Name : Mouse AFP Protein

Product Source :
Recombinant Mouse AFP Protein is expressed from HEK293 with His tag at the C-Terminus. It contains Lys19-Val605.[Accession | P02772]

Molecular Weight :
The protein has a predicted MW of 66.40 kDa. Due to glycosylation, the protein migrates to 68-72 kDa based on Tris-Bis PAGE result.

Endotoxin Level :
Less than 1EU per μg by the LAL method.

Purity :
> 95% as determined by Tris-Bis PAGE> 95% as determined by HPLC

Formulation :
Lyophilized from 0.22μm filtered solution in PBS (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization.

Reconstitution :
Centrifuge the tube before opening. Reconstituting to a concentration more than 100 μg/ml is recommended. Dissolve the lyophilized protein in distilled water.

Storage and Stability :
-20 to -80°C for 12 months as supplied from date of receipt.-80°C for 3-6 months after reconstitution.2-8°C for 2-7 days after reconstitution.Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.

Product Concentration :
Tris-Bis PAGE Mouse AFP on Tris-Bis PAGE under reduced condition. The purity is greater than 95%. SEC-HPLC The purity of Mouse AFP is greater than 95% as determined by SEC-HPLC.

Background :
Alpha-fetoprotein is a shuttle protein that delivers nutrients through receptor-mediated endocytosis to embryotic cells. In adults, alpha-fetoprotein can shuttle drugs into alpha-fetoprotein receptor-positive myeloid-derived suppressor, regenerating and also cancer cells. Drugs with high-binding affinity to alpha-fetoprotein can activate or deplete targeted cells. Myeloid-derived suppressor cells activation leads to immune suppression that can be used for treating autoimmune diseases.

Synonyms :
Alpha-fetoprotein; Alpha-1-fetoprotein; Alpha-feto; AFP; HPAFP; AFPD; FETA

References & Citations :
(1) Pak VN. The use of alpha-fetoprotein for the treatment of autoimmune diseases and cancer. Ther Deliv. 2018 Jan;9(1):37-46. doi: 10.4155/tde-2017-0073. PMID: 29216804.

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