MIC-HM20B-100μg / 询价
MIC-HM20B-500μg / 询价
MIC-HM20B-500μgx2 / 询价
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Human MICB Protein
Recombinant Human MICB Protein is expressed from HEK293 with hFc tag at the C-Terminus.It contains Ala23-Gly298 [Accession | Q29980-1].
The protein has a predicted MW of 58.21 kDa. Due to glycosylation, the protein migrates to 70-80 kDa based on Bis-Tris PAGE result.
> 95% as determined by Bis-Tris PAGE
> 95% as determined by HPLC
Less than 1EU per μg by the LAL method.
Lyophilized from 0.22μm filtered solution in PBS (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization.
Centrifuge the tube before opening. Reconstituting to a concentration more than 100 μg/ml is recommended. Dissolve the lyophilized protein in distilled water.
-20 to -80°C for 12 months as supplied from date of receipt.
-80°C for 3 months after reconstitution.
Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Human MICB on Bis-Tris PAGE under reduced condition. The purity is greater than 95%.
The purity of Human MICB is greater than 95% as determined by SEC-HPLC.
Human MICB, hFc Tag captured on CM5 Chip via Protein A can bind Human NKG2D, His Tag with an affinity constant of 95.15 nM as determined in SPR assay (Biacore T200).
Immobilized Human MICB, hFc Tag at 2μg/ml (100μl/Well) on the plate. Dose response curve for Biotinylated Anti-MICB Antibody, hFc Tag with the EC50 of 26.6ng/ml determined by ELISA (QC Test).
MICB (MHC class I chain-related gene B) is a transmembrane glycoprotein that functions as a ligand for NKG2D. A closely related protein, MICA, shares 85% amino acid identity with MICB.MICB Seems to have no role in antigen presentation. Acts as a stress-induced self-antigen that is recognized by gamma delta T cells. Ligand for the KLRK1/NKG2D receptor. Binding to KLRK1 leads to cell lysis.
MICB; MIC-B; PERB11.2
(1)Spear P , Wu M R , Sentman M L , et al. NKG2D ligands as therapeutic targets[J]. Cancer immunity: a journal of the Academy of Cancer Immunology, 2013, 13(2):8.
