Purity>95% SDS-PAGE.FunctionMay play an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly- -Leu bond. Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide.BackgroundMatrix 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. In addition to the human enzyme, the recombinant mouse MMP-9 is also available.
Specification: ActiBioPure™, Bioactive, Animal Free, Carrier Free, Azide Free, High performance, ≥95%(SDS-PAGE)
Related Documents: https://ald-pub-files.oss-cn-shanghai.aliyuncs.com/aladdinsci/pdp/sds/1/RP148898-SCI_1331948757c7d1ac03de1f2146230d3b.pdf
- UPC:
- 41141704
- Condition:
- New
- Availability:
- 4-8 weeks
- Weight:
- 0.07 Ounces
- HazmatClass:
- No
- WeightUOM:
- LB
- MPN:
- rp148898-1mg
- Product Size:
- 1mg
