目录号 | 产品详情 | 靶点 | |
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T63797 | |||
PDZ1i 是有效的、能够透过血脑屏障的 MDA-9/Syntenin 特异性抑制剂。PDZ1i 能够抑制关键的 GBM (多形性成胶质细胞瘤)信号,包括 FAK 及 EGFRvIII,并能够减少 MMP 分泌。PDZ1i 可以提高患脑瘤小鼠的生存率并减少肿瘤的侵袭。 | |||
T80108 | |||
Hepcidin-1 (mouse) 是调控铁平衡的内源性多肽激素,通过上调TRAP、组织蛋白酶K和MMP-9的mRNA水平及增强TRAP-5b蛋白的分泌作用。此外,Hepcidin-1 (mouse) 降低FPN1蛋白水平并提升细胞内铁含量,且促进破骨细胞的分化。 | |||
T28251 | |||
ONO-8809 is a thromboxane A2 receptor antagonist. ONO-8809 inhibited the LTC4-induced airway hyperresponsiveness to histamine in a dose-dependent manner. Macrophage accumulation and matrix metalloproteinase-9 (MMP-9) activity in the stroke-negative area i | |||
T74680 | |||
NecroIr1 是一种铱 (III) 复合物,是顺铂 (Cisplatin) 耐药肺癌细胞 (A549R) 的坏死诱导剂。NecroIr1 选择性积累在线粒体中,导致氧化应激和线粒体膜电位 (MMP) 的损失。NecroIr1 能够激活受体相互作用的丝氨酸苏氨酸激酶 3 (RIPK3) 和混合谱系激酶结构域样假激酶 (MLKL),调节CDK4表达。 | |||
T79477 | Mitochondrial Metabolism | ||
SCAL-266为线粒体复合物I (CI) 的有效抑制剂,IC50值为0.83 μM。它能够抑制线粒体功能,阻断氧耗量率(OCR),诱导活性氧(ROS)的产生,降低线粒体膜电位(MMP)。此外,SCAL-266对依赖氧化磷酸化(OXPHOS)的癌细胞展示出强烈的抗增殖效果。 | |||
T83708 | |||
Mca-KPLGL-Dap(Dnp)-AR-NH2是一种用于矩阵金属蛋白酶(MMPs)的荧光底物。当被MMPs切割时,7-甲氧基香豆素-4-乙酰基(Mca)会释放,其荧光可用来定量MMP活性。Mca的激发/发射峰值分别为328/420 nm。 | |||
T79476 | Mitochondrial Metabolism | ||
SCAL-255,作为有效的线粒体复合物 I (CI) 抑制剂,具有 1.14 μM 的 IC50 值。该化合物通过抑制 OCR、诱导 ROS 产生并降低 MMP,干扰线粒体功能,对氧化磷酸化(OXPHOS)依赖性癌细胞显示出显著的抗增殖活性。 | |||
T73833 | |||
Anticancer agent 39 (compound B12) 是济源冬凌草素 A (JOA) 的荧光衍生物,可诱导线粒体膜电位 (MMP) 的崩溃,从而诱导细胞凋亡。Anticancer agent 39 抑制细胞克隆和迁移。Anticancer agent 39 具有抗 HGC-27 细胞增殖活性 IC50值为 0.39 μM。 | |||
T35701 | |||
FSL-1 TFA, a bacterial-derived toll-like receptor 2/6 (TLR2/6) agonist, enhances resistance to experimental HSV-2 infection[1]. FSL-1 TFA induces MMP-9 production through TLR2 and NF-κB/AP-1 signaling pathways in monocytic THP-1 cells[2]. FSL-1 significantly reduces HSV-2 replication in human vaginal epithelial cells (EC)[1].FSL-1 induces significant resistance to experimental genital HSV-2 infection through elaboration of a specific cytokine response profile[1].FSL-1 (50 ng/mL, 24 hours) induces MMP-9 expression at both mRNA and protein levels in human monocytic THP-1 cells[2].FSL-1 activates the MAP kinase/NF-κB signaling pathway[2]. Cell Viability Assay[1] Cell Line: V11I, V12I or V19I immortalized human vaginal EC FSL-1 application significantly protectes against genital HSV-2 challenge in mice[1]. Animal Model: Female Swiss-Webster mice (weighing 20-25 g)[1] [1]. William A Rose 2nd, et al. FSL-1, a bacterial-derived toll-like receptor 2/6 agonist, enhances resistance to experimental HSV-2 infection. Virol J. 2009 Nov 10;6:195. [2]. Cathryn J Kurkjian,et al. The Toll-Like Receptor 2/6 Agonist, FSL-1 Lipopeptide, Therapeutically Mitigates Acute Radiation Syndrome. Sci Rep. 2017 Dec 11;7(1):17355. | |||
T70957 | |||
NMac1is a small molecule phenylbutenoid dimer that has novel anti-proliferative effect only under glucose starvation in metastatic breast cancer cells. NMac1 causes significant activation of AMPK by decreasing ATP synthesis, lowers mitochondrial membrane potential (MMP, ΔΨm), and inhibits oxygen consumption rate (OCR) under glucose starvation. These effects of NMac1 are provoked by a consequence of OXPHOS complex I inhibition. |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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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-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-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-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-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-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-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-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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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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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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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-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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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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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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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-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-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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TMPK-01286 | MMP-8 Protein, Cynomolgus, Recombinant (His) | Cynomolgus | HEK293 Cells | ||
Alteration of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) expression has been studied for various cardiac diseases, including dilated cardiomyopathy (DCM), with the significance of surrogate markers of extracellular matrix (ECM) remodeling. MMP-8 was identified only in myocardiocytes, while MMP-9 and TIMP-2 were present in both myocardiocytes and stroma, but with different intensity. The increasing intensity of MMP-8 and TIMP-2 immunoreactions was significantly associated with low HCS.
