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MMP-9 (D6O3H) Rabbit Monoclonal Antibody (Biotinylated) #15561

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  • WB

    Product Specifications

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 84,92
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Description

    This Cell Signaling Technology® antibody is the biotinylated version of the unconjugated MMP-9 (D6O3H) Rabbit Monoclonal Antibody #13667 and is expected to exhibit the same species cross-reactivity. The concentration of the biotinylated antibody is 500 ug/ml. Peptide ELISA data were generated using the biotinylated antibody. Western blot data were generated using the unconjugated antibody.
    MW (kDa) 84,92

    Product Usage Information

    Biotinylated antibodies are ideal for immunoassay technologies and high-throughput ELISA platforms that require antibody pairs where both antibodies are from the same host. Platforms utilizing biotinylated antibodies include, but are not limited to, MSD, xMAP, Quanterix Simoa, AlphaLISA, AlphaScreen, HTRF, LANCE, and TR-FRET.

    Optimal dilutions/working concentrations should be determined by the end user. Please contact us if you require the antibody clone biotinylated at a different concentration, a carrier-free formulation, or a more customized packaging solution.
    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 140 mM NaCl, 3 mM KCl, 10 mM sodium phosphate (pH 7.4) dibasic, 2 mM potassium phosphate monobasic, 2 mg/mL BSA, and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    MMP-9 (D6O3H) Rabbit Monoclonal Antibody (Biotinylated) recognizes the full-length, proenzyme (92 kDa) and the cleaved, active enzyme (84 kDa) of MMP-9.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Phe542 of human MMP-9 protein.

    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).

    Alternate Names

    67 kDa matrix metalloproteinase-9; 82 kDa matrix metalloproteinase-9; 92 kDa gelatinase; 92 kDa type IV collagenase; CLG4B; Gelatinase B; GELB; macrophage gelatinase; MANDP2; matrix metallopeptidase 9; matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase); matrix metalloproteinase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase); Matrix metalloproteinase-9; MMP-9; MMP9; type V collagenase

    For Research Use Only. Not for Use in Diagnostic Procedures.
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