can tightly bind to bacterial siderophore through a cell surface receptor, possibly serving as a potent bacteriostatic agent by sequestering iron, regulating innate immunity and protecting kidney epithelial cells from ischemia–reperfusion injury. This protein is mainly expressed in neutrophils and in lower levels in the kidney, prostate, and epithelia of the respiratory and alimentary tracts.Recent evidence also suggests its role as a biomarker for renal injury and inflammation.
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TMPJ-00605 | GPVI Protein, Mouse, Recombinant (His) | Mouse | HEK293 Cells | ||
Glycoprotein VI (GPVI) is a 63 kDa platelet/megakaryocyte-specific type I transmembrane glycoprotein of the immunoglobulin superfamily that is an important collagen receptor and initiator of platelet activation, aggregation and thrombin generation. GPVI is also a secondary receptor required for platelet spreading on laminin. GPVI associates with the Fc receptor gamma -chain via charged aa in the TM domains of GPVI (arginine) and the FcR gamma (aspartic acid). Collagen binding by the GPVI Ig-like domains initiates signaling through the FcR gamma ITAM sequence. Dimerization of GPVI (2:2 with FcR gamma ) and N-glycosylation greatly enhances collagen binding. Type I and III collagens are strong thrombus-forming components in the vascular subendothelium and atherosclerotic plaques. GPVI initiates binding to fibrillar collagens under flow conditions, then activates integrin alpha 2 beta 1 which binds collagen more tightly. GPVI deficiencies cause only a mild bleeding tendency, probably because integrin alpha 2 beta 1 is able to minimally initiate collagen binding. Normal human GPVI concentration can vary widely and affect maximum thrombin generation. Engagement of GPVI by collagens or other agonists, including autoantibodies, causes calmodulin-regulated metalloproteinase cleavage of the 57 kDa ECD and depletes surface GPVI.
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TMPY-00886 | MMP-1 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
MMP1, also known as MMP-1, contains 4 hemopexin-like domains and is a member of the matrix metalloproteinase (MMP) family. Matrix metalloproteases, also called matrixins, are zinc-dependent endopeptidases that are the major proteases involved in ECM degradation. MMPs are capable of degrading a wide range of extracellular molecules and some bioactive molecules. MMP activity is regulated by two major endogenous inhibitors: alpha2-macroglobulin and tissue inhibitors of metalloproteases (TIMPs). MMPs play a central role in cell proliferation, migration, differentiation, angiogenesis, apoptosis, and host defenses. Dysregulation of MMPs has been implicated in many diseases including arthritis, chronic ulcers, encephalomyelitis, and cancer. Tumour metastasis is a multistep process involving the dissemination of tumor cells from the primary tumor to secondary at a distant organ or tissue. One of the first steps in metastasis is the degradation of the basement membrane, a process in which MMPs have been implicated. MMPs are secreted by tumor cells themselves or by surrounding stromal cells stimulated by the nearby tumor. Numerous studies have linked altered MMP expression in different human cancers with poor disease prognosis. MMP-1, -2, -3, -7, -9, -13 and -14 all have elevated expression in primary tumors and/or metastases. MMP-1 cleaves collagens of types I, II, and III at one site in the helical domain. It also cleaves collagens of types VII and X. In case of HIV infection, MMP1 interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity.
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