The gene CLEC4G (C-type lectin domain family 4 member G) gene forms a lectin gene cluster at human chromosome 19p13.3 along with DC-SIGN, and L-SIGN and CD23. CLEC4G is expressed on sinusoidal endothelial cells in liver and lymph nodes along with DC-SIGNR. The C-type lectins contain a C-terminal carbohydrate recognition domain (CRD) that functions as an attachment factor. This domain links high mannose oligosaccharides or N-linked glycosylated protein. The neck region of CRD contains repeat units called the VNTR (variable number tandem repeat).
Synonyms: Anti-C-type lectin domain family 4 member G
Storage: -20C
Application: All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project (www.proteinatlas.org)and as a result, are supported by the most extensive characterization in the industry. The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Biochem Physiol Actions: The C-type lectin encoded by the gene CLEC4G (C-type lectin domain family 4 member G) plays an important role in the activation of B-cells. It interacts with and mediates viral and bacterial pathogen recognitions. The human CLEC4G protein was previously referred to as LSECtin. It is capable of interacting with BACE1 (ß-Site amyloid precursor protein cleaving enzyme-1 ) molecule and negatively regulate it. BACE1 cleaves amyloid precursor protein (APP) to form toxic amyloid-ß (Aß) peptides and has been implicated in Alzheimer's disease (AD).
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