Name :
MMP-9 Protein
Description :
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.
Species :
Cynomolgus
Uniprotkb :
HEK293
Tag :
C-His
Synonyms :
MMP-9, CLG4B, Gelatinase B, MANDP2, GELB
Construction :
Recombinant Cynomolgus MMP-9 Protein is expressed from HEK293 with His tag at the C-Terminus. The protein needs to be activated by APMA to have hydrolytic activity. It contains Ala20-Asp706.[Accession |A0A2K5UU71]
Protein Purity :
> 95% as determined by Tris-Bis PAGE; > 95% as determined by HPLC
Molecular Weight :
The protein has a predicted MW of 77.44 kDa. Due to glycosylation, the protein migrates to 85-100 kDa based on Tris-Bis PAGE result.
Endotoxin :
Less than 1EU per μg by the LAL method.
Formulatione :
Lyophilized from 0.22μm filtered solution in PBS (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization.
Reconstitution :
Centrifuge the tube before opening. Reconstituting to a concentration more than 100 μg/ml is recommended. Dissolve the lyophilized protein in distilled water.
Stability & Storage :
-20 to -80°C for 12 months as supplied from date of receipt. -20 to -80°C for 3-6 months in unopened state after reconstitution. 2-8°C for 2-7 days after reconstitution. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Shipping :
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Research Background :
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.
References and Literature :
1. Zhang C, et al. FOXO1 deletion in keratinocytes improves diabetic wound healing through MMP9 regulation. Sci Rep. 2017;7(1):10565. Published 2017 Sep 5. doi:10.1038/s41598-017-10999-3
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