Analytical Data
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Gene name
C4orf3
- Application
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Alternative Names
Hepatitis C virus F protein-transactivated protein 1 ;HCV F-transactivated protein 1
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8WVX3
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Expression Region
1-44aa
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Molecular Weight
20.8 kDa
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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
C4orf3, also known as Chromosome 4 Open Reading Frame 3, has emerged as a significant subject of research due to its potential roles in various cellular processes and diseases. As a gene located on chromosome 4, C4orf3 encodes a protein that participates in critical biological activities, including cell signaling, proliferation, and differentiation. Studies have suggested that alterations in C4orf3 expression may be linked to several conditions, encompassing cancer, neurodegenerative diseases, and other pathologies. Furthermore, the investigation of C4orf3 recombinant proteins offers valuable insights into its functional mechanisms and interactions at the molecular level. By creating recombinant versions of the C4orf3 protein, researchers can better understand its structure, stability, and activity, paving the way for potential therapeutic applications. Additionally, the use of recombinant proteins provides a platform for high-throughput screening of small molecules that may modulate the function of C4orf3, thereby highlighting its relevance in drug discovery efforts. Overall, ongoing research into C4orf3 and its recombinant proteins holds promise for elucidating its biological significance and developing novel therapeutic strategies targeting diseases associated with its dysfunction.
