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Human MMP-1 Phycoerythrin MAb (Clone 36607)  100 TESTS图1

Human MMP-1 Phycoerythrin MAb (Clone 36607) 100 TESTS

2024-11-24 16:56IP属地 广东省东莞市 电信00留言

Applications

Please Note: Optimal dilutions should be determined by each laboratory for each application.  are available in the Technical Information section on our website.

Data Examples

Intracellular Staining by Flow Cytometry      
     

Detection of MMP‑1 in PC‑3 Human Cell Line by Flow Cytometry. PC‑3 human prostate cancer cell line was stained with Mouse Anti-Human MMP‑1 PE‑conjugated Monoclonal Antibody (Catalog # IC9011P, filled histogram) or isotype control antibody (Catalog # , open histogram). To facilitate intracellular staining, cells were fixed with Flow Cytometry Fixation Buffer (Catalog # ) and permeabilized with Flow Cytometry Permeabilization/Wash Buffer I (Catalog # ). View our protocol for .

Preparation and Storage

Background: MMP-1

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, IGF-BP3, IGF-BP5, 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 (1).

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