Detects both the pro and active forms of human MMP-3 in direct ELISAs and Western blots. In direct ELISAs, 50‑100% cross-reactivity with recombinant mouse MMP-3 is observed, 10% cross-reactivity with recombinant human (rh) MMP-10 is observed and no cross-reactivity with rhMMP-1, -2, -7, -8, -9, -12 or -13 is observed.
Monoclonal Mouse IgG1 Clone # 50647
Protein A or G purified from hybridoma culture supernatant
Chinese hamster ovary cell line CHO-derived recombinant human MMP‑3 Tyr18-Cys477 Accession # P08254
Supplied 0.2 mg/mL in a saline solution containing BSA and Sodium Azide.
Detection of MMP-3 in Human MG-63 Cell Line byFlow Cytometry.
MG-63 Human osteosarcoma cell line was stainedwith Mouse Anti-HumanMMP-3 Alexa Fluor® 405-conjugated Monoclonal Antibody (Catalog #IC513V, filled histogram) or isotype control antibody (Catalog # IC002V,open histogram). To facilitate intracellular staining, cells were fixed withFlow Cytometry Fixation Buffer (Catalog # FC004)and permeabilized with Flow Cytometry Permeabilization/Wash Buffer I(Catalog # FC005).View our protocol for Staining Intracellular Molecules.
Preparation and Storage
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze.
12 months from date of receipt, 2 to 8 °C as supplied.
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-3 (stromelysin-1), can degrade a broad range of substrates including collagen alpha chains, aggrecan, laminin, fibronectin, elastin, casein, alpha -1 antitrypsin, myelin basic protein, IL-1 beta, IGFBP-3, pro MMP-1, pro MMP-7, pro MMP-8, pro MMP-9 and pro MMP-13. MMP-3 does not cleave the triple helical region of interstitial collagens, a characteristic which distinguishes the stromelysins from the collagenases. The MMP-3 substrate repertoire extends beyond extracellular matrix proteins and implicates MMP-3 in roles other than direct tissue remodelling, for instance, enzyme cascades and cytokine regulation. MMP-3 is expressed by fibroblasts, chrondrocytes, osteoblasts, endothelial cells, smooth muscle cells and macrophages. Structurally, MMP-3 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.
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