Name : Cynomolgus MICA Protein

Product Source :
Recombinant Cynomolgus MICA Protein is expressed from HEK293 with His tag at the C-Terminus. It contains Glu1-Trp284.[Accession | AAO24115.1]

Molecular Weight :
The protein has a predicted MW of 33.53 kDa. Due to glycosylation, the protein migrates to 48-58 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 Cynomolgus MICA on Tris-Bis PAGE under reduced condition. The purity is greater than 95%. SEC-HPLC The purity of Cynomolgus MICA is greater than 95% as determined by SEC-HPLC. ELISA Data Immobilized Cynomolgus MICA, His Tag at 1μg/ml (100μl/well) on the plate. Dose response curve for Human NKG2D, hFc Tag with the EC50 of 0.14μg/ml determined by ELISA.

Background :
MICA (MHC class I chain-related gene A) is a transmembrane glycoprotein that functions as a ligand for human NKG2D. A closely related protein, MICB, shares 85% amino acid identity with MICA. These proteins are distantly related to the MHC class I proteins. They possess three extracellular Ig‑like domains, but they have no capacity to bind peptide or interact with beta 2-microglobulin..

Synonyms :
Mafa-MIC1; MICA

References & Citations :
(1)Friese M A , Platten M , Lutz S Z , et al. MICA/NKG2D-mediated immunogene therapy of experimental gliomas.[J]. Cancer Research, 2003, 63(24):8996-9006.

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