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Recombinant Swine Metalloproteinase Inhibitor 2 (TIMP2), N-His

Cat. No.AP9C744

Product TypeAnimal Proteins

Size

Product Overview

BioVenic's Recombinant Swine Metalloproteinase Inhibitor 2 (TIMP2), N-His is a recombinant protein expressed from E.coli. Its predicted molecular weight is N/A. The purity is>97% (SDS-PAGE).

Specifications

Type Recombinant Protein
Species Swine
Expression System E.coli
Purity >97% (SDS-PAGE)
Endotoxin < 1 EU/µg
Predicted Molecular Weight N/A
Physical State Lyophilized
Formulation The buffer before lyophilization is PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.

Target Information

Swine tissue inhibitors of metalloproteinase 2 (TIMP-2) is a regulatory protein composed of 194 amino acids with a molecular weight of around 21 kDa. It has dual functionality: reducing MMP activity and facilitating pro-MMP-2 activation. TIMP-2 is crucial for maintaining the structural and functional integrity of tissues, particularly in the kidneys, by regulating the extracellular matrix components.

Protein Swine Metalloproteinase Inhibitor 2 (TIMP2)
Protein Synonym CSC-21K; TIMP Metallopeptidase Inhibitor 2
Gene ID 396988
UniProt ID Q9WUC6

Shipping and Storage

This product is shipped with dry ice. It is recommended to aliquote as needed and store at -80°C upon receipt. Reconstituted protein solution can be stored at 4°C for 1 week, at < -80°C for 12 months.

Documents

COA

To request a Certificate of Analysis, please enter the Lot No. in the search box. Note: Certificate of Analysis not available for kits.

The product is for research use only.
Not for commercial, prophylactic, diagnostic, or therapeutic applications.

User Note

  1. Always centrifuge tubes before opening. Avoid mixing by vortexing or pipetting. Reconstitute in 10mM PBS (pH7.4) to a concentration of 0.1-1.0 mg/mL.Aliquote the reconstituted solution to minimise freeze-thaw cycles.

References

  1. Meléndez, J. et al. Cloning and expression of guinea pig TIMP-2. Expression in normal and hyperoxic lung injury. American journal of physiology. Lung cellular and molecular physiology. 2000, 278,4: L737-43.
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