MMP2 antibody - Hemopexin domain (ab38922)

Product Name 

MMP2 antibody - Hemopexin domain

Product type 

Primary antibodies

Description 

Rabbit polyclonal to MMP2 - Hemopexin domain

Immunogen 

Synthetic peptide of the hemopexin domain of Human MMP2.

(Peptide available as ab44848.)

Reacts with 
(species key)

Hu

Specificity 

The antibody binds to both native and reduced forms of MMP2, but does not cross react with the other MMP family members.

We have a range of domain specific antibodies for this target. For a full list please see all MMP2 antibodies

Tested applications 
(see key)

WB

Abreviews 

Customer reviews (see key)

Read about Abreviews

Application notes 
(see key)

Recommended dilutions
WB: The recommended starting concentration for Western blots is 1:1000 when using colorimetric substrates such as BCIP/NBT, and 1:5000 for chemiluminescent substrates. Higher concentration of antibody may be needed for non-human samples. The low protein levels produced (pg/ml) often require concentration of cell culture media to visualize the bands by Western Blotting. Gelatinase-A and Gelatinase-B may be enriched from conditioned culture media by binding to gelatin-agarose, and eluted by 10% DMSO. Detects a band of approximately 67 - 74 kDa (predicted molecular weight: 74 kDa). Dilution optimised using Chromogenic detection. Not yet tested in other applications. Optimal dilutions/concentrations should be determined by the end user.

Positive control 
(see definition)

Cell media from human neonatal dermal fibroblasts (treated with IL1 beta)

Cellular localization 

Secreted

Research areas 

Cancer >> Cancer Metabolism >> Response to hypoxia
Cancer >> Tumor biomarkers >> Enzymes >> MMPs
Cell Biology >> Proteolysis / Ubiquitin >> Proteolytic enzymes >> Metalloprotease >> MMPs
Cancer >> Invasion/microenvironment >> ECM >> Extracellular matrix >> MMPs
Cardiovascular >> Angiogenesis >> Adhesion / ECM >> Matrix Metalloproteinases >> MMP

Relevance 

The matrix metalloproteinases (MMPs) are a family of at least eighteen secreted and membrane-bound zinc endopeptidases. Collectively, these enzymes can degrade all the components of the extracellular matrix, including fibrillar and non-fibrillar collagens, fibronectin, laminin and basement membrane glycoproteins. In general, a signal peptide, a propeptide, and a catalytic domain containing the highly conserved zinc-binding site characterizes the structure of the MMPs. In addition, fibronectin-like repeats, a hinge region, and a C terminal hemopexin-like domain allow categorization of MMPs into the collagenase, gelatinase, stomelysin and membrane type MMP subfamilies. All MMPs are synthesized as proenzymes, and most of them are secreted from the cells as proenzymes. Thus, the activation of these proenzymes is a critical step that leads to extracellular matrix breakdown. MMPs are considered to play an important role in wound healing, apoptosis, bone elongation, embryo development, uterine involution, angiogenesis and tissue remodeling, and in diseases such as multiple sclerosis, Alzheimer's, malignant gliomas, lupus, arthritis, periodontis, glumerulonephritis, atherosclerosis, tissue ulceration, and in cancer cell invasion and metastasis.

MMP2, also known as Gelatinase A, is a type IV collagenase that specifically cleaves type IV collagen, the major structural component of basement membranes. The metastatic potential of tumor cells has been found to correlate with the activity of this enzyme.

Database links 

Raised in 

Rabbit

Clonality 

Polyclonal

Isotype 

IgG

Purity 

Immunogen affinity purified

Storage buffer 

Preservative: 0.05% Sodium Azide
Constituents: 50% Glycerol

Material safety datasheets (MSDS) for this product:
Glycerol MSDS
Sodium Azide MSDS

Form 

Liquid

Concentration 

1.000 mg/ml

Storage instructions 

Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze / thaw cycles.

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