Recombinant Human Omentin/Intelectin-1/ITLN-1 (N-6His)

Source: E. coli. MW :32.7kD. Recombinant Human Intelectin-1 is produced by our E.coli expression system and the target gene encoding Thr19-Ser298 is expressed with a 6His tag at the N-terminus. Intelectin-1(ITLN1) is a secreted protein and contains 1 fibrinogen C-terminal domain. Intelectin-1 is a 40 kDa Ca-dependent galactofuranose-binding lectin that is not a C-type lectin. It is expressed on multiple cell types and appears to participate in insulin signaling and microbe recognition. The protein has no effect on basal glucose uptake but enhances insulin-stimulated glucose uptake in adipocytes. It increases AKT phosphorylation in the absence and presence of insulin and it may play a role in the defense systemagainst microorganisms. It also may specifically recognize carbohydrate chains of pathogens and bacterial components containing galactofuranosy l residues, in a calcium-dependent manner. Protein function: Lectin that specifically recognizes microbial carbohydrate chains in a calcium-dependent manner (PubMed:11313366, PubMed:26148048). Binds to microbial glycans that contain a terminal acyclic 1,2-diol moiety, including beta- linked D-galactofuranose (beta-Galf), D-phosphoglycerol-modified glycans, D-glycero-D-talo-oct-2-ulosonic acid (KO) and 3-deoxy-D- manno-oct-2-ulosonic acid (KDO) (PubMed:26148048). Binds to glycans from Gram-positive and Gram-negative bacteria, including K.pneumoniae, S.pneumoniae, Y.pestis, P.mirabilis and P.vulgaris (PubMed:26148048). Does not bind human glycans (PubMed:26148048). Probably plays a role in the defense system against microorganisms (Probable). May function as adipokine that has no effect on basal glucose uptake but enhances insulin-stimulated glucose uptake in adipocytes (PubMed:16531507). Increases AKT phosphorylation in the absence and presence of insulin (PubMed:16531507). May interact with lactoferrin/LTF and increase its uptake, and may thereby play a role in iron absorption (PubMed:11747454, PubMed:23921499). [The UniProt Consortium]