Active Recombinant Human MMP3, His-tagged

• Cat.No.: MMP3-200H
• Product Overview: Recombinant Human MMP3 is a proform of the Human MMP3 [Tyr18-Cys477 (Lys45Glu)] and fused with a ployhistide tag at the C-terminus. It was expressed in HEK 293Cells.

Specification

• Cat. No.: MMP3-200H
• Description: MMP-3 enzyme is also known as Stromelysin-1or as Transin-1 which hydrolyzes natural collagen at physiological pH and temperature. It dissolves the intervertebral nucleus pulposus and annulus fibrosus of Herniated Lumbar Intervertebral Disk. MMP-3 hydrolyzes components of the extracellular matrix like proteoglycan, laminin, fibronectin, gelatin and collagen types III, IV and IX. It also activates pro-MMP-9 and pro-MMP-8 and superactivates plasmin activated MMP-1. MMP-3 is secreted as a latent proenzyme and is activated by a variety of proteinases, e.g. plasmin, trypsin, chymotrypsin, cathepsin G or human neutrophil elastase. MMP-3 was found to be capable of activating the precursor of IL1-beta.
• Source: HEK293 Cells
• Molecular Mass: 52kDa
• Purity: Greater than 95% as determined by SDS-PAGE.
• Formulation: Supplied as a 0.2µm filtered solution in Tris, NaCl and Brij35.
• Bio-activity: The activity was measured by its ability to cleave the fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK(Dnp)-NH2. The specific activity is > 150 pmoles/min/µg.
• Storage: Store at -20°C. Avoid multiple freeze-thaw cycles.
• OfficialSymbol: MMP3

Gene Information

• Gene Name: MMP3 matrix metallopeptidase 3 (stromelysin 1, progelatinase) [ Homo sapiens ]
• Synonyms: matrix metallopeptidase 3 (stromelysin 1, progelatinase); SL-1; STMY; STR1; CHDS6; MMP-3; STMY1; MGC126102; transin-1; MMP3; MGC126103; matrix metalloproteinase 3; CHDS6; Transin-1; proteoglycanase; MGC126104; Matrix metalloproteinase-3; EC 3.4.24.17
• Gene ID: 4314
• mRNA Refseq: NM_002422
• Protein Refseq: NP_002413
• MIM: 185250
• UniProt ID: P08254
• Chromosome Location: 11q22.3
• Function: calcium ion binding; metalloendopeptidase activity; peptidase activity; zinc ion binding