Analytical Data
-
Gene name
HLAC
- Application
-
Alternative Names
HLA-C;HLAC;HLA class I histocompatibility antigen. C alpha chain
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P10321
-
Expression Region
25-308aa
-
AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSCSHSMRY FDTAVSRPGR GEPRFISVGY VDDTQFVRFD SDAASPRGEP RAPWVEQEGP EYWDRETQKY KRQAQADRVS LRNLRGYYNQ SEDGSHTLQR MSGCDLGPDG RLLRGYDQSA YDGKDYIALN EDLRSWTAAD TAAQITQRKL EAARAAEQLR AYLEGTCVEW LRRYLENGKE TLQRAEPPKT HVTHHPLSDH EATLRCWALG FYPAEITLTW QRDGEDQTQD TELVETRPAG DGTFQKWAAV VVPSGQEQRY TCHMQHEGLQ EPLTLSWEPS SQPTIPI
-
Molecular Weight
35 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
HLAC (Human Leukocyte Antigen Complex) is an essential component of the immune system, playing a critical role in antigen presentation and the regulation of immune responses. The study of HLAC recombinant proteins has gained significant attention due to their potential applications in immunotherapy and vaccine development. Understanding the structural and functional properties of HLAC proteins can help unveil mechanisms of immune recognition and tolerance, which are crucial for addressing autoimmune diseases and organ transplant rejection. Recent advancements in molecular cloning and protein expression technologies have facilitated the production of recombinant HLAC proteins, allowing researchers to investigate their interactions with T-cell receptors and other immune molecules. Moreover, the reconstitution of HLAC molecules in various model systems offers valuable insights into their roles in disease pathology. As research progresses, the characterization of HLAC recombinant proteins is anticipated to contribute to the development of novel therapeutic strategies, including personalized medicine approaches that harness the power of the immune system to target specific diseases more effectively.
