CLEC4E/Mincel Protein(C-6His) (recombinant human)

Protein Construction: Recombinant Human C-Type Lectin Domain Family 4 Member E is produced by our Mammalian expression system and the target gene encoding Arg41-Leu219 is expressed with a 6His tag at the C-terminus. Sequence: Arg41-Leu219. Fusion tag: C-6His Endotoxin: < 1.0 EU per µg as determined by the LAL method. Apparent Molecular Mass: 26 kDa. Protein function: C-Type Lectin Domain Family 4 Member E (CLEC4E) is a 219 amino acid single-pass type II membrane protein that contains one C-type Lectin domain. It is expressed in monocytes, CLEC4E functions as a downstream target of C/EBP ß and is thought to play a role in the inflammatory response, possibly via transcriptional control of C/EBP ß. CLEC4E may play a role in the response to inflammatory stimuli in peritoneal macrophages and may be involved in immune surveillance processes under transcriptional control of CEBPB. Human CLEC4E shares 67% sequence identity with its mouse counterpart, suggesting a similar function between species. CLEC-4E exists as multiple alternatively spliced isoforms that are encoded by a gene which maps to a natural killer gene complex region on human chromosome 12. Protein function: A calcium-dependent lectin that acts as a pattern recognition receptor of the innate immune system. Recognizes damage-associated molecular patterns (DAMPs) of abnormal self and pathogen-associated molecular patterns (PAMPs) of bacteria and fungi (PubMed:18509109, PubMed:23602766). The PAMPs notably include mycobacterial trehalose 6,6'-dimycolate (TDM), a cell wall glycolipid with potent adjuvant immunomodulatory functions (PubMed:23602766, PubMed:24101491). Interacts with signaling adapter Fc receptor gamma chain/FCER1G to form a functional complex in myeloid cells. Binding of mycobacterial trehalose 6,6'- dimycolate (TDM) to this receptor complex leads to phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of FCER1G, triggering activation of SYK, CARD9 and NF-kappa-B, consequently driving maturation of antigen-presenting cells and shaping antigen-specific priming of T-cells toward effector T- helper 1 and T-helper 17 cell subtypes. Specifically recognizes alpha-mannose residues on pathogenic fungi of the genus Malassezia and mediates macrophage activation. Through recognition of DAMPs released upon nonhomeostatic cell death, enables immune sensing of damaged self and promotes inflammatory cell infiltration into the damaged tissue. [The UniProt Consortium]