Intelectin-1/ITLN1 Protein, Human (N-His, C-Myc)

Intelectin-1/ITLN1 is a lectin with specific affinity for microbial carbohydrate chains and recognizes β-linked D-galactofuranosose, D-glycerolphosphate modified glycans, D-glycerol-D-talo-oct- 2-ulosonic acid (KO) and 3-deoxy-D-manno-oct-2-keto acid (KDO). It binds to bacterial glycans and helps defend against microorganisms. Intelectin-1/ITLN1 Protein, Human (N-His, C-myc) is the recombinant human-derived Intelectin-1/ITLN1 protein, expressed by E. coli , with N-10*His, C-Myc labeled tag.

The Intelectin-1/ITLN1 protein operates as a lectin with a specific affinity for microbial carbohydrate chains in a calcium-dependent manner. It recognizes microbial glycans containing a terminal acyclic 1,2-diol moiety, such as 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). This lectin binds to glycans found in both Gram-positive and Gram-negative bacteria, including K. pneumoniae, S. pneumoniae, Y. pestis, P. mirabilis, and P. vulgaris, while showing no affinity for human glycans. Likely contributing to the defense system against microorganisms, Intelectin-1/ITLN1 may function as an adipokine with a potential role in glucose uptake regulation and insulin-stimulated glucose uptake in adipocytes. It enhances AKT phosphorylation, both in the absence and presence of insulin. Additionally, Intelectin-1/ITLN1 may interact with lactoferrin/LTF, increasing its uptake and potentially playing a role in iron absorption. The protein forms homotrimers through disulfide linkages and may interact with lactoferrin/LTF.

Measured by its binding ability in a functional ELISA. Immobilized Human ITLN1 Protein at 2 μg/mL (100 μL/well) can bind Anti-ITLN1 Polyclonal antibody. The ED₅₀ for this effect is 5-15 ng/mL.

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  Immobilized Human ITLN1 Protein at 2 μg/mL (100 μL/well) can bind Anti-ITLN1 Polyclonal antibody. The ED₅₀ for this effect is 7.12 ng/mL.

Human

E. coli

N-10*His;C-Myc

Q8WWA0 (T19-S298)

55600

Full Length of Mature Protein

TDEANTYFKEWTCSSSPSLPRSCKEIKDECPSAFDGLYFLRTENGVIYQTFCDMTSGGGGWTLVASVHENDMRGKCTVGDRWSSQQGSKAVYPEGDGNWANYNTFGSAEAATSDDYKNPGYYDIQAKDLGIWHVPNKSPMQHWRNSSLLRYRTDTGFLQTLGHNLFGIYQKYPVKYGEGKCWTDNGPVIPVVYDFGDAQKTASYYSPYGQREFTAGFVQFRVFNNERAANALCAGMRVTGCNTEHHCIGGGGYFPEASPQQCGDFSGFDWSGYGTHVGYS

Approximately 36 kDa, based on SDS-PAGE under reducing conditions.

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  ≥ 90%, as determined by reducing SDS-PAGE.

Lyophilized powder

1.Lyophilized from a 0.22 μm filtered solution of 10 mM Tris-HCl, 1 mM EDTA, 6% Trehalose, pH 8.0.
2.Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4, 6% trehalose.
Please refer to the lot-specific COA for specific buffer information.
Note: For SPR assay, please replace the buffer. Primary amine components (e.g., Tris, imidazole) can affect protein-coupled chips.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O.

Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.