Render Target: STATIC
Render Timestamp: 2024-10-31T10:35:49.635Z
Commit: 23cb9f61fe67e1e9093fd644a533c4ff516a6463
XML generation date: 2024-09-30 01:58:07.141
Product last modified at: 2024-09-30T08:00:52.744Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

MMP-8 (E1C4L) Rabbit mAb #78399

Filter:
  • WB
  • IP
  • IHC

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous (IHC-P), Transfected (W)
    MW (kDa) 70
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    • IHC-Immunohistochemistry 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:100
    Immunohistochemistry (Paraffin) 1:200 - 1:800

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    MMP-8 (E1C4L) Rabbit mAb recognizes endogenous levels of total MMP-8 protein by IHC-P and transfected levels of MMP-8 protein by Western blot. Non-specific staining was observed in human salivary gland by immunohistochemistry.

    Species Reactivity:

    Human

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the amino terminus of human MMP-8 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). MMP-8 is also known as Neutrophil Collagenase as it is stored in special granules in neutrophils. Like other MMPs, it also cleaves fibrillar collagens. It also is implicated in various cancers and is thought to be pro-tumorigenic (6).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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