Mouse MMP-9 Protein 2947

Additional Information:
inaccessionP41245|express systemHEK293|product tagC-His|purity> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC|backgroundMatrix 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.|molecular weightThe protein has a predicted MW of 79.64 kDa. Due to glycosylation, the protein migrates to 80-110 kDa based on Tris-Bis PAGE result.|available size100 g, 500 g|endotoxinLess than 1EU per g by the LAL method.|Mouse MMP-9 Protein 2947proteinSize and concentration100, 500g and lyophilizedFormLyophilizedStorage InstructionsValid for 12 months from date of receipt when stored at -80C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.Storage bufferShipped at ambient temperature.Purity> 95% as determined by Tris-Bis PAGEtarget relevanceMatrix 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.Protein namesMatrix metalloproteinase-9 (MMP-9) (EC 3.4.24.35) (92 kDa gelatinase) (92 kDa type IV collagenase) (Gelatinase B) (GELB)Gene namesMmp9,Mmp9 Clg4bProtein familyPeptidase M10A familyMass80535DaFunctionMatrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (By similarity). Could play a role in bone osteoclastic resorption (PubMed:8132709). Cleaves KiSS1 at a Gly-|-Leu bond (By similarity). Cleaves NINJ1 to generate the Secreted ninjurin-1 form (PubMed:23142597, PubMed:32883094). Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide (By similarity).Catalytic activityReaction=Cleavage of gelatin types I and V and collagen types IV and V.; EC=3.4.24.35; Evidence=;Subellular locationSecreted, extracellular space, extracellular matrixStructureExists as monomer or homodimer; disulfide-linked. Exists also as heterodimer with LCN2. Macrophages and transformed cell lines produce only the monomeric form. Interacts with ECM1.Post-translational modificationN- and O-glycosylated.Target Relevance information above includes information from UniProt accession: P41245The UniProt Consortium|