MHC-HM413T-100μg / 询价
MHC-HM413T-500μg / 询价
MHC-HM413T-500μgx2 / 询价
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Chimeric HLA-A*02:01 (mα3) &B2M&LMP2 (CLGGLLTMV) Tetramer Protein
Recombinant Chimeric HLA-A*02:01(mα3)&B2M&LMP2 (CLGGLLTMV) Tetramer Protein is expressed from HEK293 with His tag and Avi tag at the C-Terminus, tetramer is assembled by biotinylated monomer and streptavidin. It contains Gly25-Thr206(Human HLA-A*02:01 α1&α2)&Asp207-Glu299(Mouse H-2Ld α3), Ile21-Met119(B2M) and CLGGLLTMV peptide.[Accession | A0A140T913(Human HLA-A*02:01 α1&α2)&P01897(Mouse H-2Ld α3)&P61769(B2M)&CLGGLLTMV]
The protein has a predicted MW of 258 kDa. Due to glycosylation, the protein migrates to 260-265 kDa under Non reducing (N) condition based on Tris-Bis PAGE result.
Less than 1EU per μg by the LAL method.
> 95% as determined by Tris-Bis PAGE
> 95% as determined by HPLC
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 3-6 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.
Chimeric HLA-A*02:01 (mα3) &B2M&LMP2 (CLGGLLTMV) Tetramer on Tris-Bis PAGE under Non reducing (N) condition. The purity is greater than 95%.
The purity of Chimeric HLA-A*02:01 (mα3) &B2M&LMP2 (CLGGLLTMV) Tetramer was greater than 95% as determined by SEC-HPLC.
Immobilized Chimeric HLA-A*02:01(mα3)&B2M&LMP2 (CLGGLLTMV) Tetramer, His Tag at 1μg/ml (100μl/well) on the plate. Dose response curve for Anti-HLA-A*02:01&B2M&LMP2 (CLGGLLTMV) Antibody, hFc Tag with the EC50 of 10.6ng/ml determined by ELISA.
The immunoproteasome, having been linked to neurodegenerative diseases and hematological cancers, has been shown to play an important role in MHC class I antigen presentation. The development of molecular probes that selectively inhibit the major catalytic subunit, LMP2, of the immunoproteasome,LMP2-rich cancer cells compared to LMP2-deficient cancer cells are more sensitive to growth inhibition by the LMP2-specific inhibitor, implicating an important role of LMP2 in regulating cell growth of malignant tumors that highly express LMP2.
MHC; RMF; LMP2; LMP-2; Macropain chain 7; Proteasome chain 7; PSMB9; RING12
(1) Ho YK, Bargagna-Mohan P, Wehenkel M, Mohan R, Kim KB. LMP2-specific inhibitors: chemical genetic tools for proteasome biology. Chem Biol. 2007 Apr;14(4):419-30. doi: 10.1016/j.chembiol.2007.03.008. PMID: 17462577; PMCID: PMC5541682.
