Analytical Data
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Gene name
GPATCH4
- Application
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Alternative Names
GPATCH4；GPATC4；G patch domain-containing Protein 4
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q5T3I0
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Expression Region
1-446aa
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AA Sequence
MNVTPEVKSRGMKFAEEQLLKHGWTQGKGLGRKENGITQALRVTLKQDTHGVGHDPAKEFTNHWWNELFNKTAANLVVETGQDGVQIRSLSKETTRYNHPKPNLLYQKFVKMATLTSGGEKPNKDLESCSDDDNQGSKSPKILTDEMLLQACEGRTAHKAARLGITMKAKLARLEAQEQAFLARLKGQDPGAPQLQSESKPPKKKKKKRRQKEEEEATASERNDADEKHPEHAEQNIRKSKKKKRRHQEGKVSDEREGTTKGNEKEDAAGTSGLGELNSREQTNQSLRKGKKKKRWHHEEEKMGVLEEGGKGKEAAGSVRTEEVESRAYADPCSRRKKRQQQEEEDLNLEDRGEETVLGGGTREAESRACSDGRSRKSKKKRQQHQEEEDILDVRDEKDGGAREAESRAHTGSSSRGKRKRQQHPKKERAGVSTVQKAKKKQKKRD
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Molecular Weight
50.3kDa
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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
Related Products
Protein Description
GPATCH4, a member of the G-patch domain-containing protein family, has garnered significant attention in recent years due to its potential roles in various biological processes, including RNA metabolism and cellular regulation. Initial studies suggest that GPATCH4 may be involved in the regulation of gene expression and has been implicated in several cellular pathways, including those associated with stress response and viral infection. Its unique structural features enable interactions with RNA and other protein partners, making it a critical player in post-transcriptional modifications. Research has indicated that altered expression levels of GPATCH4 could be linked to various diseases, including cancer and neurodegenerative disorders, emphasizing the need for a deeper understanding of its functional mechanisms. As such, investigations into GPATCH4 recombinant proteins have become essential for elucidating their roles in cellular contexts and identifying potential therapeutic targets. Recent advances in protein expression systems have facilitated the production and purification of GPATCH4, allowing researchers to characterize its functional properties and interactions in vitro. This ongoing research aims to unravel the complexities of GPATCH4 in health and disease, ultimately contributing to the development of novel strategies for diagnosis and treatment.
