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MMP-9 Antibody #3852

Filter:
  • WB
  • IP
Western Blotting Image 1: MMP-9 Antibody
Western blot analysis of partially purified, concentrated, serum-free medium containing human MMP-9, using MMP-9 Antibody.

To Purchase # 3852

Cat. # Size Qty. Price
3852S 100 µl
$306

Supporting Data

REACTIVITY H
SENSITIVITY Endogenous
MW (kDa) 84, 92
SOURCE Rabbit
Application Key:
  • WB-Western Blotting 
  • IP-Immunoprecipitation 
Species Cross-Reactivity Key:
  • H-Human 
  • Related Products

Product Information

Product Usage Information

Application Dilution
Western Blotting 1:1000
Immunoprecipitation 1:50

Storage

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

Protocol

Specificity / Sensitivity

MMP-9 Antibody detects full length (proenzyme, 92 kDa) and cleaved (active enzyme, 84 kDa) MMP-9.

Species Reactivity:

Human

The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.

Species predicted to react based on 100% sequence homology:

Rat

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Lys115 of human MMP-9. Antibodies are purified by protein A and peptide affinity chromatography.

Background

The matrix metalloproteinases (MMPs) are a family of proteases that target many extracellular proteins including other proteases, growth factors, cell surface receptors, and adhesion molecules (1). Among the family members, MMP-2, MMP-3, MMP-7, and MMP-9 have been characterized as important factors for normal tissue remodeling during embryonic development, wound healing, tumor invasion, angiogenesis, carcinogenesis, and apoptosis (2-4). Research studies have shown that MMP activity correlates with cancer development (2). One mechanism of MMP regulation is transcriptional (5). Once synthesized, MMP exists as a latent proenzyme. Maximum MMP activity requires proteolytic cleavage to generate active MMPs by releasing the inhibitory propeptide domain from the full-length protein (5).

Pathways

Explore pathways related to this product.


For Research Use Only. Not For Use In Diagnostic Procedures.
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