Analytical Data
-
Gene name
gldA
- Application
-
Alternative Names
gldA;Hydroxyacid-oxoacid transhydrogenase. mitochondrial
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P32816
-
Expression Region
1-370aa
-
AA Sequence
MAAERVFISP AKYVQGKNVI TKIANYLEGI GNKTVVIADE IVWKIAGHTI VNELKKGNIA AEEVVFSGEA SRNEVERIAN IARKAEAAIV IGVGGGKTLD TAKAVADELD AYIVIVPTAA STDAPTSALS VIYSDDGVFE SYRFYKKNPD LVLVDTKIIA NAPPRLLASG IADALATWVE ARSVIKSGGK TMAGGIPTIA AEAIAEKCEQ TLFKYGKLAY ESVKAKVVTP ALEAVVEANT LLSGLGFESG GLAAAHAIHN GFTALEGEIH HLTHGEKVAF GTLVQLALEE HSQQEIERYI ELYLSLDLPV TLEDIKLKDA SREDILKVAK AATAEGETIH NAFNVTADDV ADAIFAADQY AKAYKEKHRK
-
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
The gldA gene encodes for glucose-6-phosphate dehydrogenase (G6PD), an essential enzyme involved in the pentose phosphate pathway, which is crucial for cellular metabolism and maintaining redox balance. Research on gldA recombinant proteins has gained significant attention due to their potential applications in biotechnology and medicine. G6PD plays a vital role in protecting cells from oxidative stress by generating NADPH, a reducing agent that is pivotal for biosynthetic reactions and the detoxification of reactive oxygen species (ROS). Mutations in the gldA gene can lead to G6PD deficiency, resulting in various health issues, including hemolytic anemia. By producing gldA recombinant proteins, researchers aim to better understand the enzyme's structure-function relationship, explore its regulatory mechanisms, and establish its role in different biological processes. Additionally, gldA recombinant proteins are of great interest for developing diagnostic tools and therapeutic strategies for conditions associated with G6PD deficiency. The ability to produce these proteins in large quantities through recombinant DNA technology allows for detailed biochemical characterization and potential applications in enzyme replacement therapies, drug design, and metabolic engineering. This research not only enhances our understanding of gldA's biological significance but also opens new avenues for innovative treatments targeting metabolic disorders and oxidative stress-related diseases.











