目录号 | 产品详情 | 靶点 | |
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T37713 | |||
Funalenone is a phenalenone originally isolated from A. niger. It inhibits HIV-1 integrase (IC50 = 10 μM) and HIV-1 replication in human peripheral blood cells transformed by murine leukemia virus (HPB-M(a); IC50 = 1.7 μM) but is less cytotoxic to mammalian HPB-M(a) cells (IC50 = 87 μM). Funalenone selectively inhibits matrix metalloproteinase-1 (MMP-1; IC50 = 170 μM) over MMP-2 and MMP-9, which it inhibits by 18.3 and 38.2%, respectively, when used at a concentration of 400 μM. It also inhibits the bacterial cell wall synthesis enzymes MraY and MurG (IC50s = 25.5 μM in a membrane plate assay) and inhibits growth of S. aureus with a MIC value of 64 μg/mL. | |||
T36408 | |||
Rhein-13C4 is intended for use as an internal standard for the quantification of rhein by GC- or LC-MS. Rhein is an anti-inflammatory anthraquinone found in rhubarb and is the bioactive derivative of its prodrug diacerein . At 10 μM, rhein inhibits IL-1β signaling, suppressing signaling through NF-κB, and reduces the expression of the matrix metalloproteases MMP-1 and MMP-13.1 It inhibits IKKβ (IC50 = 11.8 μM), decreasing iNOS and IL-6 expression in LPS-stimulated macrophages but paradoxically increasing TNF-α, IL-1β, and HMBG1 expression.2 Rhein shows efficacy against pancreatic fibrosis, chronic pancreatitis, and hyperglycemia-induced pancreatic β-cell apoptosis.3,4 It also inhibits angiogenesis of breast cancer cells under normoxic and hypoxic conditions.5 | |||
T82150 | |||
Hyaluronan-IN-1是一种具有生物活性的12个氨基酸构成的肽类透明质酸(HA)抑制剂,HA为广泛存在于细胞外基质及细胞表面的高分子糖胺聚糖。该肽特异性地与可溶性、固定化及细胞相关的HA形态结合,能几乎完全抑制白细胞与HA底物的粘附。 | |||
T36531 | |||
PAR2 (1-6) is a synthetic peptide agonist of proteinase-activated receptor 2 (PAR2) that corresponds to residues 1-6 of the amino terminal tethered ligand sequence of mouse and rat PAR2. It also corresponds to residues 39-44 and 37-42 of the mouse and rat full-length sequences, respectively. PAR2 (1-6) induces relaxation in precontracted rat arteries in a concentration-dependent manner, an effect that can be reduced by the nitric oxide synthase inhibitor L-NNA . It inhibits keratinocyte growth in the presence and absence of growth factors. PAR2 (1-6) inhibits LPS-induced pulmonary neutrophil influx and increases in matrix metalloproteinase-2 (MMP-2) activity in mice. | |||
T62090 | |||
Rac)-Tanomastat ((Rac)-BAY 12-9566) 是 Tanomastat 的外消旋体。其中 Tanomastat (BAY 12-9566) 是一种口服具有活力的、含锌羧基的非肽联苯基质金属蛋白酶(MMPs)抑制剂,能够抑制 MMP-2 (Ki: 11 nM)、MMP-3 (Ki: 143 nM)、MMP-9 (Ki: 301 nM)、MMP-13 (Ki: 1470 nM)。在几种实验性肿瘤模型中,Tanomastat 表现出抗侵袭和抗转移作用。 | |||
T82151 | |||
Hyaluronan-binding peptide, biotin labeled 是通过 C 端 GGGSK 残基生物素化的透明质酸结合肽,能够干预 HA 与 CD44 受体的作用,并阻碍 T 细胞增殖。 HA 在细胞外基质和细胞表面广泛表达,参与多种生物过程,包括受精、胚胎发育、伤口修复、血管新生、炎症反应和肿瘤转移。 | |||
T36844 | |||
Inostamycin A is a bacterial metabolite that has been found inStreptomycesand has anticancer activity.1It is an inhibitor of CDP-diacylglycerol:inositol 3-phosphatidyltransferase (IC50= 0.02 μg/ml in A431 cell membranes) and is selective for CDP-diacylglycerol:inositol 3-phosphatidyltransferase over phospholipase C (PLC) and phosphatidylinositol kinase at 10 μg/ml.2Inostamycin A decreases viability of YCU-T892, KCC-TC873, KB, HSC-4, and YCU-T891 oral squamous cell carcinoma (OSCC) cells in a concentration-dependent manner.3It induces cell cycle arrest in the G1phase in HSC-4 cells when used at a concentration of 250 ng/ml and induces apoptosis in Ms-1 small cell lung cancer cells at 300 ng/ml.3,4Inostamycin A also reduces levels of matrix metalloproteinase-2 (MMP-2) and MMP-9 and inhibits EGF-induced