CLEC5A Human
Description
CLEC5A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
C-type lectin domain family 5-member A isoform 1 (CLEC5A), belonging to the CTL/CTLD superfamily, participates in various cellular processes such as cell-cell signaling, cell adhesion, and glycoprotein turnover. Additionally, it plays a crucial role in inflammation and immune responses. This protein acts as an attachment receptor for all four serotypes of Dengue virus and Japanese encephalitis virus. Upon binding to the dengue virus, CLEC5A initiates intracellular signaling by phosphorylating TYROBP, preventing viral entry but triggering the release of proinflammatory cytokines. Furthermore, CLEC5A acts as a positive regulator of osteoclastogenesis and a key player in synovial injury and bone erosion during autoimmune joint inflammation.
Product Science Overview
C-Type Lectin Domain Family 5, Member A (CLEC5A), also known as Myeloid DAP12-Associating Lectin-1 (MDL-1), is a protein encoded by the CLEC5A gene in humans. This protein is part of the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily, which is characterized by a common protein fold and diverse functions, including cell adhesion, cell-cell signaling, glycoprotein turnover, and roles in inflammation and immune response .
CLEC5A is a type II transmembrane protein with a short cytoplasmic tail and no intrinsic signaling motifs. It requires association with the adaptor protein DAP12 to generate signals via the Syk pathway . CLEC5A is highly expressed on myeloid lineages such as neutrophils, monocytes, macrophages, osteoclasts, microglia, and dendritic cells .
CLEC5A functions as a positive regulator of osteoclastogenesis and plays a crucial role in regulating inflammatory responses . It acts as a cell surface receptor that signals via TYROBP (DAP12) and is involved in the innate immune system and DAP12 interactions . The activation of CLEC5A induces the production of various cytokines (e.g., TNF-α, IL-1, IL-6, IL-8, and IL-17A) and chemokines (e.g., MIP-1α, RANTES, IP-10, MDC), amplifying the innate immune response .
One of the most well-known ligands for CLEC5A is the dengue virus. The binding of dengue virus to CLEC5A triggers signaling through the phosphorylation of DAP12, leading to the release of pro-inflammatory cytokines . This interaction does not result in viral entry but stimulates a strong inflammatory response, which is responsible for severe dengue virus-induced conditions such as dengue hemorrhagic fever (DHF) and dengue shock syndrome (DSS) .
Recombinant CLEC5A is produced using recombinant DNA technology, which involves inserting the CLEC5A gene into an expression system to produce the protein in vitro. This recombinant form is used in various research applications to study its structure, function, and role in diseases. It is also utilized in the development of therapeutic interventions targeting CLEC5A-mediated pathways.
Given its role in inflammatory responses and viral infections, CLEC5A is a potential therapeutic target for conditions such as osteoporosis, rheumatoid arthritis, and dengue virus infections. Inhibitors or modulators of CLEC5A signaling pathways could provide new avenues for treating these diseases.
