Anti-MMP3 Antibody [1B4] (A279080)

Anti-MMP3 Antibody [1B4]

Mouse monoclonal [1B4] antibody to MMP3.

This antibody recognises human matrix metalloproteinase 3, also known as MMP-3, stromelysin-1 or transin-1. MMP-3 in its pro-form is a 477 amino acid ~54kDa zinc dependent endopeptidase processed to a 378 amino acid, ~45 kDa peptide in the mature form containing 4 hemopexin-like repeats. MMPs are also involved in cell proliferation, migration, differentiation and apoptosis. Most MMP’s are synthesised as inactive zymogens and a propeptide region must be cleaved off before the enzyme becomes active. Their expression is increased dramatically in a variety of cancer types, where it indicates invasive disease and a poor prognosis. MMP-3 can degrade proteoglycan, fibronectin, laminin, and type IV collagen, but not interstitial type I collagen. It can activate other MMP’s and may be involved in the repair processes of the heart after myocardial infarction. Mouse anti human MMP-3 antibody, clone 1B4 has been used successfully for the identification of MMP-3 in gastric cancer by both Western blotting and immunohistochemistry

WB, IHC-P, ELISA

Human

Ovalbumin conjugated synthetic peptide corresponding to a region within the C-terminus of human MMP-3.

Mouse

Monoclonal

1B4

IgG1

Protein G affinity chromatography of tissue culture supernatant.

Approximately 50 kDa in cell lysates.

Liquid

Supplied in Phosphate Buffered Saline with 0.09% Sodium Azide.

Shipped at ambient temperature. Upon delivery aliquot and store at -20°C. When thawed, aliquot the sample as needed. Short term (up to 4 weeks): store at 4°C. Long term: store at -20°C. Avoid freeze / thaw cycles. Storage in frost free freezers is not recommended.

Mouse anti Human MMP-3 antibody, clone 1B4 recognizes human matrix metalloproteinase 3, also known as MMP-3, stromelysin-1 or transin-1. MMP-3 in its pro-form is a 477 amino acid ~54kDa zinc dependent endopeptidase processed to a 378 amino acid, ~45 kDa peptide in the mature form containing 4 hemopexin-like repeats. MMPs are also involved in cell proliferation, migration, differentiation and apoptosis (Jana et al. 2012). Most MMP’s are synthesised as inactive zymogens and a propeptide region must be cleaved off before the enzyme becomes active. Their expression is increased dramatically in a variety of cancer types, where it indicates invasive disease and a poor prognosis (Holmberg et al. 2013). MMP-3 can degrade proteoglycan, fibronectin, laminin, and type IV collagen, but not interstitial type I collagen (Wilhelm et al. 1993). It can activate other MMP’s and may be involved in the repair processes of the heart after myocardial infarction (Wang et al. 2011).Mouse anti human MMP-3 antibody, clone 1B4 has been used successfully for the identification of MMP-3 in gastric cancer by both Western blotting and immunohistochemistry (Murray et al. 1998)

Matrix metalloproteinase-3, MMP-3, SL-1, STMY1, Stromelysin-1, Transin-1