Human HLA-A*11:01&B2M&LMP2 (SSCSSCPLTK) Tetramer Protein
Catalog No: LMP2-HP005
- Species
- Human
- Expression System
- HEK293
- Tag
- His, Avi
Product overview
Recombinant Human LMP2(HLA-A*11:01) 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-Thr305(HLA-A*11:01), Ile21-Met119(B2M) and SSCSSCPLTK peptide (accession: AAV53343.1(HLA-A*11:01) & P61769(B2M) &SSCSSCPLTK).
Product Details
- Molecular Aliases
- MHC; RMF; LMP2; LMP-2; Macropain chain 7; Proteasome chain 7; PSMB9; RING12
- Protein Length
- Gly25-Thr305
- Expression System
- HEK293
- Theoretical Molecular Weight
- The protein has a predicted MW of 258 kDa. Due to glycosylation, the protein migrates to 260-265 kDa under Non reduced (N) condition based on Bis-Tris PAGE result.
- Purity
- > 95% as determined by Bis-Tris PAGE > 95% as determined by HPLC
- Endotoxin
- Less than 1 EU per μg by the LAL method.
- Buffer / Formulation
- Lyophilized from 0.22μm filtered solution in PBS (pH 7.4). Normally 8% trehalose is added as protectant before lyophilization.
- State
- Lyophilized
- Storage Conditions
- -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.
- Reconstitution Advice
- Dissolve the lyophilized protein in distilled water. Please refer to the Certificate of Analysis for detailed instructions.
Data Display
Human HLA-A*11:01&B2M&LMP2 (SSCSSCPLTK) Tetramer on Bis-Tris PAGE under Non reduced (N) condition. The purity is greater than 95%.
The purity of Human HLA-A*11:01&B2M&LMP2 (SSCSSCPLTK) Tetramer is greater than 95% as determined by SEC-HPLC.
Background
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.
References
- (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.
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