Anti-MMP-9

Evaluated by Western Blotting in lysate from PMA-conditioned HL60 cells.

Western Blotting Analysis: A 1:500 dilution of this antibody detected MMP-9 in lysate from Phorbol 12-myristate 13-acetate (PMA)-conditioned HL60 cells.

Anti-MMP-9, Cat. No. ABT544, is a rabbit polyclonal antibody that detects Matrix Metalloroteinase-9 and is tested for use in Immunohistochemistry (Paraffin) and Western Blotting..

Immunohistochemistry Analysis: A 1:250 dilution from a representative lot detected MMP-9 in rat spleen and human bone marrow tissues.

Research Category
Cell Structure

This rabbit polyclonal antibody detects human and rat Matrix metalloproteinase-9. It targets an epitope within 16 amino acids from the N-terminal half.

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Matrix metalloproteinase-9 (UniProt: P50282; also known as EC: 3.4.24.35, MMP-9, 92 kDa gelatinase, 92 kDa type IV collagenase, Gelatinase B, GELB) is encoded by the Mmp9 gene (Gene ID: 81687) in rat. Matrix Metalloproteinases (MMPs) are a family of zinc metallo-endopeptidases secreted by cells and are responsible for much of the turnover of matrix components. MMP-9 is a secreted extracellular matrix metalloproteinase that exhibits a broad range of substrate specificity for native collagens including types IV, V, VII, and X as well as gelatin, proteoglycans, and elastin. It can exist as monomer or disulfide-linked homodimer. MMP-9 is synthesized with a signal peptide (aa 1-19) and a propeptide (aa 20-107) that are subsequently cleaved to produce active enzyme. Its activity can be inhibited by TIMP-1, which binds exclusively to pro-MMP-9 (Kd ~35 nM). MMP-9 contain a fibronectin-like domain inserted into the catalytic domain, presumably to enhance substrate binding. MMP-9 also contains a collagen type-V-like domain, which may enhance substrate binding and specificity. MMP-9 contains a cysteine switch (aa 98-105) where the conserved cysteine binds the catalytic zinc ion and inhibits its enzyme activity. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.

~85 kDa obsereved; 78.61 kDa calculated. Uncharacterized bands may be observed in some lysate(s).

Epitope: domain of:

KLH-conjugated linear peptide corresponding to 16 amino acids from the N-terminal half of rat Matrix metalloproteinase-9.

Concentration: Please refer to lot specific datasheet.

Affinity Purified

Purified rabbit polyclonal antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Stable for 1 year at 2-8°C from date of receipt.