Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
COLEC12 encodes a member of the C-lectin family, proteins that possess collagen-like sequences and carbohydrate recognition domains. Additionally we are shipping COLEC12 Proteins (10) and COLEC12 Kits (3) and many more products for this protein.
Showing 10 out of 52 products:
Human Polyclonal COLEC12 Primary Antibody for WB - ABIN2779674
Yoshida, Tsuruta, Iwasaki, Yamane, Ochi, Suzuki: SRCL/CL-P1 recognizes GalNAc and a carcinoma-associated antigen, Tn antigen. in Journal of biochemistry 2003
Chicken Polyclonal COLEC12 Primary Antibody for WB - ABIN2784129
Coombs, Graham, Drickamer, Taylor: Selective binding of the scavenger receptor C-type lectin to Lewisx trisaccharide and related glycan ligands. in The Journal of biological chemistry 2005
rs17684886 (ZNRF1 (show ZNRF1 Antibodies)) and rs599019 (COLEC12) are associated with diabetic retinopathy and rs6427247 (SCYL1BP1 (show GORAB Antibodies)) and rs899036 (API5 (show API5 Antibodies)) are associated with severe diabetic retinopathy in Chinese patients with type 2 diabetes
The common presence of Lewis(x (show FUT4 Antibodies)) groups in granule protein glycans can thus target granule proteins for clearance by SRCL.
The Le(x) residues of both, CEACAM1 (show CEACAM1 Antibodies) and CEA (show CEACAM5 Antibodies), interact with the human Le(x)-binding glycan receptors DC-SIGN (show CD209 Antibodies) and SRCL.
haplotype structure of the CL-P1 gene obtained from six single-nucleotide polymorphisms that were genotyped with 108 alleles in Japanese subjects
SRCL is expressed in some but not all nurse-like cells; its C-type lectin (show MBL2 Antibodies) domain binds specifically to several carbohydrates including GalNAc, T and Tn antigen in a Ca2 (show CA2 Antibodies)+-dependent manner.
SRCL might be involved in selective clearance of specific desialylated glycoproteins from circulation and/or interaction of cells bearing Lewis(x (show FUT4 Antibodies))-type structures with the vascular endothelium
CL-P1 is not a common membrane protein on endothelial cells found in normal tissues under steady state conditions.
CL-P1 predominantly mediated phagocytosis for fungi in vascular endothelia.
Structural analysis of carbohydrate-recognition domain of SRCL in complex with Lewis(x (show FUT4 Antibodies)) and mutagenesis show the basis for this specificity, which is analogous to how selectins and DC-SIGN (show CD209 Antibodies) bind to related fucosylated glycans [scavenger receptor C]
This gene encodes a member of the C-lectin family, proteins that possess collagen-like sequences and carbohydrate recognition domains. This protein is a scavenger receptor, a cell surface glycoprotein that displays several functions associated with host defense. It can bind to carbohydrate antigens on microorganisms, facilitating their recognition and removal. It also mediates the recognition, internalization, and degradation of oxidatively modified low density lipoprotein by vascular endothelial cells.
collectin sub-family member 12
, collectin placenta protein 1
, nurse cell scavenger receptor 2
, scavenger receptor class A, member 4
, scavenger receptor with C-type lectin
, collectin 1 precursor CL-3