Analytical Data
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Gene name
CLEC4M
- Application
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Alternative Names
CLEC4M；CD209L；CD209L1；CD299；C-type lectin domain family 4 member M
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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
Q9H2X3
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Expression Region
78-399aa
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AA Sequence
SLSQEQSEQD AIYQNLTQLK AAVGELSEKS KLQEIYQELT QLKAAVGELP EKSKLQEIYQ ELTRLKAAVG ELPEKSKLQE IYQELTRLKA AVGELPEKSK LQEIYQELTR LKAAVGELPE KSKLQEIYQE LTELKAAVGE LPEKSKLQEI YQELTQLKAA VGELPDQSKQ QQIYQELTDL KTAFERLCRH CPKDWTFFQG NCYFMSNSQR NWHDSVTACQ EVRAQLVVIK TAEEQNFLQL QTSRSNRFSW MGLSDLNQEG TWQWVDGSPL SPSFQRYWNS GEPNNSGNED CAEFSGSGWN DNRCDVDNYW ICKKPAACFR DE
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Molecular Weight
65 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
CLEC4M, also known as DC-SIGN (Dendritic Cell-Specific ICAM-3-Grabbing Non-integrin), is a C-type lectin receptor predominantly expressed on dendritic cells and macrophages. It plays a crucial role in immune response by recognizing and binding various pathogens, including viruses and bacteria, thus facilitating their uptake and presentation to T cells. Research into CLEC4M has gained significance due to its involvement in several infectious diseases, including HIV, dengue, and tuberculosis, as it serves as a major entry point for these pathogens into host cells. Understanding the structural and functional aspects of CLEC4M is essential for developing novel therapeutic strategies and vaccines. Recent studies have focused on the receptor’s role in modulating immune responses, its interaction with microbial components, and the implications of genetic polymorphisms in susceptibility to infections. Moreover, the potential use of CLEC4M as a biomarker for disease progression and prognosis is being explored, highlighting its significance in both basic and clinical immunology research. The ongoing investigation into the reorganization of CLEC4M not only elucidates its biological function but also contributes to the broader understanding of immune regulation and host-pathogen interactions.