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TMPH-00010 | MMP-14 Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
Endopeptidase that degrades various components of the extracellular matrix such as collagen. Activates progelatinase A. Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development. May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues in association with pro-MMP2. Cleaves ADGRB1 to release vasculostatin-40 which inhibits angiogenesis.
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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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TMPH-01644 | MMP-7 Protein, Human, Recombinant (GST) | Human | E. coli | ||
Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase. MMP-7 Protein, Human, Recombinant (GST) is expressed in E. coli expression system with N-GST tag. The predicted molecular weight is 46.1 kDa and the accession number is P09237.
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TMPH-03331 | MMP-7 Protein, Rat, Recombinant (GST) | Rat | E. coli | ||
Degrades casein, gelatins of types I, III, IV, and V, and fibronectin. Activates procollagenase. MMP-7 Protein, Rat, Recombinant (GST) is expressed in E. coli expression system with N-GST tag. The predicted molecular weight is 45.9 kDa and the accession number is P50280.
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TMPH-01633 | MMP-12 Protein, Human, Recombinant (His) | Human | E. coli | ||
May be involved in tissue injury and remodeling. Has significant elastolytic activity. 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. MMP-12 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 46.1 kDa and the accession number is P39900.
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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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TMPH-02915 | MMP-3 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase. MMP-3 Protein, Mouse, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 46.2 kDa and the accession number is P28862.
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TMPH-02594 | MMP-13 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion.
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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-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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TMPH-02146 | MMP-10 Protein, Human, Recombinant (His) | Human | E. coli | ||
Can degrade fibronectin, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V. Activates procollagenase. MMP-10 Protein, Human, Recombinant (His) is expressed in E. coli expression system with N-6xHis tag. The predicted molecular weight is 47.0 kDa and the accession number is P09238.
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TMPH-01646 | MMP-20 Protein, Human, Recombinant (His & Myc) | Human | Baculovirus Insect Cells | ||
Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation. Cleaves aggrecan at the '360-Asn-|-Phe-361' site.
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TMPH-02780 | MMP-24 Protein, Mouse, Recombinant (His & Myc) | Mouse | E. coli | ||
MMP-24 Protein, Mouse, Recombinant (His & Myc) is expressed in E. coli.
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TMPH-01124 | MMP-13 Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
MMP-13 Protein, Human, Recombinant (His & SUMO) is expressed in E. coli expression system with N-6xHis-SUMO tag. The predicted molecular weight is 58.3 kDa and the accession number is P45452.
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TMPH-02145 | MMP-3 Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase.
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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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TMPH-01647 | MMP-20 Protein, Human, Recombinant (E. coli, His & Myc) | Human | E. coli | ||
Degrades amelogenin, the major protein component of the enamel matrix and two of the macromolecules characterizing the cartilage extracellular matrix: aggrecan and the cartilage oligomeric matrix protein (COMP). May play a central role in tooth enamel formation. Cleaves aggrecan at the '360-Asn-|-Phe-361' site.