migration of HSC-4 cells.5 1.Imoto, M., Umezawa, K., Takahashi, Y., et al.Isolation and structure determination of inostamycin, a novel inhibitor of phosphatidylinositol turnoverJ. Nat. Prod.53(4)825-829(1990) 2.Imoto, M., Taniguchi, Y., and Umezawa, K.Inhibition of CDP-DG: inositol transferase by inostamycinJ. Biochem.112(2)299-302(1992) 3.Baba, Y., Tsukuda, M., Mochimatsu, I., et al.Cytostatic effect of inostamycin, an inhibitor of cytidine 5'-diphosphate 1,2-diacyl-sn-glycerol (CDP-DG): inositol transferase, on oral squamous cell carcinoma cell linesCell Biol. Int.25(7)613-620(2001) 4.Imoto, M., Tanabe, K., Simizu, S., et al.Inhibition of cyclin D1 expression and induction of apoptosis by inostamycin in small cell lung carcinoma cellsJpn. J. Cancer Res.89(3)315-322(1998) 5.Baba, Y., Tsukuda, M., Mochimatsu, I., et al.Inostamycin, an inhibitor of cytidine 5'-diphosphate 1,2-diacyl-sn-glycerol (CDP-DG): Inositol transferase, suppresses invasion ability by reducing productions of matrix metalloproteinase-2 and -9 and cell motility in HSC-4 tongue carcinoma cell lineClin. Exp. Metastasis18(3)273-279(2000) | |||
T78018 | |||
Plasminogen是一种可由尿激酶血浆蛋白原激活剂(uPA)或组织血浆蛋白原激活剂(tPA)裂解激活的分泌性蛋白,生成血浆蛋白,该酶可以广泛裂解纤维蛋白及其他ECM成分。作为促炎调节剂,Plasminogen能促进急性及糖尿病相关伤口愈合。该蛋白在伤口愈合、炎症和低纤溶酶原血症的研究中有重要应用。 | |||
T37631 | |||
12(S)-HETE is a product of arachidonic acid metabolism through the 12-lipoxygenase pathway. It is primarily found in platelets, leukocytes, and to a lesser extent in smooth muscle cells. It enhances tumor cell adhesion to endothelial cells, fibronectin, and the subendothelial matrix. tetranor-12(S)-HETE is the major β-oxidation product resulting from peroxisomal metabolism of 12(S)-HETE in numerous tissues, and Lewis lung carcinoma cells. No biological function has yet been determined for tetranor-12(S)-HETE. Some data indicate it may play a role in controlling the inflammatory response in injured corneas. In some diseases (e.g., Zellweger's Syndrome) peroxisomal abnormalities result in the inability of cells to metabolize 12(S)-HETE, which may be responsible for symptoms of the disease. The tetranor derivative of 12(S)-HETE is available as a research tool for the elucidation of the metabolic fate of its parent compound. | |||
T69995 | |||
Chlorhexidine-d8 is intended for use as an internal standard for the quantification of chlorhexidine by GC- or LC-MS. Chlorhexidine is a bis(biguanide) antimicrobial disinfectant and antiseptic agent. It inhibits growth of clinical methicillin-resistant S. aureus (MRSA) isolates (MIC90 = 4 μg/ml). It is also active against canine isolates of MRSA, methicillin-susceptible S. aureus (MSSA), methicillin-resistant S. pseudintermedius (MRSP), and methicillin-susceptible S. pseudintermedius (MSSP; MIC90s = 4, 2, 2, and 1 mg/L, respectively). Chlorhexidine inhibits growth of E. faecium strains (MICs = 1.2-19.6 μg/ml) and C. albicans (MIC = 5.15 μg/ml). It generates cations that bind to and destabilize the bacterial cell wall to induce death.6 Chlorhexidine also completely inhibits matrix metalloproteinase-2 (MMP-2) and MMP-9 when used at concentrations of 0.0001 and 0.002%, respectively, in a gelatin degradation assay. Formulations containing chlorhexidine have been used in antisept...... |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-00065 | Ebola virus EBOV (subtype Bundibugyo, strain Uganda 2007) VP40/Matrix protein VP40 Protein (His) | EBOV | E. coli | ||
Ebola virus EBOV (subtype Bundibugyo, strain Uganda 2007) VP40/Matrix protein VP40 Protein (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 34.4 kDa and the accession number is B8XCM9.
