Analytical Data
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Gene name
DCAF1
- Application
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Alternative Names
KIAA0800; RIP; VPRBP
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Species
Human
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Source
Baculovirus
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9Y4B6-1
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Expression Region
F1071-G1390
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Protein Length
Partial
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Molecular Weight
36.6 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
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Protein Description
DCAF1, or DDB1 and CUL4-associated factor 1, is a key protein involved in the regulation of various cellular processes, including transcription, DNA repair, and cell cycle progression. It acts as a substrate receptor for the CRL4 ubiquitin ligase complex, facilitating the ubiquitination and subsequent degradation of target proteins. Research on DCAF1 has gained traction due to its implications in tumorigenesis and its role in the response to DNA damage, making it a potential biomarker for cancer prognosis and a target for therapeutic intervention. Recent studies have focused on the structural characterization and functional analysis of DCAF1, revealing its intricate interactions with other proteins and RNA. The recombinant expression of DCAF1 in various systems has allowed researchers to explore its biochemical properties, including its affinity for specific substrates and involvement in cellular signaling pathways. Understanding the nuances of DCAF1 function could provide insight into the underlying mechanisms of cancer development and progression, as well as open avenues for novel therapeutic strategies targeting the ubiquitin-proteasome system.
