货号 | IC9081U-100UG |
别名 | CLG1HNC; Collagenase 2; EC 3.4.24; EC 3.4.24.34; matrix metallopeptidase 8 (neutrophil collagenase); matrix metalloproteinase 8 (neutrophil collagenase); Matrix metalloproteinase-8; MMP8; MMP-8; neutrophil collagenase; PMNL collagenase; PMNL-CL | 全称 | Matrix Metalloproteinase 8 |
应用 | Intracellular Staining by Flow Cytometry |
目标/特异性 | Detects both pro and active forms of human MMP-8 in Western blots. In Western blots, no cross-reactivity with recombinant human (rh) MMP-1, -2, -3, -7, -9, -10, -12, or -13 is observed. |
使用方法 | Intracellular Staining by Flow Cytometry: 0.25-1 µg/106cells |
来源 | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
产品组分 |
供应商 | R&D Systems |
Entrez Gene IDs | 4317 (Human); 17394 (Mouse); 63849 (Rat) |
免疫原 | Mouse myeloma cell line NS0-derived recombinant human MMP‑8 Phe21-Gly467 Accession # AAZ38714 |
生物活性 | Human |
标记 | Alexa Fluor 350 |
背景 | Matrix metalloproteinases (MMPs) are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-8 (neutrophil collagenase) is expressed in neutrophils, where it is stored in specific granules. MMP-8 release from the neutrophils is stimulated by various factors such as interleukins 1 and 8, TNF-alpha and GM-CSF. MMP-8 is capable of cleaving types I, II and III triple-helical collagen, gelatin peptides, fibronectin, proteoglycans, aggrecan, serpins, beta -casein and peptides such as angiotensin and substance P. In addition to its function in phagocytosis, MMP‑8 has a high capacity for infiltrating connective tissue, and is implicated in the breakdown of the extracellular matrix in diseases such as rheumatoid arthritis. Structurally, MMP-8 consists of several domains: a pro-domain that is cleaved upon activation, a catalytic domain containing the zinc-binding site, a short hinge region and a hemopexin-like domain. MMP-8 is heavily glycosylated. |
运输条件 | Blue Ice |
存放说明 | 4℃ |
参考文献 |
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