"MMP9" Related Products

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Recombinant Human matrix metallopeptidase 9, His-tagged

Cat. No.: MMP9-105H
Product Overview: Recombinant Human MMP-9 comprises a 338aa fragment (113-450) corresponding to the catalytic domain of the protein and is expressed in E. coli with an N-terminal 6xHis tag.
Description: Matrix metalloproteinases are a family of zinc and calcium-dependent endopeptidases, which degrade extracellular matrix proteins. MMP-9 is secreted as a 92kDa zymogen. Cleavage of pro-MMP-9 results in the active enzyme with a molecular weight of ~82kDa. MMP-9 has a gelatin-binding domain consisting of three fibronectin type II units, a catalytic domain containing the zinc-binding site, a proline-rich type V collagen-homologous domain and a hemopexin-like domain. MMP9 is produced by monocytes, macrophages, neutrophils, keratinocytes, fibroblasts, osteoclasts and endothelial cells, and is involved in inflammatory responses, tissue remodelling, wound healing, tumour growth and metastasis.
Source: E.coli.
Purity: >95% by SDS-PAGE
Form: Liquid
Storage: Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. Please avoid freeze thaw cycles.
Gene Name: MMP9 matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase) [ Homo sapiens ]
Synonyms: Matrix metalloproteinase 9; gelatinase B; 92kD gelatinase; 92kD type IV collagenase precursor;CLG4B; GELB; MMP9; CLG4B; GELB; MMP-9; matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase); matrix metalloproteinase 9; OTTHUMP00000031674; type V collagenase; macrophage gelatinase; EC 3.4.24.35; 92 kDa gelatinase; 92 kDa type IV collagenase; Gelatinase B; matrix metallopeptidase 9 (gelatinase B, 92kDa gelatinase, 92kDa type IV collagenase).
Gene ID: 4318
mRNA Refseq: NM_004994
Protein Refseq: NP_004985
MIM: 120361
UniProt ID: P14780
Chromosome Location: 20q11.2-q13.1
Function: calcium ion binding; collagen binding; metalloendopeptidase activity; peptidase activity; zinc ion binding

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