CHI3L1 Protein, Human (HEK293, His)

The CHI3L1 protein is a binding lectin that lacks chitinase activity. CHI3L1 contributes to tissue remodeling, cellular adaptation to environmental changes, and T helper type 2 inflammatory responses. CHI3L1 also controls hyperoxia-induced injury, inflammation, and epithelial cell apoptosis. CHI3L1 Protein, Human (HEK293, His) is the recombinant human-derived CHI3L1 protein, expressed by HEK293 , with C-6*His labeled tag.

Chitinase-3-like protein 1 (CHI3L1) is a carbohydrate-binding lectin with a specific affinity for chitin, although it lacks chitinase activity. Its main role extends beyond chitin degradation, as it is implicated in tissue remodeling and cellular responses to environmental changes. CHI3L1 plays a crucial role in T-helper cell type 2 (Th2) inflammatory responses and IL-13-induced inflammation, influencing allergen sensitization, inflammatory cell apoptosis, dendritic cell accumulation, and the differentiation of M2 macrophages. Additionally, it facilitates the invasion of pathogenic enteric bacteria into colonic mucosa and lymphoid organs. CHI3L1 is involved in the activation of the AKT1 signaling pathway, leading to IL8 production in colonic epithelial cells. Furthermore, it regulates antibacterial responses in the lungs, contributing to macrophage bacterial killing, controlling bacterial dissemination, and enhancing host tolerance. In lung tissues, CHI3L1 also plays a role in regulating hyperoxia-induced injury, inflammation, and epithelial apoptosis. Structurally, CHI3L1 functions as a monomer.

Measured by the ability of the immobilized protein to support the adhesion of FaDu human squamous cell carcinoma cells. The ED₅₀ for this effect is 0.6-3.0 μg/mL.

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  Measured by the ability of the immobilized protein to support the adhesion of FaDu human squamous cell carcinoma cells. The ED₅₀ for this effect is 2.603 μg/mL, corresponding to a specific activity is 384.1721 units/mg.

Human

HEK293

C-6*His

P36222 (Y22-T383)

1116  [NCBI]

Full Length of Mature Protein

YKLVCYYTSWSQYREGDGSCFPDALDRFLCTHIIYSFANISNDHIDTWEWNDVTLYGMLNTLKNRNPNLKTLLSVGGWNFGSQRFSKIASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPGRRDKQHFTTLIKEMKAEFIKEAQPGKKQLLLSAALSAGKVTIDSSYDIAKISQHLDFISIMTYDFHGAWRGTTGHHSPLFRGQEDASPDRFSNTDYAVGYMLRLGAPASKLVMGIPTFGRSFTLASSETGVGAPISGPGIPGRFTKEAGTLAYYEICDFLRGATVHRILGQQVPYATKGNQWVGYDDQESVKSKVQYLKDRQLAGAMVWALDLDDFQGSFCGQDLRFPLTNAIKDALAAT

Approximately 41-46 kDa band in SDS-PAGE under reducing conditions due to the glycosylation.

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  ≥ 95%, as determined by reducing SDS-PAGE.

Lyophilized powder

1.Lyophilized from a 0.22 μm filtered solution of 20 mM Tris-HCl, 300 mM NaCl, 2 mM EDTA, pH 8.5.
2.Lyophilized from a 0.22 μm filtered solution of 20 mM PB, 150 mM NaCl, 2 mM EDTA, pH 7.4.
3.Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4, 8% 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. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

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.