MMP 9 (MMP9)
(Matrix Metallopeptidase 9 (Gelatinase B, 92kDa Gelatinase, 92kDa Type IV Collagenase) (MMP9))
Protein-Typ
Recombinant
Proteineigenschaft
AA 20-469
Spezies
Human
Quelle
HEK-293 Cells
Aufreinigungstag / Konjugat
Dieses MMP 9 Protein ist gelabelt mit His tag.
Sequenz
AA 20-469
Produktmerkmale
This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 50.8 kDa. The protein migrates as 55-65 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
MMP9
Spezies: Human
Wirt: HEK-293 Cells
Recombinant
The purity of the protein is greater than 95 % as determined by SDS-PAGE and Coomassie blue staining.
MMP9
Spezies: Human
Wirt: HEK-293 Cells
Recombinant
The purity of the protein is greater than 85 % as determined by SDS-PAGE and Coomassie blue staining.
MMP9
Spezies: Human
Wirt: HEK-293 Cells
Recombinant
The purity of the protein is greater than 95 % as determined by SDS-PAGE and Coomassie blue staining.
MMP9
Spezies: Maus
Wirt: HEK-293 Cells
Recombinant
> 95 % as determined by SDS-PAGE
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Lyophilized
Buffer
50 mM Tris, 150 mM NaCl, pH 7.5
Handhabung
Please avoid repeated freeze-thaw cycles.
Lagerung
-20 °C
Informationen zur Lagerung
Lyophilized Protein should be stored at -20 °C or lower for long term storage. Upon reconstitution, working aliquots should be stored at -20 °C or -70 °C. Avoid repeated freeze-thaw cycles.
Target
MMP 9 (MMP9)
(Matrix Metallopeptidase 9 (Gelatinase B, 92kDa Gelatinase, 92kDa Type IV Collagenase) (MMP9))
Matrix metallopeptidase 9 (MMP-9) is also known as 92 kDa type IV collagenase, 92 kDa gelatinase or gelatinase B (GELB), CLG4B, is secreted from neutrophils, macrophages, and a number of transformed cells, and is the most complex family member in terms of domain structure and regulation of its activity. . Structurally, MMP9 maybe be divided into five distinct domains: a prodomain which is cleaved upon activation, a gelatinbinding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a prolinerich linker region, and a carboxyl terminal hemopexinlike domain. This enzyme degrades various substrates including gelatin, collagen types IV and V, and elastin. MMP9 is involved in a variety of autoimmune diseases such as systemic lupus erythematosus, rheumatoid arthritis, and multiple sclerosis, and be regarded as a potential therapeutic target.