Analytical Data
-
Gene name
CLEC4C
- Application
-
Alternative Names
CLEC4C；BDCA2；CLECSF11；CLECSF7；C-type lectin domain family 4 member C
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8WTT0
-
Expression Region
45-213aa
-
AA Sequence
NFMYSKTVKRLSKLREYQQYHPSLTCVMEGKDIEDWSCCPTPWTSFQSSCYFISTGMQSWTKSQKNCSVMGADLVVINTREEQDFIIQNLKRNSSYFLGLSDPGGRRHWQWVDQTPYNENVTFWHSGEPNNLDERCAIINFRSSEEWGWNDIHCHVPQKSICKMKKIYI
-
Molecular Weight
24.1 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
CLEC4C, also known as DC-SIGNR, is a C-type lectin receptor primarily expressed in dendritic cells and macrophages, playing a pivotal role in the immune response. This receptor is known for its ability to bind to a variety of pathogens, including viruses and bacteria, facilitating their recognition and internalization by antigen-presenting cells. Research has indicated that CLEC4C can influence T-cell activation and polarize immune responses, making it a potential target for therapeutic strategies in infectious diseases, cancer, and autoimmune disorders. The study of CLEC4C recombinant proteins has gained significant interest as these proteins can serve as tools for understanding the receptor's structure-function relationships, its interactions with various ligands, and its role in immune modulation. By elucidating the mechanisms underlying CLEC4C interactions, researchers aim to develop novel immunotherapies and vaccines that enhance immune responses or attenuate undesirable inflammatory processes. Furthermore, as the landscape of infectious diseases evolves, understanding the specificity and efficacy of CLEC4C in recognizing emerging pathogens remains a critical area of investigation. The recombinant form of CLEC4C not only aids in basic research but also holds promise for clinical applications, offering a pathway to harness the immune system more effectively against various diseases. Overall, the exploration of CLEC4C recombinant proteins represents a significant step forward in immunology, with implications that extend from fundamental science to the development of innovative therapeutic approaches.
