Weight | 1 lbs |
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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 |
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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 |
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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 9541Da |
Catalytic activity BINDING 99; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="2"; /ligand_note="catalytic"; /note="in inhibited form"; /evidence="ECO:0000256|PIRSR:PIRSR621190-2"; BINDING 131; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000256|PIRSR:PIRSR621190-2"; BINDING 165; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000256|PIRSR:PIRSR621190-2"; BINDING 175; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000256|PIRSR:PIRSR621190-2"; BINDING 177; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000256|PIRSR:PIRSR621190-2"; BINDING 182; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000256|PIRSR:PIRSR621190-2"; BINDING 183; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000256|PIRSR:PIRSR621190-2"; BINDING 187; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000256|PIRSR:PIRSR621190-2"; BINDING 190; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000256|PIRSR:PIRSR621190-2"; BINDING 201; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="2"; /evidence="ECO:0000256|PIRSR:PIRSR621190-2"; BINDING 203; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_label="1"; /evidence="ECO:0000256|PIRSR:PIRSR621190-2"; BINDING 205; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000256|PIRSR:PIRSR621190-2"; BINDING 206; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000256|PIRSR:PIRSR621190-2"; BINDING 208; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="3"; /evidence="ECO:0000256|PIRSR:PIRSR621190-2"; BINDING 208; /ligand="Ca(2+)"; /ligand_id="ChEBI:CHEBI:29108"; /ligand_label="1"; /evidence="ECO:0000256|PIRSR:PIRSR621190-2" |
Subellular location Secreted, extracellular space, extracellular matrix . |
Target Relevance information above includes information from UniProt accession: A0A2K5UU71 |
The UniProt Consortium |
Publications
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We haven't added any publications to our database yet. |
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