MMP1 Antibody Blocking Peptide(bs-0424P)-500ug

MMP1 Antibody Blocking Peptide

(bs-0424P)-500ug
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  • ¥880
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  • bs-0424P
  • 2025年10月16日
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      500ug

    产品编号bs-0424P
    英文名称MMP1 Antibody Blocking Peptide
    中文名称基质金属蛋白酶-1封闭多肽
    英文别名27 kDa interstitial collagenase; CLGN; CLG; collagenase, fibroblast; Fibroblast collagenase; Interstitial collagenase; MMP 1; MMP-1; MMP; Fibroblast collagenase; Interstitial collagenase; Matrix metallopeptidase 1 (interstitial collagenase); Matrix metalloprotease 1; Matrix metalloproteinase-1; MMP1_HUMAN; OTTHUMP00000045866; Matrix Metalloproteinase 1.
    性状Lyophilized
    纯化方法HPLC
    研究领域

    Cancer > Invasion/microenvironment > Angiogenesis > ECM enzymes > MMPs

    Cancer > Tumor biomarkers > Enzymes > MMPs

    Cardiovascular > Angiogenesis > Adhesion / ECM > Matrix Metalloproteinases > MMP

    Cardiovascular > Atherosclerosis > Thrombosis > Endothelial mediators/regulators

    Cell Biology > Proteolysis / Ubiquitin > Proteolytic enzymes > Metalloprotease > MMPs

    Signal Transduction > Cytoskeleton / ECM > Extracellular Matrix > ECM Enzymes > MMP

    亚基Interacts with HIV-1 Tat.
    亚细胞定位Secreted, extracellular space, extracellular matrix (Probable).
    翻译后修饰Undergoes autolytic cleavage to two major forms (22 kDa and 27 kDa). A minor form (25 kDa) is the glycosylated form of the 22 kDa form. The 27 kDa form has no activity while the 22/25 kDa form can act as activator for collagenase.
    相似性Belongs to the peptidase M10A family.
    Contains 4 hemopexin-like domains.
    功能Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat's mediated neurotoxicity.
    保存条件Shipped at 4℃. Stored at -20℃ for one year. Avoid repeated freeze/thaw cycles.
    背景资料The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane bound zincendopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc binding site characterizes the structure of the MMPs. In addition, fibronectin like repeats, a hinge region, and a C terminal hemopexin like domain allow categorization of MMPs into the collagenase, gelatinase, stomelysin and membrane type MMP subfamilies. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown. MMPs are considered to play an important role in wound healing, apoptosis, bone elongation, embryo development, uterine involution, angiogenesis and tissue remodeling, and in diseases such as multiple sclerosis, Alzheimer's, malignant gliomas, lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis.

     

     

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