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TMPY-05717 | Integrin alpha V beta 8 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
Integrin alpha V beta 8 is a receptor for fibronectin. It recognizes the sequence R-G-D in its ligands. ITGAVB8 does not appear to assume different activation states; and the cytoplasmic tail does not connect to the cytoskeleton. It binds ligands containing an RGD motif; including vitronectin; fibrin and the latency associated peptide (LAP) of the latent TGF-beta complex. High affinity binding of alpha V beta 8 to LAP allows proteolytic cleavage by MT1-MMP; which releases active TGF-beta. This mechanism differs from that of alpha V beta 6; the other alpha V integrin which can activate TGF-beta from latency through non-proteolytic mechanisms.
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TMPH-01665 | TIMP3 Protein, Human, Recombinant (His) | Human | E. coli | ||
Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. May form part of a tissue-specific acute response to remodeling stimuli. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-9, MMP-13, MMP-14 and MMP-15.
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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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TMPY-05250 | CLEC3A Protein, Mouse, Recombinant (His) | Mouse | Baculovirus Insect Cells | ||
C-type lectin domain family 3 member A (CLEC3A) is a poorly characterized protein belonging to the superfamily of C-type lectins. Elevated CLEC3A expression may correlate with breast IDC metastatic potential and indicated a poor prognosis in breast IDC. CLEC3A knockdown inhibited BC cell growth and metastasis might be through suppressing PI3K/AKT signaling activity. That CLEC3A is a promising therapeutic target for BC in the future. Matrilysin (MMP-7) plays important roles in tumor progression. Previous studies have suggested that MMP-7 binds to tumor cell surface and promotes their metastatic potential. C-type lectin domain family 3 member A (CLEC3A) as a membrane-bound substrate of MMP-7. CLEC3A binds to heparan sulfate proteoglycans on cell surface, leading to the enhancement of cell adhesion to integrin ligands on ECM. It can be speculated that the cleavage of CLEC3A by MMP-7 weakens the stable adhesion of tumor cells to the matrix and promotes their migration in tumor microenvironments.
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TMPK-00093 | TIMP-1 Protein, Mouse, Recombinant (hFc) | Mouse | HEK293 Cells | ||
Tissue inhibitor of metalloprotease-1 (TIMP-1) is a tissue inhibitor of matrix metalloproteinases (MMPs). It however exerts multiple effects on biological processes, such as cell growth, proliferation, differentiation and apoptosis, in an MMP-independent manner.
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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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TMPJ-00948 | Endostatin Protein, Mouse, Recombinant (His) | Mouse | HEK293 Cells | ||
Endostatin, an endogenous non‑glycosylated inhibitor of endothelial cell proliferation and angiogenesis. It is produced and/or trimmed by metalloproteinases such as MMP‑2 and MMP‑9, and cathepsins S, B and L. The N‑terminal ~27 aa of Endostatin appear to contain the majority of its activity. This region contains zinc binding sites that are thought to be critical for its anti‑endothelial and anti‑tumor effects, as well as multiple cleavage sites that, when used, can modify its activity. Mouse Endostatin shares 96% aa sequence identity with rat and 85‑87% with human, bovine and equine Endostatin. It is predominantly expressed in liver, kidney, lung, skeletal muscle and testis. Endostatin inhibits endothelial cell growth by inducing cell cycle arrest in G1 phase and initiating apoptosis. It is also thought to down‑regulate angiogenesis by blocking VEGF‑induced endothelial cell migration. Endostatin may also be involved with down‑regulation of angiogenesis after establishment of placental circulation in the pregnant uterus.
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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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TMPY-01900 | Kallikrein 4/KLK4 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
Kallikrein-4, also known as Enamel matrix serine proteinase 1, Kallikrein-like protein 1, KLK-L1, Serine protease 17, KLK4, PRSS17, and EMSP1, is a secreted protein that belongs to the peptidase S1 family and Kallikrein subfamily. Kallikrein-4 / KLK4 is a serine protease expressed during enamel maturation, and proteolytic processing of the enamel matrix by KLK4 is critical for proper enamel formation. Kallikrein-4 / KLK4 contains one peptidase S1 domain. Kallikrein-4 / KLK4 is secreted by transition- and maturation-stage ameloblasts. KLK4 aggressively degrades the retained organic matrix following the termination of enamel protein secretion. Two proteases are secreted into the enamel matrix of developing teeth. The early protease is enamelysin (MMP-2). The late protease is kallikrein 4 (KLK4). The principal functions of MMP-2 and KLK4 in dental enamel formation are to facilitate the orderly replacement of organic matrix with mineral, generating an enamel layer that is harder, less porous, and unstained by retained enamel proteins. Defects in Kallikrein-4 / KLK4 are the cause of Amelogenesis Imperfecta Hypomaturation type 2A1 (AI2A1) which is an autosomal recessive defect of enamel formation. The disorder involves both primary and secondary dentitions.
