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Recombinant Mouse TIMP2 protein (rFc Tag)(HPLC verified)

Species

Mouse

Purity

>90 %, SDS-PAGE
>90 %, SEC-HPLC

Tag

rFc Tag

Activity

not tested

Cat no : Eg2960

Validation Data Gallery

  • Purity of Recombinant Mouse TIMP2 was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) conditions and stained using Coomassie blue.

    Purity of Recombinant Mouse TIMP2 was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) conditions and stained using Coomassie blue.

  • The purity of Mouse TIMP2 was greater than 90% as determined by SEC-HPLC.

    The purity of Mouse TIMP2 was greater than 90% as determined by SEC-HPLC.

Product Information

Purity >90 %, SDS-PAGE
>90 %, SEC-HPLC
Endotoxin <0.1 EU/μg protein, LAL method
Activity 
Not tested
Expression HEK293-derived Mouse TIMP2 protein Cys27-Pro220 (Accession# P25785) with a rabbit IgG Fc tag at the C-terminus.
GeneID 21858
Accession P25785
PredictedSize 47.8 kDa
SDS-PAGE 44-50 kDa, reducing (R) conditions
Formulation Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
Reconstitution Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
Storage Conditions
It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

Background

Metalloproteinases-2 (TIMP2) is a secreted protein ~21 kDa in size, primarily known for its role in regulating peripheral extracellular matrix (ECM) remodeling through its unique dual roles in regulating activation of latent matrix metalloproteinases (MMPs), including MMP2, to proteolytically active forms, and the inhibition of MMP activity.

References:

1. Brew K. et al. (2010) Biochim Biophys Acta. 1803:55–71.
2. Caterina JJ. et al. (2000) J Biol Chem. 275:26416–22.
3. Wang Z. et al. (2000) J Biol Chem. 275:26411–5.