MMP 9 (MMP9)
(Matrix Metallopeptidase 9 (Gelatinase B, 92kDa Gelatinase, 92kDa Type IV Collagenase) (MMP9))
Type de proteíne
Recombinant
Origine
Humain
Source
HEK-293 Cells
Purification/Conjugué
Cette MMP 9 protéine est marqué à la His-Avi Tag,Biotin.
Séquence
Ala20-Asp707
Pureté
> 95% as determined by Tris-Bis PAGE,> 95% as determined by HPLC
Stérilité
0.22 μm filtered
niveau d'endotoxine
Less than 1EU per μg by the LAL method.
Biological Activity Comment
Immobilized Anti-MMP-9 Antibody, hFc Tag at 0.5μg/ml (100μl/well) on the plate. Dose response curve for Biotinylated Human MMP-9, His Tag with the EC50 of 14.3ng/ml determined by ELISA. See testing image for detail.
MMP9
Origine: Humain
Hôte: Escherichia coli (E. coli)
Recombinant
> 95 % as determined by reducing SDS-PAGE.
Restrictions
For Research Use only
Format
Lyophilized
Reconstitution
Centrifuge tubes before opening. Reconstituting to a concentration more than 100 μg/mL is recommended (usually we use 1 mg/mL solution for lyophilization). Dissolve the lyophilized protein in distilled water.
Buffer
Lyophilized from 0.22μm filtered solution in PBS ( pH 7.4). Normally 5 % trehalose is added as protectant before lyophilization.
Stock
4 °C,-80 °C
Stockage commentaire
Reconstituted protein stable at -80°C for 12 months, 4°C for 1 week. Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Date de péremption
12 months
Antigène
MMP 9 (MMP9)
(Matrix Metallopeptidase 9 (Gelatinase B, 92kDa Gelatinase, 92kDa Type IV Collagenase) (MMP9))
MMP-9, GELB, CLG4B, MANDP2, Gelatinase B,Matrix metalloproteinase 9 (MMP9) contributes to this process and deficiencies in the MMP9 lead to impaired healing. Inappropriate expression of MMP9 also contributes to impaired re-epithelialization. Previously we demonstrated that FOXO1 was activated in wound healing but to higher levels in diabetic wounds. To address mechanisms of impaired re-epithelialization we examined MMP9 expression in vivo in full thickness dermal scalp wounds created in experimental K14.
Poids moléculaire
79.3 kDa. Due to glycosylation, the protein migrates to 95-105 kDa based on Tris-Bis PAGE result.