PROVETOP

Biotinylated Human HLA-A*11:01&B2M&LMP2 (SSCSSCPLTK) Monomer Protein

Catalog No: LMP2-HB001

Species
Human
Expression System
HEK293
Tag
with His, Avi

Product overview

Recombinant Biotinylated Human LMP2(HLA-A*11:01) Protein is expressed from HEK293 with with His tag and Avi tag at the C-terminus. 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 50.4 kDa. Due to glycosylation, the protein migrates to 51-60 kDa 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

Bis-Tris PAGE
LMP2-HB001 Bis-Tris-PAGE-white result

Biotinylated Human HLA-A*11:01&B2M&LMP2 (SSCSSCPLTK) Monomer on Bis-Tris PAGE under reduced condition. The purity is greater than 95%.

SEC-HPLC
LMP2-HB001 SEC-HPLC result

The purity of Biotinylated Human HLA-A*11:01&B2M&LMP2 (SSCSSCPLTK) Monomer 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. (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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