Western blot shows Recombinant Human MMP-3 Western Blot Standard Protein (Catalog # WBC015) and lysate of U‑118‑MG human glioblastoma/astrocytoma cell line. PVDF membrane was probed with 2 µg/mL of Goat ...read more
MMP‑3 was detected in immersion fixed paraffin-embedded sections of human bladder cancer tissue using Goat Anti-Human/Primate MMP‑3 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF513) at 10 µg/mL ...read more
MMP‑3 was detected in immersion fixed paraffin-embedded sections of human lung cancer using Goat Anti-Human/Primate MMP‑3 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF513) at 15 µg/mL overnight at 4 ...read more
Mouse myeloma cell line NS0-derived recombinant human MMP‑3 Tyr18-Cys477 (Lys45Glu) Accession # P08254
Detects human and primate MMP-3 in ELISAs and Western blots. In sandwich ELISAs, less than 2.5% cross-reactivity with recombinant human (rh) MMP‑10 is observed and less than 0.1% cross-reactivity with rhMMP-1, -2, -7, -8, -9, -12, -13, and recombinant mouse MMP‑9 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-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.
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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PRODUCT AVAILABILITY: Update Regarding the Evolving COVID-19 Situation
Bio-Techne appreciates the critical role that you and our products and services play in research efforts to further scientific innovation and discovery. We are continually assessing our manufacturing and supplier capabilities during the COVID-19 situation and are implementing precautionary measures to ensure uninterrupted supply of products and services. Currently, and as we abide by local shelter in place orders across the world, we are fully operational and do not anticipate any material supply disruptions across our Bio-Techne brands and product lines. As the situation evolves, our goal is to utilize preventive measures to reduce the threat that COVID-19 poses to our ability to meet the needs of our customers globally.