Recombinant Mouse LILRB3 protein (His tag)
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(1 Publication)
Recombinant Mouse LILRB3 protein (His tag) is a Mouse Fragment protein, in the 1 to 640 aa range, expressed in HEK 293 cells, with >95%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE.
View Alternative Names
Lilrb3, Paired immunoglobulin-like receptor B, PIR-B, Cell-surface glycoprotein p91, Leukocyte immunoglobulin-like receptor subfamily B member 3, LIR-3, Leukocyte immunoglobulin-like receptor 3
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Mouse LILRB3 protein (His tag) (AB276923)
SDS-PAGE analysis of ab276923
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 PIRB 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-794 and Tyr-824 by LYN is important for interaction with PTPN6/SHP-1 and PTPN11/SHP-2.
Target data
Publications (1)
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Nature communications 14:2615 PubMed37147336
2023
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
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