Analytical Data
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Gene name
LECT1
- Application
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Alternative Names
Cleaved into the following 2 chains: Chondrosurfactant protein Short name: CH-SP Chondromodulin-1 Alternative name(s): Chondromodulin-I Short name: ChM-I
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O75829
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Expression Region
215-334aa
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Molecular Weight
29.8 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Recombinant proteins, such as LECT1 (lectin-like protein 1), have garnered significant attention in the fields of molecular biology and biotechnology due to their diverse functions and potential therapeutic applications. LECT1 is a member of the C-type lectin family, which is characterized by its ability to bind carbohydrates in a calcium-dependent manner. Research has shown that LECT1 plays a crucial role in various biological processes, including cell-cell interactions, immune response modulation, and inflammation, suggesting its involvement in both physiological and pathological conditions. The production of LECT1 through recombinant DNA technology allows for large-scale generation and purification of this protein, enabling detailed studies of its structural and functional properties. Furthermore, understanding the mechanisms of LECT1 in disease contexts, such as cancer and autoimmune disorders, opens avenues for developing novel therapeutic strategies. Overall, the study of recombinant LECT1 not only enhances our comprehension of its biological roles but also paves the way for its potential use in diagnostics and targeted therapies.
