TIMP-4 Antibody Blocking Peptide(bs-0418P)-500ug

TIMP-4 Antibody Blocking Pepti

de(bs-0418P)-500ug
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  • bs-0418P
  • 2025年10月16日
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      500ug

    产品编号bs-0418P
    英文名称TIMP-4 Antibody Blocking Peptide
    中文名称金属蛋白酶组织抑制因子-4封闭多肽
    英文别名Metalloproteinase inhibitor 4; TIMP 4; TIMP4; TIMP metallopeptidase inhibitor 4; TIMP-4; Timp4; TIMP4_HUMAN; Tissue inhibitor of metalloproteinase 4.
    性状Lyophilized
    纯化方法HPLC
    研究领域

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

    Cancer > Invasion/microenvironment > ECM > Extracellular matrix > TIMPs

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

    Cell Biology > Proteolysis / Ubiquitin > Protease inhibitors > Metalloprotease inhibitors > TIMPs

    亚细胞定位Secreted.
    组织特异性Abundant in heart and present at low levels in many other tissues.
    相似性Belongs to the protease inhibitor I35 (TIMP) family.
    Contains 1 NTR domain.
    功能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.
    保存条件Shipped at 4℃. Stored at -20℃ for one year. Avoid repeated freeze/thaw cycles.
    背景资料The tissue inhibitors of metalloproteinases (TIMPs) are naturally occurring proteins that specifically inhibit matrix metalloproteinases and regulate extracellular matrix turnover and tissue remodeling by forming tightbinding inhibitory complexes with the MMPs. Thus, TIMPs maintain the balance between matrix destruction and formation. An imbalance between MMPs and the associated TIMPs may play a significant role in the invasive phenotype of malignant tumors. The TIMP proteins share several structural features including six loops held in place by six disulfide bonds arranged in three knot-like structures. These proteins also contain twelve cysteine residues in conserved regions of the molecule that form six disulfide bonds, essential for the formation of native conformations, and the N terminal region that is necessary for inhibitory activities. The N terminus of each TIMP contains a consensus sequence (VIRAK) and each TIMP is translated with a 29 amino acid leader sequence that is cleaved off to produce the mature protein. The C terminal regions are divergent, which enhances the selectivity of inhibition and binding efficiency. Although the TIMP proteins share high homology, they may either be secreted extracellularly in soluble form (TIMP1, TIMP2 and TIMP4) or bind to extracellular matrix components (TIMP3). The MMPs and TIMPs can be divided into two groups with respect to gene expression: the majority exhibit inducible expression and a small number are produced constitutively or are expressed at very low levels and are not inducible. Among agents that induce MMP and TIMP production are the inflammatory cytokines TNF alpha and IL1 beta. A marked cell type specificity is a hallmark of both MMP and TIMP gene expression (i.e. a limited number of cell types can be induced to make these proteins). Tissue Inhibitor of Metalloproteinases 4 (TIMP4) was identified by molecular cloning. TIMP4 shows 37 % amino acid identity with TIMP1 and 51 % homology with TIMP2 and TIMP3. TIMP4 is secreted extracellularly, predominantly in heart and brain tissue. It may function in a tissue specific fashion in extracellular matrix (ECM) homeostasis. TIMP4 has a strong inhibitory effect on the invasion of human breast cancer cells across reconstituted basement membranes suggesting that TIMP4 may have an important role in inhibiting primary tumor growth and progression. The human TIMP4 gene has the chromosomal location of 3p25.

     

     

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