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TMPY-00610 | RAB2 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
RAB2A, a protein essential for ER-to-Golgi transport, is critical in promoting proteolytic activity and 3D invasiveness of breast cancer (BC) cell lines.RAB2A is amplified and elevated in human BC and is a powerful and independent predictor of disease recurrence in BC patients. Thus, RAB2A is a novel trafficking determinant essential for regulation of a mesenchymal invasive program of BC dissemination. At the cellular levels, RAB2A controls both canonical polarized Golgi-to-Plasma membrane trafficking of the junctional protein E-cadherin, and post-endocytic trafficking of the membrane-bound metalloprotease, MT1-MMP.
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TMPJ-00159 | EMMPRIN/CD147 Protein, Human, Recombinant (Avi & His), Biotinylated | Human | HEK293 Cells | ||
Basigin/CD147 is a member of the immunoglobulin superfamily with homology to both the immunoglobulin V domain and MHC class II antigen beta-chain. This protein play important roles in variety of events including spermatogenesis, embryo implantation, neural network formation. CD147 induces the production and release of matrix metalloproteinases (MMP) in the surrounding mesenchymal cells and tumor cells, and thereby promotes invasion, metastasis, growth and survival of malignant cells. Furthermore, CD147 also serves as a receptor for extracellular cyclophilinthe and its association with integrins might be important in signal transduction. CD147 displays increased expression in many cancers, and it has been previously demonstrated to participate in cancer metastasis and progression.
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TMPY-02404 | ADAM9 Protein, Mouse, Recombinant (His) | Mouse | HEK293 Cells | ||
ADAM9 (A disintegrin and metallopeptidase domain 9, MDC9, meltrin gamma), is a type 1 transmembrane protein that has been associated with cancer development and metastases. ADAM9 is consistently overexpressed in various human cancers, and plays a role in tumorigenesis in mouse models. ADAM9 cleaves and releases a number of molecules with important roles in tumorigenesis and angiogenesis, such as EGF, FGFR2iiib, Tie-2, Flk-1, EphB4, CD40, VCAM-1, and VE-cadherin, and could represent a potential therapeutic target in tumors where it is highly expressed. ADAM9 belongs to a family of transmembrane, disintegrin-containing metalloproteinases involved in protein ectodomain shedding and cell-cell and cell-matrix interactions. ADAM-9 adhesive domain plays a role in regulating the motility of cells by interaction with beta1 integrins and modulates MMP synthesis.
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TMPJ-01060 | CXCL6 Protein, Human, Recombinant (His) | Human | HEK293 Cells | ||
Chemokine (C-X-C-Motif) Ligand 6 (CXCL6) is a small cytokine belonging to the CXC chemokine family. It is a potent neutrophil chemotactic and activating factor and it exhibits extensive similarity to other CXC chemokines such as IL-8 and ENA-78. CXCL6 can promote the release of MMP-9 from granulocytes indicating its potential role as an inflammatory mediator. It functionally uses both of the IL-8/CXCL8 receptors to chemoattract neutrophils but that is structurally most related to epithelial cell-derived neutrophil attractant-78 (ENA-78)/CXCL5. The human CXCL6 gene has been cloned and is physically mapped to the CXC chemokine locus on chromosome 4. Mature human CXCL6 is a 75 amino acid (aa) protein with a predicted molecular weight of approximately 8 kDa. Human CXCL6 shares 60% and 67% aa identity with mouse and bovine CXCL6, respectively.
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TMPH-00711 | BioH Protein, E. coli, Recombinant (His & Myc) | E. coli | E. coli | ||
The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. E.coli employs a methylation and demethylation strategy to allow elongation of a temporarily disguised malonate moiety to a pimelate moiety by the fatty acid synthetic enzymes. BioH shows a preference for short chain fatty acid esters (acyl chain length of up to 6 carbons) and short chain p-nitrophenyl esters. Also displays a weak thioesterase activity. Can form a complex with CoA, and may be involved in the condensation of CoA and pimelic acid into pimeloyl-CoA, a precursor in biotin biosynthesis.; Catalyzes the hydrolysis of the methyl ester bond of dimethylbutyryl-S-methyl mercaptopropionate (DMB-S-MMP) to yield dimethylbutyryl mercaptopropionic acid (DMBS-MPA) during the biocatalytic conversion of simvastin acid from monacolin J acid. Can also use acyl carriers such as dimethylbutyryl-S-ethyl mercaptopropionate (DMB-S-EMP) and dimethylbutyryl-S-methyl thioglycolate (DMB-S-MTG) as the thioester substrates.
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