Recombinant Human LILRB3 protein (His tag)
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Recombinant Human LILRB3 protein (His tag) is a Human Fragment protein, in the 1 to 443 aa range, expressed in HEK 293 cells, with >97%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE.
View Alternative Names
CD85a, ILT5, LIR3, LILRB3, Leukocyte immunoglobulin-like receptor subfamily B member 3, LIR-3, Leukocyte immunoglobulin-like receptor 3, CD85 antigen-like family member A, Immunoglobulin-like transcript 5, Monocyte inhibitory receptor HL9, ILT-5
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human LILRB3 protein (His tag) (AB276450)
SDS-PAGE analysis of ab276450
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The LILRB3 protein participates in downregulating immune cell activation and preventing overactivation that might lead to tissue damage. It belongs to the family of leukocyte immunoglobulin-like receptors. LILRB3 cooperates with other molecules on the cell surface to form a complex that modulates immune response via the transmission of inhibitory signals.
Pathways
The LILRB3 protein is involved in the immune checkpoint pathways that regulate immune cell activity and tolerance. It has important connections with the NF-κB pathway influencing the inflammatory response and maturation of dendritic cells. LILRB3's function relates to the PD-1 pathway which is another regulatory mechanism that ensures immune cells do not become overly active.
Specifications
Form
Lyophilized
General info
Function
May act as receptor for class I MHC antigens. Becomes activated upon coligation of LILRB3 and immune receptors, such as FCGR2B and the B-cell receptor. Down-regulates antigen-induced B-cell activation by recruiting phosphatases to its immunoreceptor tyrosine-based inhibitor motifs (ITIM).
Post-translational modifications
Phosphorylated on tyrosine residues by LYN. Phosphorylation at Tyr-595 and Tyr-625 is important for interaction with PTPN6/SHP-1 and PTPN11/SHP-2.
Target data
Product promise
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