Genetic Strategies: Western blot shows lysates of PC‑3 human prostate cancer parental cell line and MMP-1 knockout PC‑3 cell line (KO). PVDF membrane was probed with 1 µg/mL of Goat Anti-Human MMP‑1 ...read more
MMP‑1 was detected in immersion fixed paraffin-embedded sections of human ovarian cancer tissue using 15 µg/mL Goat Anti-Human MMP‑1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF901) overnight at 4 ...read more
MMP‑1 was detected in immersion fixed paraffin-embedded sections of human prostate tissue using Goat Anti-Human MMP‑1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF901) at 10 µg/mL overnight at 4 °C. ...read more
Western blot shows lysates of PC‑3 human prostate cancer cell line and HEK001 human epidermal keratinocyte cell line. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human MMP‑1 Antigen Affinity-purified ...read more
Mouse myeloma cell line NS0-derived recombinant human MMP-1 Phe20-Asn469 Accession # P03956
Detects human MMP-1 in ELISAs and Western blots. In sandwich immunoassays, less than 0.5% cross-reactivity with recombinant human (rh) MMP‑2, rhMMP-3, rhMMP-7, rhMMP-8, rhMMP-9, rhMMP-10, rhMMP-12, rhMMP-13, and rhMMP-16 is observed.
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Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-1 (interstitial collagenase), can degrade a broad range of substrates including types I, II, III, VII, VIII, and X collagens as well as casein, gelatin, alpha -1 antitrypsin, myelin basic protein, L-Selectin, pro-TNF, IL-1 beta, IGFBP-3, IGFBP-5, pro-MMP-2, and pro-MMP-9. A significant role of MMP-1 is the degradation of fibrillar collagens in extracellular matrix remodeling, characterized by the cleavage of the interstitial collagen triple helix into ¾, ¼ fragments. However, as the list of substrates above illustrates, the role of MMP-1 is more diverse than originally envisaged, and may involve enzyme cascades, cytokine regulation, and cell surface molecule modulation. MMP-1 is expressed by fibroblasts, keratinocytes, endothelial cells, monocytes, and macrophages. Structurally, MMP-1 may be divided into several distinct domains; a pro-domain which is cleaved upon activation; a catalytic domain containing the zinc binding site; a short hinge region and a carboxyl terminal (hemopexin-like) domain.
Cawston, T.E. (2004) in Interstitial Collagenase. Barrett, A.J. et al. (eds): Handbook of Proteolytic Enzymes, San Diego: Academic Press, p. 472.
This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.
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