Recombinant Human LILRA3 protein
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Recombinant Human LILRA3 protein is a Human Full Length protein, in the 19 to 439 aa range, expressed in HEK 293 cells, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE, HPLC.
View Alternative Names
CD85e, ILT6, LIR4, LILRA3, Leukocyte immunoglobulin-like receptor subfamily A member 3, CD85 antigen-like family member E, Immunoglobulin-like transcript 6, Leukocyte immunoglobulin-like receptor 4, Monocyte inhibitory receptor HM43/HM31, ILT-6, LIR-4
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
LILRA3 modulates immune responses by binding to unknown ligands. It does not associate with any known receptor complex because it does not possess a transmembrane or cytoplasmic domain. LILRA3 may act as a natural antagonist to other LILR receptors by interfering with their ligand interactions. This antagonism helps regulate the functions of the innate and adaptive immune responses by competing with membrane-bound LILR forms for binding with common ligands.
Pathways
LILRA3 influences the pathways involved in immune regulation including the modulation of cytokine production. It has been linked to pathways associated with the inhibition of inflammation intersecting with receptors like LILRA2 and LILRB1 which are also part of the LILR family. These interactions are essential in balancing immune responses possibly by inhibiting excessive activation that could lead to inflammation or autoimmunity.
Specifications
Form
Lyophilized
Additional notes
Purity is greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE.
General info
Function
Acts as a soluble receptor for class I MHC antigens. Binds both classical and non-classical HLA class I molecules but with reduced affinities compared to LILRB1 or LILRB2. Binds with high affinity to the surface of monocytes, leading to abolish LPS-induced TNF-alpha production by monocytes.
Post-translational modifications
N-glycosylation is required for ligand binding.
Target data
Product promise
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