Analytical Data
-
Gene name
HLA-C
- Application
-
Alternative Names
HLA class I histocompatibility antigen, C alpha chain; HLA-C protein; MHC class I antigen; HLA-Cw
-
Species
Human
-
Source
E. coli
-
Tag
N-6*His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O78179
-
Expression Region
C25-I308
-
AA Sequence
CSHSMRYFYTAVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASPRGEPRAPWVEQEGPEYWDRETQKYKRQAQTDRVSLRNLRGYYNQSEAGSHTLQWMYGCDLGPDGRLLRGYDQSAYDGKDYIALNEDLRSWTAADTAAQITQRKWEAARAAEQQRAYLEGTCVEWLRRYLENGKETLQRAEHPKTHVTHHLVSDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPLTLRWEPSSQPTIPI
-
Protein Length
Partial
-
Molecular Weight
36.7 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
HLA-C (Human Leukocyte Antigen-C) is a critical component of the Major Histocompatibility Complex (MHC) class I molecules, which play a vital role in the immune response by presenting intracellular peptides to CD8+ T cells. This ability directly influences the recognition of infected or malignant cells, making HLA-C essential in both immune defense and transplantation immunology. Recent studies have shown that variations in HLA-C alleles are associated with different immune responses to pathogens, as well as with susceptibility to autoimmune diseases and the success of organ transplants. Therefore, understanding HLA-C's structure and function is paramount for developing targeted immunotherapies. Recombinant proteins of HLA-C are increasingly being utilized in research to elucidate its interactions with T cell receptors and to assess its role in immune evasion mechanisms employed by tumors and viruses. Furthermore, these recombinant proteins can serve as valuable tools for vaccine development and personalized medicine approaches by aiding in the identification of specific epitopes that can enhance T cell responses. The advances in genetic engineering technologies have facilitated the production of stable and functional HLA-C recombinant proteins, opening new avenues for experimental and clinical research aimed at harnessing the immune system to fight diseases. Overall, the exploration of HLA-C recombinant proteins can provide insights into immune regulation and pave the way for novel therapeutic strategies in infectious diseases, cancer, and autoimmune disorders.
