Clone:
REA417
Type of antibody:
Primary antibodies, Recombinant antibodies
Isotype:
recombinant human IgG1
Applications:
ICFC
Alternative names:
HSMRK222, K222, K222TA2, SFD, MIG-5

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

Overview

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

CloneREA417
Clonalitymonoclonal
Isotyperecombinant human IgG1
Isotype controlREA Control Antibody (I), human IgG1
Hostcell line
Type of antibodyPrimary antibodies, Recombinant antibodies
Specieshuman
AntigenTIMP-3
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

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

Publications

  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)
    The
    in vitro
    activity of ADAM-10 is inhibited by TIMP-1 and TIMP-3.
    FEBS Lett. 473(3): 275-279

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