antibody

Matrix Metalloproteinase 3 (MMP3)

MBS395183

0.2 mg

325 USD

monoclonal

mouse

nonconjugated

[1B4]

western blot, ELISA, immunohistochemistry, enzyme immunoassay

Antibody

Matrix Metalloproteinase 3 (MMP3)

[Matrix Metalloproteinase 3 (MMP3)]

[SL-1; Matrix metalloproteinase-3; MMP-3; Transin-1]

[stromelysin-1 preproprotein; Stromelysin-1; stromelysin-1; transin-1; proteoglycanase; matrix metalloproteinase-3; matrix metalloproteinase 3 (stromelysin 1, progelatinase); matrix metallopeptidase 3 (stromelysin 1, progelatinase); Matrix metalloproteinase-3; MMP-3; Transin-1]

[MMP3]

[MMP3; MMP3; SL-1; STMY; STR1; CHDS6; MMP-3; STMY1; STMY1; SL-1; MMP-3]

MMP3_HUMAN

Monoclonal

IgG1

[1B4]

Mouse

Human

477

Protein A/G Chromatography

Unconjugated; Provided as solution in phosphate buffered saline with 0.08% sodium azide

Product should be stored at -20 degree C. Aliquot to avoid freeze/thaw cycles. Ship at ambient temperature, freeze upon arrival.

ELISA (EIA), Western Blot (WB), Immunohistochemistry (IHC)

Antibody can be used for Western blotting (1-2 ug/ml) and immunohistochemistry on formlin-fixed paraffin-embedded tissue sections (1-5 ug/ml). Optimal concentration should be evaluated by serial dilutions. Functional Analysis: Western Blotting

Immunohistochemistry (IHC)

Immunogen: Hybridoma produced by the fusion of splenocytes from BALB/c mice immunized with a synthetic peptide derived from the C-terminus of the human MMP3 protein and mouse myeloma Ag8563 cells.

Positive Control: Oesophageal and gastric tissues. Expressed at higher levels in tumor.

Monoclonal Antibody; Extracellular Matrix

The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including Collagen, gelatin, Fibronectin, Laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP-3, MMP-10 and MMP-11 (also designated stromelysin-1, 2 and 3, respectively) activate procollagenase. MMP-3 activation of procollagenase can occur via two pathways. Direct activation by MMP-3 is slow and activation by MMP-3 in conjunction with tissue or plasma proteinases is rapid. MMP-10 is expressed in small intestine, and at lower levels in lung and heart. MMP-11 is specifically expressed in stromal cells of breast carcinomas and contributes to epithelial cell malignancies.

4505217

NP_002413.1

NM_002422.3

P08254

Activation Of Matrix Metalloproteinases Pathway (576264); Assembly Of Collagen Fibrils And Other Multimeric Structures Pathway (730306); Collagen Formation Pathway (645288); Degradation Of Collagen Pathway (730309); Degradation Of Collagen Pathway (827690); Degradation Of The Extracellular Matrix Pathway (576263); Degradation Of The Extracellular Matrix Pathway (827688); EGFR Transactivation By Gastrin Pathway (645296); Extracellular Matrix Organization Pathway (576262); Extracellular Matrix Organization Pathway (827676)

Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. This gene encodes an enzyme which degrades fibronectin, laminin, collagens III, IV, IX, and X, and cartilage proteoglycans. The enzyme is thought to be involved in wound repair, progression of atherosclerosis, and tumor initiation. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3. [provided by RefSeq, Jul 2008]

Function: Can degrade fibronectin, laminin, gelatins of type I, III, IV, and V; collagens III, IV, X, and IX, and cartilage proteoglycans. Activates procollagenase. Catalytic activity: Preferential cleavage where P1', P2' and P3' are hydrophobic residues. Cofactor: Binds 4 calcium ions per subunit.Binds 2 zinc ions per subunit. Subcellular location: Secreted extracellular space extracellular matrix . Probable. Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. Ref.13. Involvement in disease: Coronary heart disease 6 (CHDS6) [MIM:614466]: A multifactorial disease characterized by an imbalance between myocardial functional requirements and the capacity of the coronary vessels to supply sufficient blood flow. Decreased capacity of the coronary vessels is often associated with thickening and loss of elasticity of the coronary arteries.Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. A polymorphism in the MMP3 promoter region is associated with the risk of coronary heart disease and myocardial infarction, due to lower MMP3 proteolytic activity and higher extracellular matrix deposition in atherosclerotic lesions. Ref.11 Ref.12. Sequence similarities: Belongs to the peptidase M10A family.Contains 4 hemopexin repeats.

0.2 mg

325 USD