Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
accession | P16035 |
express system | HEK293 |
product tag | C-His |
purity | > 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC |
background | Tissue inhibitors of metalloproteinases or TIMPs are a family of proteins that regulate the activation and proteolytic activity of the zinc enzymes known as matrix metalloproteinases (MMPs).TIMP-2 is a non N-glycosylated protein with a molecular mass of 22 kDa produced by a wide range of cell types, which inhibits MMPs non-covalently by the formation of binary complexes. TIMP-2 also has erythroid‑potentiating and cell growth promoting activities. |
molecular weight | The protein has a predicted MW of 22.9 kDa. Due to glycosylation, the protein migrates to 24-26 kDa based on Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Human TIMP-2 Protein 4679
$240.00 – $800.00
Summary
- Expression: HEK293
- Functional: Yes (ELISA)
- Amino Acid Range: Cys27-Pro220
Human TIMP-2 Protein 4679
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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Tissue inhibitors of metalloproteinases or TIMPs are a family of proteins that regulate the activation and proteolytic activity of the zinc enzymes known as matrix metalloproteinases (MMPs).TIMP-2 is a non N-glycosylated protein with a molecular mass of 22 kDa produced by a wide range of cell types, which inhibits MMPs non-covalently by the formation of binary complexes. TIMP-2 also has erythroid-potentiating and cell growth promoting activities. |
Protein names Metalloproteinase inhibitor 2 (CSC-21K) (Tissue inhibitor of metalloproteinases 2) (TIMP-2) |
Gene names TIMP2,TIMP2 |
Protein family Protease inhibitor I35 (TIMP) family |
Mass 9606Da |
Function Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19. |
Catalytic activity BINDING 27; /ligand="Zn(2+)"; /ligand_id="ChEBI:CHEBI:29105"; /ligand_note="ligand shared with metalloproteinase partner"; /evidence="ECO:0000269|PubMed:24073280, ECO:0007744|PDB:4ILW" |
Subellular location Secreted. |
Structure Interacts (via the C-terminal) with MMP2 (via the C-terminal PEX domain); the interaction inhibits the MMP2 activity. |
Post-translational modification The activity of TIMP2 is dependent on the presence of disulfide bonds. |
Target Relevance information above includes information from UniProt accession: P16035 |
The UniProt Consortium |
Data
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