Analytical Data
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Gene name
CLEC10A
- Application
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Alternative Names
CLEC10A；CLECSF13；CLECSF14；HML；C-type lectin domain family 10 member A
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8IUN9
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Expression Region
61-316aa
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AA Sequence
QNSKFQRDLVTLRTDFSNFTSNTVAEIQALTSQGSSLEETIASLKAEVEG FKQERQAGVSELQEHTTQKAHLGHCPHCPSVCVPVHSEMLLRVQQLVQDL KKLTCQVATLNNNASTEGTCCPVNWVEHQDSCYWFSHSGMSWAEAEKYCQ LKNAHLVVINSREEQNFVQKYLGSAYTWMGLSDPEGAWKWVDGTDYATGF QNWKPGQPDDWQGHGLGGGEDCAHFHPDGRWNDDVCQRPYHWVCEAGLGQ TSQESHVDHHHHHH
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Molecular Weight
30 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
CLEC10A, also known as the dendritic cell-specific intercellular adhesion molecule-3-grabbing nonintegrin (DC-SIGN), is a C-type lectin receptor primarily expressed on dendritic cells and macrophages. This receptor plays a critical role in the immune system, particularly in the recognition of glycoproteins on pathogens, facilitating their uptake and subsequent presentation to T cells. The study of CLEC10A recombinant protein has garnered significant attention due to its potential applications in both vaccine development and immunotherapy. Research has demonstrated that CLEC10A can enhance the immune response against various infections, including viral and fungal pathogens, by promoting efficient antigen capture and activation of immune cells. Furthermore, its ability to modulate immune responses opens avenues for therapeutic interventions in autoimmune diseases and cancer. Advances in recombinant DNA technology have enabled the production of CLEC10A as a functional protein, allowing scientists to investigate its structure-function relationship and interactions with ligands, as well as its pharmacological potential. Understanding the biology and mechanisms of CLEC10A could lead to innovative strategies for harnessing the immune system to combat diseases effectively.