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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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TMPY-01884 | MMP-8 Protein, Human, Recombinant | Human | HEK293 Cells | ||
MMP-8 Protein, Human, Recombinant is expressed in HEK293 mammalian cells. The predicted molecular weight is 52 kDa and the accession number is P22894.
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TMPY-00888 | MMP-9 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
MMP-9 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 77.7 kDa and the accession number is P14780.
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TMPY-01248 | MMP-9 Protein, Human, Recombinant | Human | HEK293 Cells | ||
MMP-9 Protein, Human, Recombinant is expressed in HEK293 mammalian cells. The predicted molecular weight is 76.3 kDa and the accession number is P14780.
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TMPY-01477 | MMP-2 Protein, Human, Recombinant | Human | HEK293 Cells | ||
MMP-2 Protein, Human, Recombinant is expressed in HEK293 mammalian cells. The predicted molecular weight is 72 kDa and the accession number is A0A024R6R4.
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TMPY-01919 | MMP-9 Protein, Mouse, Recombinant | Mouse | HEK293 Cells | ||
MMP-9 Protein, Mouse, Recombinant is expressed in HEK293 mammalian cells. The predicted molecular weight is 78.4 kDa and the accession number is P41245-1.
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TMPY-02054 | MMP-9 Protein, Rat, Recombinant (His) | Rat | HEK293 Cells | ||
MMP-9 Protein, Rat, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 77.8 kDa and the accession number is A6JXD0.
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TMPY-04100 | MMP-26 Protein, Human, Recombinant | Human | E. coli | ||
MMP26 (Matrix Metallopeptidase 26) is a Protein Coding gene. MMP26 is a member of matrix metalloproteinases (MMPs) and has been reported to be highly expressed in many cancers. The protein differs from most MMP family members in that it lacks a conserved C-terminal protein domain. It may hydrolyze collagen type IV, fibronectin, fibrinogen, beta-casein, type I gelatin, and alpha-1 proteinase inhibitor, and is also able to activate progelatinase B. MMP26 is a target gene of miR-125b, and the expression profile of MMP26 showed an inverse relationship with miR-125b in vivo and in vitro. The overexpression of MMP26 in SW1353 cells increased cell invasiveness, while inhibition of MMP26 decreased cell invasiveness.
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TMPY-00333 | ECM1 Protein, Rat, Recombinant (His) | Rat | HEK293 Cells | ||
ECM1 Protein, Rat, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 62.9 kDa and the accession number is A6K307.
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TMPY-01844 | MMP-8 Protein, Mouse, Recombinant | Mouse | HEK293 Cells | ||
MMP-8 Protein, Mouse, Recombinant is expressed in HEK293 mammalian cells. The predicted molecular weight is 52 kDa and the accession number is O70138.
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TMPY-00520 | MMP-8 Protein, Mouse, Recombinant (His) | Mouse | CHO Cells | ||
MMP-8 Protein, Mouse, Recombinant (His) is expressed in CHO mammalian cells with His tag. The predicted molecular weight is 52.2 kDa and the accession number is O70138.
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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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TMPY-01908 | ECM1 Protein, Mouse, Recombinant (His) | Mouse | HEK293 Cells | ||
ECM1 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 62.5 kDa and the accession number is Q61508-1.
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TMPY-02286 | Influenza A H1N1 (A/Puerto Rico/8/34/Mount Sinai) Matrix protein 1/M1 Protein (His) | H1N1 | E. coli | ||
Influenza A H1N1 (A/Puerto Rico/8/34/Mount Sinai) Matrix protein 1/M1 Protein (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 29.3 kDa and the accession number is B4UPA8.
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TMPY-06314 | MMP-10 Protein, Human, Recombinant (HEK293, His) | Human | HEK293 Cells | ||
MMP-10 Protein, Human, Recombinant (HEK293, His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 44.38 kDa and the accession number is P09238.
