PROVETOP

Biotinylated Human LILRA1/CD85i/LIR-6 Protein

Catalog No: LILRA1-HB001

Species
Human
Expression System
HEK293
Tag
His, Avi

Product overview

Recombinant Biotinylated Human LILRA1/CD85i/LIR-6 Protein is expressed in HEK293 cells with a His tag and Avi tag at the C-terminus. It contains amino acid residues Pro17-Asn461 (UniProt accession: O75019-1).

Product Details

Molecular Aliases
CD85i; LILRA1; LIR6; LIR-6; LIR6MGC126563
Protein Length
Pro17-Asn461
Expression System
HEK293
Theoretical Molecular Weight
The protein has a predicted MW of 51.4 kDa. Due to glycosylation, the protein migrates to 70-80 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
LILRA1-HB001 Bis-Tris-PAGE-white result

Biotinylated Human LILRA1 on Bis-Tris PAGE under reduced condition. The purity is greater than 95%.

SEC-HPLC
LILRA1-HB001 SEC-HPLC result

The purity of Biotinylated Human LILRA1 is greater than 95% as determined by SEC-HPLC.

Background

LILRA1, also known as CD85i and LIR-6, is an approximately 70 kDa variably glycosylated transmembrane protein that regulates immune cell activation. Mature human LILRA1 consists of a 445 amino acid (aa) extracellular domain (ECD) with 4 Ig-like domains, a 21 aa transmembrane segment, and a 7 aa cytoplasmic tail. LILRA1 may act as receptor for class I MHC antigens.

References

  1. The MHC class I‐LILRB1 signalling axis as a promising target in cancer therapy[J]. Scandinavian Journal of Immunology, 2019.

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