Type of antibody:
Primary antibodies, Recombinant antibodies
recombinant human IgG1
Alternative names:
HSMRK222, K222, K222TA2, SFD, MIG-5

Specifications for TIMP-3 Antibody, anti-human, REAfinity™


Clone REA417 recognizes the human tissue inhibitor of metalloproteinases 3 (TIMP-3) antigen, an extracellular matrix bound protein which is also known as MIG-5. TIMP-3 is expressed ubiquitously and is induced in response to mitogenic stimulation. It is a member of a family of endogenous matrix metalloproteinases inhibitors, of which there are currently four members (TIMP-1 through TIMP-4). By virtue of their matrix metalloproteinases inhibitory activity, TIMP family members have a potentially important function in regulating matrix composition and thereby affect a wide range of physiological processes including cell growth, invasion, migration, angiogenesis, transformation, and apoptosis. TIMP-3 complexes with metalloproteinases and irreversibly inactivates them by binding to their catalytic zinc cofactor. Mutations in TIMP-3 are associated with Sorsby fundus dystrophy, a macular degenerative disease manifested by sudden loss of visual acuity in the third to fourth decades of life due to choroidal (submacular) neovascularization.
Additional information: Clone REA417 displays negligible binding to Fc receptors.

Alternative names

HSMRK222, K222, K222TA2, SFD, MIG-5

Detailed product information

Technical specifications

Isotyperecombinant human IgG1
Isotype controlREA Control Antibody (I), human IgG1
Hosthuman cell line
Type of antibodyPrimary antibodies, Recombinant antibodies
Alternative names of antigenHSMRK222, K222, K222TA2, SFD, MIG-5
Molecular mass of antigen [kDa]22
Distribution of antigenother
Entrez Gene ID7078
RRIDAB_2654191, AB_2654192, AB_2654193, AB_2654190

Resources for TIMP-3 Antibody, anti-human, REAfinity™


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References for TIMP-3 Antibody, anti-human, REAfinity™


  1. Uría, J. A. et al. (1994) Structure and expression in breast tumors of human TIMP-3, a new member of the metalloproteinase inhibitor Family. Cancer Res. 54(8): 2091-2094
  2. Qi, J. H. et al. (2003) A novel function for tissue inhibitor of metalloproteinases-3 (TIMP3): inhibition of angiogenesis by blockage of VEGF binding to VEGF receptor-2. Nat Med 9(4): 407-415
  3. Amour, A. et al. (2000)
    in vitro
    activity of ADAM-10 is inhibited by TIMP-1 and TIMP-3.
    FEBS Lett. 473(3): 275-279

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