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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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TMPY-02290 | MMP-2 Protein, Mouse, Recombinant (His) | Mouse | HEK293 Cells | ||
MMP-2 Protein, Mouse, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 30.9 kDa and the accession number is P33434-1.
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TMPY-01377 | MMP-8 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
MMP-8 Protein, Human, Recombinant (His) is expressed in HEK293 mammalian cells with His tag. The predicted molecular weight is 52.6 kDa and the accession number is P22894.
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TMPJ-01085 | DPT Protein, Human, Recombinant (hFc & His) | Human | HEK293 Cells | ||
Dermatopontin, also known as Tyrosine-rich acidic matrix protein, TRAMP and DPT, is a secreted protein which belongs to the dermatopontin family. DPT is expressed in various tissues, such as fibroblasts, heart, skeletal muscle, brain and pancreas. It seems to mediate adhesion by cell surface integrin binding. DPT may serve as a communication link between the dermal fibroblast cell surface and its extracellular matrix environment. DPT can enhance TGFB1 activity through interaction with decorin. In addition, DPT accelerates collagen fibril formation, stabilizes collagen fibrils against low-temperature dissociation and inhibits cell proliferation.
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TMPH-03693 | VSIV (strain Glasgow) Matrix Protein (His) | VSIV | E. coli | ||
VSIV (strain Glasgow) Matrix Protein (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 30.8 kDa and the accession number is P04876.
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TMPY-02010 | DMP1 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
Dentin matrix acidic phosphoprotein (DMP1) is an extracellular matrix protein and a member of the small integrin binding ligand N-linked glycoprotein family. This protein, which is critical for proper mineralization of bone and dentin, is present in diverse cells of bone and tooth tissues. DMP1 contains a large number of acidic domains, multiple phosphorylation sites, a functional arg-gly-asp cell attachment sequence, and a DNA binding domain. In undifferentiated osteoblasts it is primarily a nuclear protein that regulates the expression of osteoblast-specific genes. During osteoblast maturation, DMP1 becomes phosphorylated and is exported to the extracellular matrix, where it orchestrates mineralized matrix formation. Mutations in DMP1 are known to cause autosomal recessive hypophosphatemia, a disease that manifests as rickets and osteomalacia. DMP1 may have a dual function during osteoblast differentiation. In the nucleus of undifferentiated osteoblasts, unphosphorylated form acts as a transcriptional component for activation of osteoblast-specific genes like osteocalcin. During the osteoblast to osteocyte transition phase it is phosphorylated and exported into the extracellular matrix, where it regulates nucleation of hydroxyapatite.
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TMPJ-01245 | UCMA Protein, Human, Recombinant | Human | E. coli | ||
C10orf49 is a secreted protein which encoded by the UCMA gene. It is a member of the UCMA family. C10orf49 is predominantly expressed in resting chondrocytes. It may be involved in the negative control of osteogenic differentiation of osteochondrogenic precursor cells in peripheral zones of fetal cartilage and at the cartilage-bone interface.
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TMPH-01316 | ECM1 Protein, Human, Recombinant (GST & His & Myc) | Human | E. coli | ||
Involved in endochondral bone formation as negative regulator of bone mineralization. Stimulates the proliferation of endothelial cells and promotes angiogenesis. Inhibits MMP9 proteolytic activity. ECM1 Protein, Human, Recombinant (GST & His & Myc) is expressed in E. coli expression system with N-10xHis-GST and C-Myc tag. The predicted molecular weight is 52.4 kDa and the accession number is Q16610.
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TMPY-00725 | COMP Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
Cartilage Oligomeric Matrix Protein (COMP), also referred to as Thrombospondin-5, is a non-collagenous extracellular matrix (ECM) protein and belongs to the subgroup B of the thrombospondin protein family. This protein is expressed primarily in cartilage, ligament, and tendon, and binds to other ECM proteins such as collagen I, II and IX with high affinities depending on the divalent cations Zn2+ or Ni2+. COMP is a secreted glycoprotein that is important for growth plate organization and function. It is suggested to play a role in cell growth and development, and recent studies have revealed the possible mechanism that it protects cells against death by elevating members of the IAP (inhibitor of apoptosis protein) family of survival proteins. Mutations in COMP cause two skeletal dysplasias, pseudoachondroplasia (PSACH) and multiple epiphyseal dysplasia (EDM1), and up-regulated expression of COMP are observed in rheumatoid arthritis and certain carcinomas.
