Human MMP-9 Protein 4746

$315.00 – $1,050.00

Summary

Expression: HEK293
Functional: Yes (ELISA)
Amino Acid Range: Ala20-Asp707

SKU: 4746parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	P14780
express system	HEK293
product tag	C-His-Avi
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
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.
molecular weight	The protein has a predicted MW of 79.3 kDa. Due to glycosylation, the protein migrates to 85-100 kDa based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Human MMP-9 Protein 4746

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
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.
Protein names Matrix metalloproteinase-9 (MMP-9) (EC 3.4.24.35) (92 kDa gelatinase) (92 kDa type IV collagenase) (Gelatinase B) (GELB) [Cleaved into: 67 kDa matrix metalloproteinase-9; 82 kDa matrix metalloproteinase-9]
Gene names MMP9,MMP9 CLG4B
Protein family Peptidase M10A family
Mass 78458Da
Function FUNCTION: Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (PubMed:12879005, PubMed:1480034, PubMed:2551898). Could play a role in bone osteoclastic resorption (By similarity). Cleaves KiSS1 at a Gly-\|-Leu bond (PubMed:12879005). Cleaves NINJ1 to generate the Secreted ninjurin-1 form (PubMed:32883094). Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments (PubMed:1480034). Degrades fibronectin but not laminin or Pz-peptide. {ECO:0000250\|UniProtKB:P41245, ECO:0000269\|PubMed:12879005, ECO:0000269\|PubMed:1480034, ECO:0000269\|PubMed:2551898, ECO:0000269\|PubMed:32883094}.
Catalytic activity CATALYTIC ACTIVITY: Reaction=Cleavage of gelatin types I and V and collagen types IV and V.; EC=3.4.24.35; Evidence={ECO:0000269\|PubMed:1480034};
Subellular location SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269\|PubMed:2551898}.
Tissues TISSUE SPECIFICITY: Detected in neutrophils (at protein level) (PubMed:7683678). Produced by normal alveolar macrophages and granulocytes. {ECO:0000269\|PubMed:7683678}.
Structure SUBUNIT: Exists as monomer or homodimer; disulfide-linked (PubMed:1281792, PubMed:7683678). Also exists as heterodimer with LCN2 (PubMed:1281792, PubMed:7683678). Macrophages and transformed cell lines produce only the monomeric form. Interacts with ECM1 (PubMed:16512877). {ECO:0000269\|PubMed:10644727, ECO:0000269\|PubMed:12051944, ECO:0000269\|PubMed:12077439, ECO:0000269\|PubMed:12126625, ECO:0000269\|PubMed:1281792, ECO:0000269\|PubMed:16512877, ECO:0000269\|PubMed:7683678}.; SUBUNIT: (Microbial infection) Interacts with Staphylococcus aureus protein SSL5; this interaction inhibits MMP9 activity. {ECO:0000269\|PubMed:20479083, ECO:0000269\|PubMed:29328525}.
Post-translational modification PTM: Processing of the precursor yields different active forms of 64, 67 and 82 kDa. Sequentially processing by MMP3 yields the 82 kDa matrix metalloproteinase-9. {ECO:0000269\|PubMed:1371271, ECO:0000269\|PubMed:1400481}.; PTM: N- and O-glycosylated. {ECO:0000269\|PubMed:1464361}.
Domain DOMAIN: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. {ECO:0000269\|PubMed:12077439}.
Target Relevance information above includes information from UniProt accession: P14780
The UniProt Consortium

Data

Immobilized Human MMP-9, His Tag at 0.5µg/ml (100µl/Well) on the plate. Dose response curve for Anti-MMP-9 Antibody, hFc Tag with the EC50 of 17.4ng/ml determined by ELISA.

The purity of Human MMP-9 is greater than 95% as determined by SEC-HPLC.

Human MMP-9 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

pmid	title	authors	citation
We haven't added any publications to our database yet.

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.