LILRA2/CD85h/ILT1 Protein, Human (Biotinylated, HEK293, His-Avi)

The LILRA2/CD85h/ILT1 protein is critical in the innate immune response and recognizes N-terminally truncated immunoglobulins from a variety of pathogenic bacteria and fungi. It interacts with cleaved IgM, IgG3 and IgG4, triggering neutrophil and monocyte activation. LILRA2/CD85h/ILT1 Protein, Human (Biotinylated, HEK293, His-Avi) is the recombinant human-derived LILRA2/CD85h/ILT1 protein, expressed by HEK293 , with C-Avi, C-His labeled tag.

LILRA2/CD85h/ILT1 protein plays a crucial role in innate immune responses against microbial infection. It specifically recognizes a subset of N-terminally truncated immunoglobulins resulting from protease cleavage in various pathogenic bacteria and fungi, including L. pneumophila, M. hyorhinis, S. pneumoniae, S. aureus, and C. albicans. The protein binds to epitopes located partly in the variable region of immunoglobulin light chains, requiring the constant region for signaling. LILRA2 interacts with cleaved IgM, IgG3, and IgG4 but does not bind to cleaved IgA1. Activation through the binding of N-terminally truncated immunoglobulins triggers neutrophil activation, leading to the release of various cytokines and chemokines. In monocytes, this activation induces the release of CSF2, CF3, IL6, CXCL8, and CCL3, while down-regulating responses to bacterial lipopolysaccharide (LPS), potentially through the down-regulation of TLR4 expression. Additionally, in eosinophils, ligand binding results in the release of RNASE2, IL4, and leukotriene C4. Importantly, LILRA2 does not bind to class I MHC antigens and exists as a homodimer.

Human

HEK293

C-Avi;C-His

Q8N149-1 (G24-N449)

11027  [NCBI]

Extracellular Domain

Biotin

GHLPKPTLWAEPGSVIIQGSPVTLRCQGSLQAEEYHLYRENKSASWVRRIQEPGKNGQFPIPSITWEHAGRYHCQYYSHNHSSEYSDPLELVVTGAYSKPTLSALPSPVVTSGGNVTLQCVSQVAFDGFILCKEGEDEHPQRLNSHSHARGWSWAIFSVGPVSPSRRWSYRCYAYDSNSPYVWSLPSDLLELLVPGVSKKPSLSVQPGPMVAPGESLTLQCVSDVGYDRFVLYKEGERDFLQRPGWQPQAGLSQANFTLGPVSPSHGGQYRCYSAHNLSSEWSAPSDPLDILITGQFYDRPSLSVQPVPTVAPGKNVTLLCQSRGQFHTFLLTKEGAGHPPLHLRSEHQAQQNQAEFRMGPVTSAHVGTYRCYSSLSSNPYLLSLPSDPLELVVSEAAETLSPSQNKTDSTTTSLGQHPQDYTVEN

Approximately 67-100 kDa,based on SDS-PAGE under reducing conditions,due to the glycosylation.

≥ 90%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.