Biotinylated Human MMP-9 Protein (pro form)
Catalog No: MMP9-HB001
- Species
- Human
- Expression System
- HEK293
- Tag
- His, Avi
- Activity
- Activity verified
Product overview
Recombinant Biotinylated Human MMP-9 Protein is expressed in HEK293 cells with a His tag and Avi tag at the C-terminus. The protein needs to be activated by APMA for an activated form. It contains amino acid residues Ala20-Asp707 (UniProt accession: P14780).
Product Details
- Molecular Aliases
- MMP-9; GELB; CLG4B; MANDP2; Gelatinase B; MMP9
- Protein Length
- Ala20-Asp707
- Expression System
- HEK293
- Theoretical Molecular Weight
- The protein has a predicted MW of 79.3 kDa. Due to glycosylation, the protein migrates to 95-105 kDa based on Bis-Tris PAGE result.
- Purity
- > 95% as determined by Bis-Tris PAGE > 95% as determined by HPLC
- Endotoxin
- Less than 1 EU per μg by the LAL method.
- Buffer / Formulation
- Lyophilized from 0.22 μm filtered solution in 50mM Tris, 10mM CaCl 2, 150mM NaCl, 0.05% Brij-35 (w/v) (pH 7.5). Normally 8% trehalose is added as protectant before lyophilization.
- State
- Lyophilized
- Storage Conditions
- -20 to -80°C for 12 months as supplied from date of receipt. -80°C for 3 months after reconstitution. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
- Reconstitution Advice
- Dissolve the lyophilized protein in distilled water. Please refer to the Certificate of Analysis for detailed instructions.
Data Display
Biotinylated Human MMP-9 on Bis-Tris PAGE under reduced condition. The purity is greater than 95%.
The purity of Biotinylated Human MMP-9 is greater than 95% as determined by SEC-HPLC.
Immobilized Biotinylated Human MMP-9, His Avi tag at 0.5μg/ml (100μl/well) on the streptavidin precoated plate (5μg/ml). Dose response curve for Anti-MMP-9 Antibody, hFc Tag with the EC50 of 13.3ng/ml determined by ELISA. (QC Test)
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
- Zhang C, Lim J, Jeon HH, 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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