Analytical Data
-
Gene name
GA
- Application
-
Alternative Names
GA；DDIT1；GADD45；Growth arrest and DNA damage-inducible Protein GADD45 alpha
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P24522
-
Expression Region
1-165aa
-
AA Sequence
MTLEEFSAGEQKTERMDKVGDALEEVLSKALSQRTITVGVYEAAKLLNVDPDNVVLCLLAADEDDDRDVALQIHFTLIQAFCCENDINILRVSNPGRLAELLLLETDAGPAASEGAEQPPDLHCVLVTNPHSSQWKDPALSQLICFCRESRYMDQWVPVINLPER
-
Molecular Weight
34.3 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
GA (Glycosylated Antibody) recombinant proteins have garnered significant attention in the field of biopharmaceuticals due to their potential in therapeutic applications and diagnostic tools. Historically, antibodies have been essential in targeting specific antigens for various diseases, including cancers and autoimmune disorders. However, the production of native antibodies can be challenging due to limitations in yield, functionality, and the complex post-translational modifications they undergo. This has propelled researchers to explore recombinant technology as a viable alternative, allowing for the design of glycosylated proteins that mimic the natural counterparts more closely. Recombinant DNA technology facilitates the expression of antibodies in host systems, enabling precise control over glycosylation patterns, which are crucial for enhancing stability, efficacy, and reducing immunogenicity. Studies have demonstrated that GA recombinant proteins not only preserve the binding affinity and specificity of their native forms but also exhibit improved pharmacokinetic properties. As advances in genetic engineering and bioprocessing continue to unfold, the focus on optimizing GA recombinant protein production methods, including choosing appropriate host cells and expression systems, has intensified. This ongoing research aims to bridge the gap between basic science and clinical applications, ultimately leading to more effective and accessible therapeutic options in the fight against various diseases.
