Analytical Data
-
Gene name
gox
- Application
-
Alternative Names
gox；GOX1；2-Hydroxyacid oxidase 1
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9UJM8
-
Expression Region
1-370aa
-
AA Sequence
MRGSHHHHHHGMASMTGGQQMGRDLYDDDDKDRWGSMLPRLICINDYEQH AKSVLPKSIYDYYRSGANDEETLADNIAAFSRWKLYPRMLRNVAETDLST SVLGQRVSMPICVGATAMQRMAHVDGELATVRACQSLGTGMMLSSWATSS IEEVAEAGPEALRWLQLYIYKDREVTKKLVRQAEKMGYKAIFVTVDTPYL GNRLDDVRNRFKLPPQLRMKNFETSTLSFSPEENFGDDSGLAAYVAKAID PSISWEDIKWLRRLTSLPIVAKGILRGDDAREAVKHGLNGILVSNHGARQ LDGVPATIDVLPEIVEAVEGKVEVFLDGGVRKGTDVLKALALGAKAVFVG RPIVWGLAFQGEKGVQDVLEILKEEFRLAMALSGCQNVKVIDKTLVRKNP LAVSKI
-
Molecular Weight
45 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
Research on the GOx (glucose oxidase) recombinant protein has gained significant attention due to its diverse applications in biotechnology and medicine. GOx, an enzyme that catalyzes the oxidation of glucose to gluconic acid and hydrogen peroxide, serves as an essential tool in various fields, including biosensors, food preservation, and biocatalysis. The rise of synthetic biology has enabled the production of GOx through recombinant DNA technology, allowing for higher yields, enhanced purity, and tailored properties compared to enzyme extracted from natural sources. Further, recombinant GOx can be engineered to exhibit improved stability and activity in specific conditions, broadening its applicability. Its role in glucose monitoring has been particularly important for diabetes management, leading to the development of advanced glucose biosensors that offer rapid and accurate readings while minimizing interference. Moreover, GOx has shown potential in cancer therapy, as hydrogen peroxide produced during its enzymatic activity can induce cytotoxic effects in tumor cells. The ongoing research focuses on optimizing the expression systems, purification methods, and functional modifications of recombinant GOx to fully harness its potential, ensuring a sustainable and efficient supply for industrial and medical applications. Overall, the study of recombinant GOx is a promising avenue for advancing technologies in health care, environmental management, and food industry enhancements.
