Recombinant Human Intelectin-1/ITLN1 Protein (His Tag) | PKSH032833

Recombinant Human Intelectin-1/ITLN1 Protein (His Tag) | PKSH032833 | Gentaur US, UK & Europe Disrtribition

Synonyms: Intelectin-1; ITLN-1; Endothelial lectin HL-1; Galactofuranose-binding lectin; Intestinal lactoferrin receptor; Omentin; INTL; ITLN; LFR

Active Protein: N/A

Activity: 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.

Protein Construction: 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.

Fusion Tag: N-6His

Species: Human

Expressed Host: E.coli

Shipping: This product is provided as lyophilized powder which is shipped with ice packs.

Purity: > 90 % as determined by reducing SDS-PAGE.

Endotoxin: < 1.0 EU per µg as determined by the LAL method.

Stability and Storage: Generally, lyophilized proteins are stable for up to 12 months when stored at -20 to -80℃. Reconstituted protein solution can be stored at 4-8℃ for 2-7 days. Aliquots of reconstituted samples are stable at < -20℃ for 3 months.

Molecular Mass: 32.7 kDa

Formulation: Lyophilized from a 0.2 μm filtered solution of 50mM Tris, 100mMNaCl, 5mM GSH, 0.5mM GSSG, pH8.0 .

Reconstitution: Please refer to the printed manual for detailed information.

Background: 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.

Research Area: Signal Transduction, Microbiology, Cardiovascular, Cancer, metabolism,