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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-03692 | VSIV (strain San Juan) Matrix Protein (His & Myc) | VSIV | E. coli | ||
VSIV (strain San Juan) Matrix Protein (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 33.5 kDa and the accession number is P03519.
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TMPH-03694 | VSIV (strain Glasgow) Matrix Protein (His & Myc) | VSIV | Baculovirus Insect Cells | ||
VSIV (strain Glasgow) Matrix Protein (His & Myc) is expressed in Baculovirus insect cells with N-10xHis and C-Myc tag. The predicted molecular weight is 30.7 kDa and the accession number is P04876.
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TMPH-03430 | ECM31 Protein, S. cerevisiae, Recombinant (His) | Saccharomyces cerevisiae | E. coli | ||
ECM31 Protein, S. cerevisiae, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 38.5 kDa and the accession number is P38122.
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TMPJ-01369 | DPT Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 Cells | ||
Dermatopontin is a widely expressed noncollagenous protein component of the extracellular matrix. It is a 22 kDa molecule that is tyrosine sulfated but not glycosylated. Dermatopontin is down regulated in fibrotic growths such as leiomyoma and scar tissue, inhibits cell proliferation, accelerates collagen fibril formation, and stabilizes collagen fibrils against low-temperature dissociation, Dermatopontin deficient mice exhibit altered collagen matrix deposition and organization. Dermatopontin seems to mediate adhesion by cell surface integrin binding, may serve as a communication link between the dermal fibroblast cell surface and its extracellular matrix environment, and enhances TGFB1 activity (By similarity). Dermatopontin promotes bone mineralization under the control of the vitamin D receptor and inhibits BMP-2 effects on osteoblast precursors.
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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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TMPH-01673 | Human metapneumovirus (strain CAN97-83) Matrix protein (His) | HMPV | P. pastoris (Yeast) | ||
Plays a crucial role in virus assembly into filaments and budding. Early in infection, localizes in the nucleus where it may inhibit host cell transcription. Later in infection, traffics to the cytoplasm through the action of host CRM1 to associate with inclusion bodies, the site of viral transcription and replication. During virus assembly and budding, acts as a bridge between the nucleocapsid and the lipid bilayer.
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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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TMPH-03228 | Rabies virus (RABV) (strain SAD B19) Matrix Protein (His) | RABV | E. coli | ||
Rabies virus (RABV) (strain SAD B19) Matrix Protein (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 54.7 kDa and the accession number is P16285.
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TMPH-01672 | Human metapneumovirus (strain CAN97-83) Matrix protein (His & Myc) | HMPV | E. coli | ||
Plays a crucial role in virus assembly into filaments and budding. Early in infection, localizes in the nucleus where it may inhibit host cell transcription. Later in infection, traffics to the cytoplasm through the action of host CRM1 to associate with inclusion bodies, the site of viral transcription and replication. During virus assembly and budding, acts as a bridge between the nucleocapsid and the lipid bilayer.
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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-03227 | Rabies virus (RABV) (strain PM1503/AVO1) Matrix Protein (His) | RABV | E. coli | ||
Rabies virus (RABV) (strain PM1503/AVO1) Matrix Protein (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 54.7 kDa and the accession number is P15197.
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TMPH-03225 | Rabies virus (RABV) (strain CVS-11) Matrix Protein (His & Myc) | RABV | E. coli | ||
Plays a major role in assembly, budding and uncoating of virion after membrane fusion. Completely covers the ribonucleoprotein coil and keep it in condensed bullet-shaped form. Inhibits viral transcription and stimulates replication. Plays a major role in early induction of TRAIL-mediated apoptosis in infected neurons. Rabies virus (RABV) (strain CVS-11) Matrix Protein (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 28.1 kDa and the accession number is P25223.
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TMPH-03695 | VSIV (strain 98COE North America) Matrix Protein (His & Myc) | VSIV | E. coli | ||
VSIV (strain 98COE North America) Matrix Protein (His & Myc) is expressed in E. coli expression system with N-10xHis and C-Myc tag. The predicted molecular weight is 33.5 kDa and the accession number is Q8B0I2.
