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CD180 is a cell surface molecule consisting of extracellular leucine-rich repeats (LRR) and a short cytoplasmic tail. Additionally we are shipping CD180 Antibodies (118) and CD180 Kits (2) and many more products for this protein.
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Human CD180 Protein expressed in Human Cells - ABIN2004245
Imayoshi, Yamamoto, Watanabe, Nishimura, Tashiro, Zaitsu, Tasaki, Kimoto, Hamasaki, Ishii: Expression of CD180, a toll-like receptor homologue, is up-regulated in children with Kawasaki disease. in Journal of molecular medicine (Berlin, Germany) 2006
Show all 2 references for ABIN2004245
Mouse (Murine) CD180 Protein expressed in Human Cells - ABIN2007885
Antosz, Sajewicz, Marzec-Kotarska, Kocki, Dmoszy?ska: Different expression of CD180, CD284 and CD14 receptors on the CD19+ subpopulation of normal and B-CLL lymphocytes. in Folia histochemica et cytobiologica / Polish Academy of Sciences, Polish Histochemical and Cytochemical Society 2010
Show all 2 references for ABIN2007885
The findings of association in different populations with different SNPs support a conclusion that variation close to the ANKRA2 (show ANKRA2 Proteins)/CD180 locus analysed in this study contributes to differential response to pathogen exposure.
The role of TLR2, TLR4 (show TLR4 Proteins) and RP105/MD1 (show LY86 Proteins) in the immunoregulatory effect of acidic exopolysaccharides from Lactobacillus plantarum N14 (show CLPTM1 Proteins), is reported.
These data unveil a novel innate immune signaling axis that orchestrates key cytokine responses of macrophages and provide molecular insight into the functions of RP105 (show GPR83 Proteins) as an innate immune receptor for mycobacteria.
RP105 (show GPR83 Proteins) regulates monocyte-driven arteriogenesis in a murine hind limb ischemia model.
RP105 deficiency results in reduced early atherosclerotic plaque development with a marked decrease in lesional macrophage content, which may be due to disturbed migration of RP105 deficient monocytes resulting from CCR2 downregulation
Deficiency of the endogenous TLR4 (show TLR4 Proteins) inhibitor, RP105 (show GPR83 Proteins), leads to pronounced cardiac dilation after myocardial infarction.
Data indicate that RP105 (show GPR83 Proteins) and TLR4 (show TLR4 Proteins) are both expressed by vascular smooth muscle cells (VSMC).
RP105 (show GPR83 Proteins) deficiency on circulating cells results in an intriguing unexpected TLR-associated mechanisms that decrease atherosclerotic lesion formation with alterations on proinflammatory B2 B cells.
The function of TLR2 and TLR4 (show TLR4 Proteins) in response to TLR ligands could be associated with each other by RP105 (show GPR83 Proteins).
Data show that both RP105 (show GPR83 Proteins)/MD-1 (show LY86 Proteins) and TLR4 (show TLR4 Proteins)/MD-2 (show LY96 Proteins) are expressed in marginal zone (MZ) B cells.
The RP105 (show GPR83 Proteins)/MD-1 (show LY86 Proteins) complex is a major mediator of adipose tissue inflammation independent of TLR4 (show TLR4 Proteins) signaling and may represent a novel therapeutic target for obesity-associated metabolic disorders.
Modulation of B cell proliferation by RP105 (show GPR83 Proteins) is not a function of B cell-intrinsic expression of RP105 (show GPR83 Proteins).
By associating with PIM (show PIM1 Proteins)-1L, CD180 can thus obtain autonomous signaling capabilities, and this complex is then channeling inflammatory signals into B cell survival programs
Since MEC1 cells are derived from a CLL patient with mutated IGVH genes (M-CLL) negative correlation between CD180 and CD32 expression on cycling MEC1 cells could be limited to M-CLL.
we address of monocytes functional status through assessment of the patterns of expression of Fcgamma receptors CD64 (show FCGR1A Proteins), CD32 (show FCGR2B Proteins), CD16 (show CD16 Proteins) and CD180 receptor on monocytes from CLL patients and healthy individuals using specific mAbs and flow cytometry.
Data indicate that TLR9 (show TLR9 Proteins)-signaling as a crucial factor for turning retinoic acid (RA) into a strong stimulator of RP105-mediated B-cell proliferation.
IL-4 (show IL4 Proteins) failed to up-regulate expression of RP105 at the cell surface. In conclusion, the anti-inflammatory actions of IL-4 (show IL4 Proteins) occur independently of IL-10 (show IL10 Proteins), RP105, and the kinase activity of RIPK2 (show RIPK2 Proteins)
Both mouse and human RP105/MD-1 (show LY86 Proteins) exhibit dimerization of the 1:1 RP105/MD-1 (show LY86 Proteins) complex, demonstrating a novel organization.
Lower mRNA expression of LY64 was detected in gingival tissue of chronic periodontitis patients compared to healthy controls.
Data show that CD180, CD284 (show TLR4 Proteins) and CD14 (show NDUFA2 Proteins) expression is higher on normal B cells than on CD19 (show CD19 Proteins)+ B-cell chronic lymphocytic leukaemia cells.
RP105 cross-linkaage enhanced B-lymphocyte (show AKAP17A Proteins) proliferation, TLR9 (show TLR9 Proteins) expression, and growth.
RP105 regulated TLR4 (show TLR4 Proteins) signaling in dendritic cells
CD180 is a cell surface molecule consisting of extracellular leucine-rich repeats (LRR) and a short cytoplasmic tail. The extracellular LRR is associated with a molecule called MD-1 and form the cell surface receptor complex, RP105/MD-1. It belongs to the family of pathogen receptors, Toll-like receptors (TLR). RP105/MD1, by working in concert with TLR4, controls B cell recognition and signaling of lipopolysaccharide (LPS), a membrane constituent of Gram-negative bacteria.
, lymphocyte antigen 78
, CD180 molecule
, radio protective 105
, lymphocyte antigen 64-like protein
, radioprotective 105 kDa protein
, lymphocyte antigen 64
, lymphocyte antigen-64, radioprotective, 105kDa