CLEC5A Human, Sf9
Sf9, Baculovirus cells.
Greater than 90.0% as determined by SDS-PAGE.
Description
CLEC5A produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain (28-188 a.a.) and fused to a 9 aa His Tag at C-terminus containing a total of 170 amino acids and having a molecular mass of 19.5kDa.
CLEC5A shows multiple bands between 28-40kDa on SDS-PAGE, reducing conditions and purified by proprietary chromatographic techniques.
Product Specs
C-type lectin domain family 5-member A isoform 1 (CLEC5A), a member of the CTL/CTLD superfamily, plays diverse roles including cell-cell signaling, cell adhesion, and glycoprotein turnover. Additionally, it exhibits significant roles in inflammation and immune responses. This protein serves as a cell attachment receptor for all four serotypes of the Dengue virus and the Japanese encephalitis virus. Upon binding to the dengue virus, CLEC5A initiates signaling pathways by phosphorylating TYROBP. This interaction, while preventing viral entry, triggers the release of proinflammatory cytokines. Furthermore, CLEC5A acts as a positive regulator of osteoclastogenesis and plays a crucial role in regulating synovial injury and bone erosion during autoimmune joint inflammation.
Produced in Sf9 Baculovirus cells, CLEC5A is expressed as a single, glycosylated polypeptide chain. This protein consists of amino acids 28-188 of the CLEC5A sequence, fused to a C-terminal 9 amino acid His Tag. With a total of 170 amino acids, it has a molecular mass of 19.5kDa. On SDS-PAGE under reducing conditions, CLEC5A appears as multiple bands between 28-40kDa. It is purified using proprietary chromatographic techniques.
The CLEC5A protein solution is provided at a concentration of 0.25mg/ml and contains 20% glycerol, 1mM DTT, and Phosphate buffered saline (pH7.4).
The purity of CLEC5A is determined to be greater than 90.0% based on SDS-PAGE analysis.
Sf9, Baculovirus cells.
ADLPQIFNKS NDGFTTTRSY GTVSQIFGSS SPSPNGFITT RSYGTVCPKD WEFYQARCFF LSTSESSWNE SRDFCKGKGS TLAIVNTPEK LKFLQDITDA EKYFIGLIYH REEKRWRWIN NSVFNGNVTN QNQNFNCATI GLTKTFDAAS CDISYRRICE KNAKHHHHHH
Product Science Overview
C-Type Lectin Domain Family 5, Member A (CLEC5A), also known as C-type lectin superfamily member 5 (CLECSF5) and myeloid DAP12-associating lectin 1 (MDL-1), is a protein encoded by the CLEC5A gene in humans . This protein is a member 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 an extracellular domain containing characteristic structural motifs of the C-type lectin superfamily . It lacks signaling motifs and therefore 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 .
The primary function of CLEC5A is to act as a cell surface receptor that signals via TYROBP (DAP12) . It plays a crucial role in regulating inflammatory responses and osteoclastogenesis . Activation of CLEC5A induces the production of various cytokines, including TNF-α, IL-1, IL-6, IL-8, and IL-17A, as well as chemokines like MIP-1α, RANTES, IP-10, and MDC . This protein is also involved in amplifying the innate immune response .
One of the most well-known ligands for CLEC5A is the dengue virus. The binding of the dengue virus to CLEC5A triggers signaling through the phosphorylation of DAP12, leading to the induction of pro-inflammatory cytokines . This interaction does not result in viral entry but stimulates the release of pro-inflammatory cytokines, contributing to the severe immune response observed in dengue virus infections, such as dengue hemorrhagic fever (DHF) and dengue shock syndrome (DSS) .
Human recombinant CLEC5A produced in Sf9 cells (a cell line derived from the fall armyworm, Spodoptera frugiperda) is used for research purposes. The recombinant protein is typically used to study the structure and function of CLEC5A, as well as its interactions with ligands and its role in various biological processes. The use of recombinant proteins allows for the detailed analysis of protein function and the development of potential therapeutic interventions targeting CLEC5A.
