Analytical Data
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Gene name
CLEC1A
- Application
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Alternative Names
CLEC1A；CLECSF1；C-type lectin domain family 3 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
Q8NC01
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Expression Region
22-280aa
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AA Sequence
LHSQGSATTR HPEPRRTEHR APSSTWRPVA LTLLTLCLVL LIGLAALGLL FFQYYQLSNT GQDTISQMEE RLGNTSQELQ SLQVQNIKLA GSLQHVAEKL CRELYNKAGA HRCSPCTEQW KWHGDNCYQF YKDSKSWEDC KYFCLSENST MLKINKQEDL EFAASQSYSE FFYSYWTGLL RPDSGKAWLW MDGTPFTSEL FHIIIDVTSP RSRDCVAILN GMIFSKDCKE LKRCVCERRA GMVKPESLHV PPETLGEGD
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Molecular Weight
52 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
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Protein Description
CLEC1A, also known as C-type lectin domain family 1 member A, is a type of receptor primarily expressed on dendritic cells and macrophages, playing a crucial role in the immune system. This protein is known for its involvement in pathogen recognition and the modulation of immune responses. Research indicates that CLEC1A can bind to specific carbohydrate structures on the surface of various pathogens, including viruses and bacteria, thereby facilitating their uptake and subsequent presentation to T cells. This process is essential for the initiation and regulation of adaptive immunity. The study of CLEC1A recombinant proteins has garnered interest due to their potential application in vaccine development and immunotherapy, aiming to enhance the immune response against infectious diseases and cancer. Additionally, understanding the functional mechanisms of CLEC1A can provide insights into its role in autoimmune conditions and inflammatory responses. Advances in molecular biology and protein engineering techniques have enabled researchers to produce and characterize CLEC1A recombinant proteins, allowing for detailed studies on their structural properties and interactions with ligands. By elucidating the pathways and mechanisms by which CLEC1A operates, these studies hold promise for developing novel therapeutic strategies that harness the immune system's capabilities. Overall, the research on CLEC1A recombinant proteins is pivotal in advancing our understanding of immune modulation and opening new avenues for combatting infectious diseases and enhancing vaccine efficacy.
