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Human MMP-9 Protein 4746

$315.00$1,050.00

Summary

  • Expression: HEK293
  • Functional: Yes (ELISA)
  • Amino Acid Range: Ala20-Asp707
SKU: 4746parent Categories: , Tags: , , ,
Weight1 lbs
Dimensions9 × 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:2551898, PubMed:1480034, PubMed:12879005). 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). Exists also 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}.
Target Relevance information above includes information from UniProt accession : P14780
The UniProt Consortium

Data

ELISA with Human MMP-9 Protein
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.
HPLC of Human MMP-9 Protein
The purity of Human MMP-9 is greater than 95% as determined by SEC-HPLC.
SDS-PAGE gel of Human MMP-9 Protein
Human MMP-9 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

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.




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