MMP12 Antibody Blocking Peptide(bs-23567P)-500ug

MMP12 Antibody Blocking Peptid

e(bs-23567P)-500ug
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  • bs-23567P
  • 2025年10月16日
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      500ug

    产品编号bs-23567P
    英文名称MMP12 Antibody Blocking Peptide
    中文名称基质金属蛋白酶-12封闭多肽
    英文别名matrix metalloproteinase 12; MMP12; EC 3.4.24.65; HME; Macrophage elastase; Macrophage metaloelastase; Matrix metalloprotease 12; ME; MGC138506; MME; MMP 12; MMP12_HUMAN; MMP 12; MMP-12; MMP12.
    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

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

    亚细胞定位Secreted, extracellular space, extracellular matrix (Probable).
    组织特异性Found in alveolar macrophages but not in peripheral blood monocytes.
    相似性Belongs to the peptidase M10A family.
    Contains 4 hemopexin-like domains.
    保存条件Shipped at 4℃. Stored at -20℃ for one year. Avoid repeated freeze/thaw cycles.
    注意事项This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
    背景资料Proteins of the matrix metalloproteinase (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, metastasis, and atherosclerosis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases.MMP12 was first described in murine macrophages, later in human macrophages, and more recently in other cell types. Also known as metalloelastase, MMP12 is able to degrade elastin, entactin, laminin 1, fibronectin, type IV collagen as well as insulin B-chain and casein. MMP12 is often confused with the Serine proteinase, Leukocyte elastase (EC 3.4.21.37) because of similar nomenclature. MMP12 is structurally similar to the classical MMPs (MMP1, MMP3); it contains a propeptide with autoinhibitory cysteine switch site, a well-conserved zinc site, hinge region and hemopexin domain. MMP12 lacks a transmembrane domain and furin cleavage site. The zymogen for MMP-12 is about 54 kD, and is quickly activated to the 45 kD form; and this breaks down to cascade of active forms, ending with the common 22 kD form. Stimulated macrophages produce MMP12; it has also been found in osteosarcoma cells, synovial fibroblasts and lung fibroblasts.

     

     

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