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MMP-9[Biotin], His & Avi, Human

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.
$660.00
Z04561-100

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Product Introduction
Species Human
Protein Construction
MMP-9 (Ala20-Asp707)
Accession # P14780		 His Avi
N-term C-term
Conjugate Biotin
Purity > 95% as determined by Bis­Tris PAGE 
Endotoxin Level Less than 1EU per μg by the LAL method.
Biological Activity Measured by its binding ability in a functional ELISA. Test result was comparable to standard batch.
Expression System HEK293
Theoretical Molecular Weight 79.3 kDa
Apparent Molecular Weight Due to glycosylation, the protein migrates to 95-105 kDa based on Bis-Tris PAGE result.
Formulation Lyophilized from 0.22μm filtered solution in PBS (pH 7.4).
Reconstitution Centrifuge the tube before opening. Reconstituting to a concentration more than 100 μg/ml is recommended. Dissolve the lyophilized protein in distilled water.
Storage & Stability Upon receiving, the product remains stable for 6 months at -20℃ or below. Upon reconstitution, the product should be stable for 3 months at -80℃. Avoid repeated freeze-thaw cycles.
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MMP-9[Biotin], His & Avi, Human

Immobilized Anti-MMP-9 Antibody, hFc Tag at 1μg/ml (100μl/well) on the plate. Dose response curve for MMP-9[Biotin], His & Avi, Human, His Tag with the EC50 of 31.0ng/ml determined by ELISA. »

MMP-9[Biotin], His & Avi, Human

The purity of MMP-9[Biotin], His & Avi, Human is greater than 95% as determined by SEC-HPLC. »

MMP-9[Biotin], His & Avi, Human

MMP-9[Biotin], His & Avi, Human on Bis-Tris PAGE under reduced condition. The purity is greater than 95%. »

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Background
Target 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.
Synonyms MMP-9; GELB; CLG4B; MANDP2; Gelatinase B
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For research use only. Not intended for human or animal clinical trials, therapeutic or diagnostic use.