Analytical Data
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Gene name
CLEC2C
- Application
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Alternative Names
CLEC2C;CLEC2C;Early activation antigen CD69
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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
Q07108
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Expression Region
62-199aa
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AA Sequence
SVGQYNCPG QYTFSMPSDS HVSSCSEDWV GYQRKCYFIS TVKRSWTSAQ NACSEHGATL AVIDSEKDMN FLKRYAGREE HWVGLKKEPG HPWKWSNGKE FNNWFNVTGS DKCVFLKNTE VSSMECEKNL YWICNKPYK
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Molecular Weight
17 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
CLEC2C, a member of the C-type lectin-like receptor family, plays a crucial role in immune responses and has garnered significant attention in recent research. It is primarily expressed on various immune cells, including dendritic cells and macrophages, and is involved in recognizing specific glycoproteins associated with pathogens. Recent studies have highlighted the importance of CLEC2C in mediating immune tolerance and regulation, making it a key player in both initiating and resolving immune responses. Its unique structure and ligand-binding properties suggest that it may interact with a range of endogenous and exogenous molecules, influencing diverse physiological processes. Researchers are increasingly focusing on CLEC2C's potential as a therapeutic target in autoimmune diseases, infections, and cancers, where modulation of immune responses could lead to improved clinical outcomes. Additionally, understanding its signaling pathways and interactions may provide insights into the development of novel immunotherapies. Given its significant implications in immunology, the continued exploration of CLEC2C will likely yield valuable information pertaining to immune system dynamics and therapeutic innovations.