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TMPH-03226 | Rabies virus (RABV) (strain PM1503/AVO1) Matrix Protein (GST) | RABV | E. coli | ||
Plays a major role in assembly, budding and uncoating of virion after membrane fusion. Completely covers the ribonucleoprotein coil and keep it in condensed bullet-shaped form. Inhibits viral transcription and stimulates replication. Plays a major role in early induction of TRAIL-mediated apoptosis in infected neurons. Rabies virus (RABV) (strain PM1503/AVO1) Matrix Protein (GST) is expressed in E. coli expression system with N-GST tag. The predicted molecular weight is 49.9 kDa and the accession number is P15200.
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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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TMPJ-00242 | PARVA Protein, Human, Recombinant (His) | Human | E. coli | ||
Alpha-Parvin (PARVA) is a member of the Parvin family. PARVA contains two CH (calponin-homology) domains. PARVA is widely expressed, with highest levels in heart, skeletal muscle, kidney and liver. PARVA interacts with integrin-linked protein kinase and probably with actin and the LD1 and LD4 motifs of PXN. PARVA may play a role in the regulation of cell adhesion and cytoskeleton organization. PARVA is also involved in ciliogenesis.
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TMPH-02382 | Lake Victoria marburgvirus (MARV) (strain Angola/2005) Matrix protein VP40 (His & SUMO) | MARV | E. coli | ||
Plays an essential role virus particle assembly and budding. Promotes virus assembly and budding by interacting with host proteins of the multivesicular body pathway. The interaction with host E3 ubiquitin ligase SMURF2 facilitates virus budding. The interaction with the nucleocapsid and the plasma membrane may also facilitate virus budding. Specific interactions with membrane-associated GP and VP24 during the budding process may also occur. May play a role in genome replication.
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TMPH-02347 | Influenza A H1N1 (strain A/USA:Phila/1935) Matrix protein 2 (His) | H1N1 | E. coli | ||
Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation.
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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-01071 | CD44 Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
CD44 Protein, Human, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 80.2 kDa and the accession number is P16070.
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TMPH-02348 | Influenza A H1N1 (strain A/Puerto Rico/8/1934) Matrix protein 2 (His & Myc) | H1N1 | E. coli | ||
Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is believed to disrupt interactions between the viral ribonucleoprotein (RNP), matrix protein 1 (M1), and lipid bilayers, thereby freeing the viral genome from interaction with viral proteins and enabling RNA segments to migrate to the host cell nucleus, where influenza virus RNA transcription and replication occur. Also plays a role in viral proteins secretory pathway. Elevates the intravesicular pH of normally acidic compartments, such as trans-Golgi network, preventing newly formed hemagglutinin from premature switching to the fusion-active conformation.
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TMPY-00498 | Influenza A H3N2 (A/Aichi/2/1968) Matrix protein 1/M1 Protein (His) | H3N2 | E. coli | ||
Influenza A H3N2 (A/Aichi/2/1968) Matrix protein 1/M1 Protein (His) is expressed in E. coli expression system with His tag. The predicted molecular weight is 30 kDa and the accession number is I6SGW5.
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TMPH-01072 | CD44 Protein, Human, Recombinant (Avi & mFc), Biotinylated | Human | HEK293 Cells | ||
CD44 Protein, Human, Recombinant (Avi & mFc), Biotinylated is expressed in HEK293 mammalian cells with C-mFc-Avi tag. The predicted molecular weight is 51.0 kDa and the accession number is P16070.
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TMPH-02346 | Influenza A H1N1 (strain A/USA:Iowa/1943) Matrix protein 1 (His & Myc) | H1N1 | E. coli | ||
Plays critical roles in virus replication, from virus entry and uncoating to assembly and budding of the virus particle. M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit viral transcription. Interaction of viral NEP with M1-RNP is thought to promote nuclear export of the complex, which is targeted to the virion assembly site at the apical plasma membrane in polarized epithelial cells. Interactions with NA and HA may bring M1, a non-raft-associated protein, into lipid rafts. Forms a continuous shell on the inner side of the lipid bilayer in virion, where it binds the RNP. During virus entry into cell, the M2 ion channel acidifies the internal virion core, inducing M1 dissociation from the RNP. M1-free RNPs are transported to the nucleus, where viral transcription and replication can take place.; Determines the virion's shape: spherical or filamentous. Clinical isolates of influenza are characterized by the presence of significant proportion of filamentous virions, whereas after multiple passage on eggs or cell culture, virions have only spherical morphology. Filamentous virions are thought to be important to infect neighboring cells, and spherical virions more suited to spread through aerosol between hosts organisms.
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