Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
The protein encoded by DARC is a glycosylated membrane protein and a non-specific receptor for several chemokines. Additionally we are shipping DARC Antibodies (140) and DARC Proteins (8) and many more products for this protein.
Showing 1 out of 5 products:
DARC expression in cancer cells inhibits pancreatic ductal adenocarcinoma progression by suppressing STAT3 (show STAT3 ELISA Kits) activation through the inhibition of CXCR2 (show CXCR2 ELISA Kits) signaling
The data suggest that selective exposure of the Duffy binding protein (DBP (show GC ELISA Kits)) binding site within DARC is key to the preferential binding of DBP (show GC ELISA Kits) to immature reticulocytes, which is the potential mechanism underlying the preferential infection of a reticulocyte subset by P vivax.
population genetic analysis of DARC shows its association with malaria resistance
We showed that DARC expression is down-regulated in CRC (show CALR ELISA Kits) and associated with clinical pathological features and MVD (show MVD ELISA Kits) of CRC (show CALR ELISA Kits). DARC might be involved in tumorigenesis, progression, angiogenesis, and metastasis of CRC (show CALR ELISA Kits).
DARC is required for Staphylococcus aureus-mediated lysis of human erythrocytes, and DARC overexpression is sufficient to render cells susceptible to toxin-mediated lysis.
study demonstrates the association of SNP rs12075 from DARC gene with the levels of serum IL8 (show IL8 ELISA Kits)
DARC levels are elevated in human keloid fibroblasts and might inhibit the secretion of CCL2 (show CCL2 ELISA Kits).
Through molecular genotyping we also identified polymorphisms in RhCE, Kell, Duffy, Colton, Lutheran and Scianna loci in donors and patients.
Duffy blood group
Isothermal titration calorimetry studies show these structures are part of a multi-step binding pathway, and individual point mutations of residues contacting DARC result in a complete loss of RBC (show CACNA1C ELISA Kits) binding by DBP (show GC ELISA Kits)-RII.
DARC was exquisitely restricted to post-capillary and small collecting venules and completely absent from arteries, arterioles, capillaries, veins, and most lymphatics in every tissue analyzed. Intravital microscopy showed that adhesive leukocyte-endothelial interactions were restricted to DARC(+) venules. DARC was detectable over the entire circumference of V-ECs, but was more concentrated at cell-cell junctions.
DARC regulates recruitment of osteoclast precursors at the inflammation site
The DARC/CD234 is expressed on macrophages and stabilizes CD82 (show CD82 ELISA Kits) on long-term repopulating hematopoietic stem cells, promoting their quiescence.
Ackr1 deficiency appears to be protective in the ApoE (show APOE ELISA Kits) knockout model of atherogenesis, but it is associated with only modest changes in cytokine and chemokine (show CCL1 ELISA Kits) expression as well as T-cell subset frequency and inflammatory macrophage content.
Darc plays a role in modulating the regulation of inflammatory response to bone injury and that lack of Darc expression promotes cartilage formation in fracture calluses but does not affect bony union or fracture healing at 21 days post-fracture.
The data showed a role for erythrocyte DARC as a chemokine (show CCL1 ELISA Kits) reservoir and that endothelial DARC contributes to the pathogenesis of experimental autoimmune encephalomyelitis by shuttling chemokines across the blood-brain barrier.
DARC is crucial for chemokine (show CCL1 ELISA Kits)-mediated leukocyte recruitment in vivo.
Plasmodium yoelii uses the murine Duffy antigen receptor for chemokines as a receptor for normocyte invasion and an alternative receptor for reticulocyte invasion.
Vascular endothelial cells may induce Duffy protein to regulate leukocytes and/or chemokine (show CCL1 ELISA Kits) trafficking
role of the Duffy antigen and glycophorin A (show GYPA ELISA Kits) as receptors for rodent malaria parasite invasion of erythrocytes
the 5' flanking region of the DARC gene was isolated and characterized
The protein encoded by this gene is a glycosylated membrane protein and a non-specific receptor for several chemokines. The encoded protein is the receptor for the human malarial parasites Plasmodium vivax and Plasmodium knowlesi. Polymorphisms in this gene are the basis of the Duffy blood group system. Two transcript variants encoding different isoforms have been found for this gene.
Duffy blood group, chemokine receptor
, duffy antigen/chemokine receptor
, Duffy antigen/chemokine receptor
, Duffy blood group antigen
, Fy glycoprotein
, atypical chemokine receptor 1
, glycoprotein D
, plasmodium vivax receptor
, Duffy antigen receptor for chemokines
, blood group antigen
, duffy antigen/receptor for chemokine glycoprotein