CLEC1B Human, Sf9

C-type lectin domain family 1, member B (CLEC1B), also known as CLEC-2, is a protein encoded by the CLEC1B gene in humans. This protein is a member of the C-type lectin superfamily, which is characterized by their calcium-dependent carbohydrate-binding properties . CLEC1B is a type II transmembrane receptor that plays a crucial role in various physiological processes, including platelet activation, immune response, and angiogenesis .

CLEC1B contains a C-type lectin-like domain (CTLD) that is essential for its carbohydrate-binding activity. The protein functions as a receptor for the lymphatic endothelial marker, podoplanin (PDPN), and is involved in platelet aggregation and activation . Upon ligand binding, CLEC1B signals through the activation of SRC and SYK tyrosine kinases, leading to downstream phosphorylation events and activation of PLCG2 .

CLEC1B is primarily expressed in myeloid cells and natural killer (NK) cells . Its expression is regulated by various factors, including cytokines and other signaling molecules. The protein is also implicated in the immune response to pathogens and plays a role in the modulation of inflammatory processes .

CLEC1B has been identified as a potential prognostic biomarker in hepatocellular carcinoma (HCC). Studies have shown that the expression of CLEC1B is downregulated in various tumors, and its low expression is associated with poor prognosis in HCC patients . Additionally, CLEC1B is involved in the regulation of immune cell infiltration in the tumor microenvironment, making it a potential target for immunotherapy .

Human recombinant CLEC1B can be produced using the Sf9 insect cell expression system. This system utilizes the baculovirus expression vector to produce high yields of recombinant proteins with post-translational modifications similar to those in mammalian cells. The recombinant CLEC1B produced in Sf9 cells retains its functional properties and can be used for various research and therapeutic applications.