Analytical Data
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Gene name
RAD1
- Application
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Alternative Names
RAD1;REC1;Cell cycle checkpoint Protein RAD1
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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
O60671
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Expression Region
1-282aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMPLLTQQIQDEDDQYSLVASLDNVRNLSTI LKAIHFREHATCFATKNGIKVTVENAKCVQANAFIQAGIFQEFKVQEESV TFRINLTVLLDCLSIFGSSPMPGTLTALRMCYQGYGYPLMLFLEEGGVVT VCKINTQEPEETLDFDFCSTNVINKIILQSEGLREAFSELDMTSEVLQIT MSPDKPYFRLSTFGNAGSSHLDYPKDSDLMEAFHCNQTQVNRYKISLLKP STKALVLSCKVSIRTDNRGFLSLQYMIRNEDGQICFVEYYCCPDEEVPES ES
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Molecular Weight
34 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
RAD1 is a critical protein involved in the DNA damage response and repair mechanisms in eukaryotic cells. It forms a part of the RAD1-RAD10 complex, which plays an essential role in the nucleotide excision repair pathway, a process responsible for removing a variety of DNA lesions resulting from environmental factors such as UV radiation and chemical exposure. Research on RAD1 has garnered significant attention due to its implications in cancer biology; deficiencies in DNA repair can lead to genomic instability, a hallmark of cancer. The study of RAD1 recombinant protein provides valuable insights into its structure-function relationships, facilitating the understanding of its role in maintaining genomic integrity. Advances in molecular biology techniques have enabled researchers to produce RAD1 as a recombinant protein, allowing for detailed biochemical characterization, investigations into its interaction with other proteins, and structural studies through techniques like X-ray crystallography and NMR spectroscopy. Understanding RAD1's mechanisms is crucial for developing therapeutic strategies that target defective DNA repair pathways in tumors. Additionally, unraveling the regulatory networks involving RAD1 may highlight novel biomarkers for cancer diagnosis and prognosis, as well as potential targets for drug development. As research evolves, the continued exploration of RAD1 and its complexes promises to shed light on the intricate processes of DNA repair and their critical roles in cancer development and treatment.
