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Recombinant Mouse Fetuin-A/AHSG protein (rFc Tag)

Species

Mouse

Purity

>90 %, SDS-PAGE

Tag

rFc Tag

Activity

not tested

Cat no : Eg3151

Validation Data Gallery

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

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

Product Information

Purity >90 %, SDS-PAGE
Endotoxin <0.1 EU/μg protein, LAL method
Activity 
Not tested
Expression HEK293-derived Mouse Fetuin-A protein Ala19-Ile345 (Accession# P29699) with a rabbit IgG Fc tag at the C-terminus.
GeneID 11625
Accession P29699
PredictedSize 61.3 kDa
SDS-PAGE 62-85 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

Fetuin-A, also called Alpha 2-Heremans Schmid Glycoprotein (AHSG), is a multifunctional plasma agent with a molecular weight of approximately 60 kDa and half-life of several days. Fetuin-A is mainly synthesized by the liver. Fetuin-A plays a role as a physiological inhibitor of insulin receptor tyrosine kinase associated with insulin resistance and a negative acute phase reactant. It also regulates bone remodeling and calcium metabolism being an important inhibitor of calcium salt precipitation and vascular calcifications.

References:

1.Goustin AS, et al. (2011). Cell Signal. 23(6):980-990.
2.Dabrowska AM, et al. (2015). Biomed Pap Med Fac Univ Palacky Olomouc Czech Repub. 159(3):352-359.
3.Ochieng J, et al. (2018). Int J Mol Sci. 19(8):2211.