Recombinant Mouse LSECtin/CLEC4G Protein, CF

Recombinant Mouse LSECtin/CLEC4G Protein, CF Summary

Product Specifications

Product Datasheets

Carrier Free

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.

In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.

Background: LSECtin/CLEC4G

LSECtin (liver and lymph node sinusoidal endothelial cell C-type lectin), also known as C-type lectin superfamily 4 member G (CLEC4G), is a member of subgroup II of the C-type (Ca2+-dependent) lectin superfamily (1). The protein was named LSECtin because its initial expression was described to be restricted to liver and lymph node sinusoidal endothelial cells (1). However, LSECtin has also been detected in peripheral blood and thymic dendritic cells isolated ex vivo, and in monocyte-derived macrophages and dendritic cells at the RNA and protein level (2). Mouse LSECtin is a type II transmembrane glycoprotein that includes an N-terminal cytoplasmic tail (aa 1-30), a 21 aa transmembrane region, and a 243 aa extracellular domain (ECD). Within the ECD, mouse LSECtin shares 66% and 85% aa sequence identity with human and rat LSECtin, respectively. LSECtin binds to mannose, GlcNAc, and fucose in a Ca2+-dependent manner (1-3). In addition, LSECtin has the ability to bind to surface glycoproteins of enveloped viruses (3, 4). In particular, interaction of LSECtin with the surface glycoproteins of severe acute respiratory syndrome (SARS) coronavirus and Ebola virus has been described, and LSECtin-mediated infection of cells by Ebola virus has been demonstrated (3, 4). LSECtin is highly expressed on tumor-associated macrophages (TAMs) and enhances stemness of breast cancer cells (BCCs) (9). We identified BTN3A3, a B7 family member with previously unknown functions as the receptor for LSECtin on BCCs responsible for stemness-promoting effect of LSECtin (9). In mice bearing human tumor xenografts, either macrophage-specific ablation of LSECtin or silencing of BTN3A3 in BCCs decreased CSC frequency and tumor growth (9). Administration of LSECtin-positive macrophages increased the tumorigenic activity of BCCs dependent on BTN3A3 (9). Disruption of the LSECtin-BTN3A3 axis with BTN3A3-Fc or anti-BTN3A3 mAb has a therapeutic effect on breast cancer (9). These findings define a juxtacrine signaling mechanism by which TAMs promote cancer stemness (9). Targeting this axis in the CSC niche may provide potential therapies to breast cancer (9).

Related Research Areas

• C-type Lectin Family
• Search Immune Checkpoint Targets