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Human TIMP-1 / TIMP1 Protein (Fc Tag)

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Reactivity: Human  
Application: ELISA  
    10934-R004-50
    10934-R004-100
    50 µg 
    100 µg 
    Add to Cart
    Reactivity: Human  
    Application: ELISA  
      10934-MM03-50
      10934-MM03-100
      10934-MM03-1
      50 µg 
      100 µg 
      1 mg 
      Add to Cart
      Reactivity: Human  
      Application: ELISA  
        10934-RP01-400
        10934-RP01-200
        10934-RP01-100
        400 µg 
        200 µg 
        100 µg 
        Add to Cart
        Reactivity: Human  
        Application: ELISA  
          10934-MM02-50
          10934-MM02-200
          10934-MM02-100
          50 µg 
          200 µg 
          100 µg 
          Add to Cart
          Reactivity: Human  
          Application: ELISA  
            10934-T16-50
            10934-T16-200
            10934-T16-100
            50 µg 
            200 µg 
            100 µg 
            Add to Cart

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            TIMP-1/TIMP1 protein Background

            TIMP metallopeptidase inhibitor 1, also known as TIMP-1/TIMP1, Collagenase inhibitor 16C8 fibroblast Erythroid-potentiating activity, TPA-S1TPA-induced proteinTissue inhibitor of metalloproteinases 1, is a natural inhibitors of the matrix metalloproteinases (MMPs), a group of peptidases involved in degradation of the extracellular matrix. TIMP-1/TIMP1 is found in fetal and adult tissues. Highest levels are found in bone, lung, ovary and uterus. Complexes with metalloproteinases and irreversibly inactivates them by binding to their catalytic zinc cofactor. TIMP-1/TIMP1 mediates erythropoiesis in vitro; but, unlike IL-3, it is species-specific, stimulating the growth and differentiation of only human and murine erythroid progenitors. In addition to its inhibitory role against most of the known MMPs, the protein is able to promote cell proliferation in a wide range of cell types, and may also have an anti-apoptotic function. Transcription of this protein encoding gene is highly inducible in response to many cytokines and hormones. In addition, the expression from some but not all inactive X chromosomes suggests that this gene inactivation is polymorphic in human females. This encoding gene is located within intron 6 of the synapsin I gene and is transcribed in the opposite direction. Complexes with metalloproteinases and irreversibly inactivates them by binding to their catalytic zinc cofactor. TIMP-1/TIMP1 is Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-11, MMP-12, MMP-13 and MMP-16.

            Human TIMP-1/TIMP1 protein References
          • Hornebeck W (2004). Down-regulation of tissue inhibitor of matrix metalloprotease-1 (TIMP-1) in aged human skin contributes to matrix degradation and impaired cell growth and survival.. Pathol. Biol. 51 (10): 569-73.
          • Soini Y, et al. (2001) Expression of MMP2, MMP9, MT1-MMP, TIMP-1, and TIMP2 mRNA in valvular lesions of the heart. J Pathol. 194(2):225-31.
          • Wang X, et al. (1999) Analysis of coding sequences for tissue inhibitor of metalloproteinases 1 (TIMP-1) and 2 (TIMP2) in patients with aneurysms. Matrix Biol. 18(2):121-4.
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