Analytical Data
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Gene name
GAN
- Application
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Alternative Names
GAN1; KLHL16; Giant Axonal Neuropathy; Kelch-like protein 16
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9H2C0
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Expression Region
Cys30~Gly326
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Molecular Weight
37kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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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.
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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.
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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
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Protein Description
The study of GAN (Growth Arrest and DNA Damage-inducible 45) recombinant protein has gained significant attention due to its crucial role in cellular processes such as growth arrest, apoptosis, and response to DNA damage, which are vital for maintaining genomic stability. GAN is part of the GADD family of proteins, which are induced by various stressors, including oxidative stress and DNA damage, making it a key player in the cellular stress response. Research has shown that GAN is involved in tumor suppression and may act as a potential biomarker for cancer diagnosis and progression. Advances in recombinant DNA technology have enabled scientists to produce GAN in sufficient quantities for detailed structural and functional studies, facilitating a deeper understanding of its mechanisms at the molecular level. This understanding is essential for exploring therapeutic avenues, as targeting the pathways mediated by GAN could lead to novel strategies in cancer treatment and other diseases linked to cellular stress responses. Furthermore, the ability to engineer and modify GAN recombinant proteins opens up possibilities for their application in targeted therapies and gene editing techniques, thus underscoring the significance of this research in both basic biology and translational medicine.
