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
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.pmid | title | authors | citation |
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Protocols
relevant to this product |
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Documents
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