Analytical Data
-
Gene name
XPG
- Application
-
Alternative Names
ERCM2; ERCC5; UVDR; XPGC; Excision Repair Cross-Complementing Rodent Repair Deficiency 5; Cockayne Syndrome; DNA repair protein complementing XP-G cells
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P28715
-
Expression Region
Leu778~Ala986
-
Molecular Weight
31kDa
-
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
XPG, or xeroderma pigmentosum group G protein, is a crucial component of the nucleotide excision repair (NER) pathway, which is responsible for repairing DNA lesions caused by environmental agents like UV radiation and chemical mutagens. Mutations in the XPG gene are associated with Xeroderma Pigmentosum, a rare genetic disorder characterized by extreme sensitivity to UV light and a predisposition to skin cancer. Research on XPG recombinant protein has gained significant attention due to its role in maintaining genomic stability and preventing carcinogenesis. Understanding the structure and function of XPG can provide insights into its interactions with other NER components, as well as its enzymatic activities, such as endonuclease function that facilitates the excision of damaged DNA. This knowledge is pivotal for developing therapeutic strategies not only for conditions related to NER deficiencies but also for enhancing DNA repair mechanisms in cancer therapies. By investigating the properties of recombinant XPG, researchers aim to elucidate its role in DNA repair, explore its potential applications in gene therapy, and develop novel approaches to treat disorders linked to DNA damage and stress response.











