Render Target: STATIC
Render Timestamp: 2024-11-22T12:07:06.851Z
Commit: 5c4accf06eb7154018ba3f54329c7590f97f534a
XML generation date: 2024-05-10 06:21:07.823
Product last modified at: 2024-11-03T18:30:08.147Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77

MMP-9 (D6O3H) XP® Rabbit mAb (PE Conjugate) #27647

Filter:
  • F

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa)
    Source/Isotype Rabbit IgG
    Application Key:
    • F-Flow Cytometry 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Description

    This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated MMP-9 (D6O3H) XP® Rabbit mAb #13667.

    Product Usage Information

    Application Dilution
    Flow Cytometry (Fixed/Permeabilized) 1:50

    Storage

    Supplied in PBS (pH 7.2), less than 0.1% sodium azide and 2 mg/ml BSA. Store at 4°C. Do not aliquot the antibodies. Protect from light. Do not freeze.

    Protocol

    Specificity / Sensitivity

    MMP-9 (D6O3H) XP® Rabbit mAb (PE Conjugate) 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).
    For Research Use Only. Not For Use In Diagnostic Procedures.
    Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
    XP is a registered trademark of Cell Signaling Technology, Inc.
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