MMP 9 (MMP9)
(Matrix Metallopeptidase 9 (Gelatinase B, 92kDa Gelatinase, 92kDa Type IV Collagenase) (MMP9))
Type de proteíne
Recombinant
Attributs du protein
AA 20-469
Origine
Humain
Source
HEK-293 Cells
Purification/Conjugué
Cette MMP 9 protéine est marqué à la His tag.
Séquence
AA 20-469
Attributs du produit
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.
Crystallography grade
MMP9
Origine: Souris
Hôte: Cellules d'insectes
Recombinant
>95 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
WB, SDS, ELISA, Crys
Restrictions
For Research Use only
Format
Lyophilized
Buffer
50 mM Tris, 150 mM NaCl, pH 7.5
Conseil sur la manipulation
Please avoid repeated freeze-thaw cycles.
Stock
-20 °C
Stockage commentaire
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.
Antigène
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.