Weight | 1 lbs |
---|---|
Dimensions | 9 × 5 × 2 in |
accession | A0A2K5UU71 |
express system | HEK293 |
product tag | C-His |
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 77.44 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. |
Cynomolgus MMP-9 Protein 3059
$315.00 – $1,050.00
Summary
- Expression: HEK293
- Functional: Yes (ELISA)
- Amino Acid Range: Ala20-Asp706
Cynomolgus MMP-9 Protein 3059
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 (EC 3.4.24.35) (92 kDa gelatinase) (92 kDa type IV collagenase) (Gelatinase B) |
Gene names MMP9,MMP9 |
Protein family Peptidase M10A family |
Mass 78366Da |
Function FUNCTION: Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration. Could play a role in bone osteoclastic resorption. Cleaves KiSS1 at a Gly-|-Leu bond. Cleaves NINJ1 to generate the Secreted ninjurin-1 form. 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. {ECO:0000256|ARBA:ARBA00045780}. |
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:0000256|ARBA:ARBA00001425}; |
Subellular location SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}. |
Structure SUBUNIT: Exists 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. {ECO:0000256|ARBA:ARBA00024379}. |
Target Relevance information above includes information from UniProt accession: A0A2K5UU71 |
The UniProt Consortium |
Data
Publications
Publications
pmid | title | authors | citation |
---|---|---|---|
We haven't added any publications to our database yet. |
Protocols
relevant to this product |
---|
Documents
# | ||
---|---|---|
Please enter your product and batch number here to retrieve product datasheet, SDS, and QC information. |