Recombinant Human MMP-9 Protein

Item Number

rp181214

• Product Name: Recombinant Human MMP-9 Protein
• Synonyms: matrix metalloproteinase-9 | MMP9 | MMP-9 | type V collagenase | 92 kDa gelatinase | 92 kDa type IV collagenase | CLG4B | EC 3.4.24 | EC 3.4.24.35 | Gelatinase B | GELB | macrophage gelatinase | MANDP2 | matrix metallopeptidase 9 | matrix metalloproteinas
• Grade: Animal Free, Bioactive, Carrier Free, High Performance
• Specifications & Purity: Animal Free, Carrier Free, Bioactive, High performance, ≥95%(SDS-PAGE)
• Bioactivity: 1. Measured in a cell migration assay using A549 cells. 5.0 ng/mL of Recombinant Human MMP-9 can effectively induce A549 cells migration. 2. Immobilized Recombinant Human MMP-9 Protein (rp181214) at 1.0 μg/mL can bind Andecaliximab (anti-MMP9), the EC50
• Endotoxin Concentration: ＜1.0 EU/μg
• Expression System: HEK293
• Amino Acids: 1-707 aa
• Sequence: MSLWQPLVLVLLVLGCCFAAPRQRQSTLVLFPGDLRTNLTDRQLAEEYLYRYGYTRVAEMRGESKSLGPALLLLQKQLSLPETGELDSATLKAMRTPRCGVPDLGRFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDAFARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGVVVPTRFGNADGAACHFPFIFEGRSYSACTTDGRSDGLPW
• Protein Tag: C-His
• Predicted molecular weight: 77.2 kDa
• SDS-PAGE: 81.8-106.3 kDa, under reducing condition.

Product Description

Purity: ≥95%, by SDS-PAGE visualized with Coomassie® Blue Staining.
Description：
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-9 (gelatinase B) can degrade a broad range of substrates including gelatin, collagen types IV and V, elastin and proteoglycan core protein. It is believed to act synergistically with interstitial collagenase (MMP-1) in the degradation of fibrillar collagens as it degrades their denatured gelatin forms. MMP-9 is produced by keratinocytes, monocytes, macrophages and PMN leukocytes. MMP-9 is present in most cases of inflammatory responses. Structurally, MMP-9 maybe be divided into five distinct domains: a pro-domain which is cleaved upon activation, a gelatin-binding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a proline-rich linker region, and a carboxyl terminal hemopexin-like domain.