Clone REA957 recognizes the mouse CD180 antigen, also known as RP105, a type I transmembrane protein structurally similar to toll-like receptors (TLRs) with the conserved features of TLRs, including a leucine-rich repeat extracellular domain and regions containing conserved cysteines. However, in contrast to TLRs, CD180 lacks a typical TIR domain, containing only 6–11 intracytoplasmic amino acids. Antibody mediated ligation of CD180 was shown to induce B cell proliferation and protection from subsequent radiation- or dexamethasone-induced apoptosis. Expression of CD180 is found on mature B cells, monocytes, macrophages, and dendritic cells. CD180 activity is dependent on physical association with a molecule called MD-1. In B cells, CD180, together with TLR4, has been shown to induce B cell proliferation in response to LPS. However, in primary myeloid cells and
in vivo
, CD180 acts as an inhibitor of TLR4 signaling.
Additional information: Clone REA957 displays negligible binding to Fc receptors.
Alternative Names
Ly78, RP105
Alternative Names
Ly78, RP105
Clone REA957 recognizes the mouse CD180 antigen, also known as RP105, a type I transmembrane protein structurally similar to toll-like receptors (TLRs) with the conserved features of TLRs, including a leucine-rich repeat extracellular domain and regions containing conserved cysteines. However, in contrast to TLRs, CD180 lacks a typical TIR domain, containing only 6–11 intracytoplasmic amino acids. Antibody mediated ligation of CD180 was shown to induce B cell proliferation and protection from subsequent radiation- or dexamethasone-induced apoptosis. Expression of CD180 is found on mature B cells, monocytes, macrophages, and dendritic cells. CD180 activity is dependent on physical association with a molecule called MD-1. In B cells, CD180, together with TLR4, has been shown to induce B cell proliferation in response to LPS. However, in primary myeloid cells and
in vivo
, CD180 acts as an inhibitor of TLR4 signaling.
Additional information: Clone REA957 displays negligible binding to Fc receptors.
原厂资料:
Clone REA957 recognizes the mouse CD180 antigen, also known as RP105, a type I transmembrane protein structurally similar to toll-like receptors (TLRs) with the conserved features of TLRs, including a leucine-rich repeat extracellular domain and regions containing conserved cysteines. However, in contrast to TLRs, CD180 lacks a typical TIR domain, containing only 6–11 intracytoplasmic amino acids. Antibody mediated ligation of CD180 was shown to induce B cell proliferation and protection from subsequent radiation- or dexamethasone-induced apoptosis. Expression of CD180 is found on mature B cells, monocytes, macrophages, and dendritic cells. CD180 activity is dependent on physical association with a molecule called MD-1. In B cells, CD180, together with TLR4, has been shown to induce B cell proliferation in response to LPS. However, in primary myeloid cells and
in vivo
, CD180 acts as an inhibitor of TLR4 signaling.
Additional information: Clone REA957 displays negligible binding to Fc receptors.
Alternative Names
Ly78, RP105
Clone REA957 recognizes the mouse CD180 antigen, also known as RP105, a type I transmembrane protein structurally similar to toll-like receptors (TLRs) with the conserved features of TLRs, including a leucine-rich repeat extracellular domain and regions containing conserved cysteines. However, in contrast to TLRs, CD180 lacks a typical TIR domain, containing only 6–11 intracytoplasmic amino acids. Antibody mediated ligation of CD180 was shown to induce B cell proliferation and protection from subsequent radiation- or dexamethasone-induced apoptosis. Expression of CD180 is found on mature B cells, monocytes, macrophages, and dendritic cells. CD180 activity is dependent on physical association with a molecule called MD-1. In B cells, CD180, together with TLR4, has been shown to induce B cell proliferation in response to LPS. However, in primary myeloid cells and
in vivo
, CD180 acts as an inhibitor of TLR4 signaling.
Additional information: Clone REA957 displays negligible binding to Fc receptors.