Analytical Data
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Gene name
RBKS
- Application
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Alternative Names
RBKS;RBSK;Ribokinase
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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
Q9H477
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Expression Region
1-322aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMAASGEPQRQWQEEVAAVVVVGSCMTDLVS LTSRLPKTGETIHGHKFFIGFGGKGANQCVQAARLGAMTSMVCKVGKDSF GNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIVAGANLL LNTEDLRAAANVISRAKVMVCQLEITPATSLEALTMARRSGVKTLFNPAP AIADLDPQFYTLSDVFCCNESEAEILTGLTVGSAADAGEAALVLLKRGCQ VVIITLGAEGCVVLSQTEPEPKHIPTEKVKAVDTTGAGDSFVGALAFYLA YYPNLSLEDMLNRSNFIAAVSVQAAGTQSSYPYKKDLPLTLF
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Molecular Weight
36 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
RBKS, or ribonucleoside-triphosphate reductase subunit M2, is a crucial enzyme involved in the de novo synthesis of deoxyribonucleotides, which are essential for DNA replication and repair. The enzyme catalyzes the reduction of ribonucleoside diphosphates to their corresponding deoxyribonucleotides, thereby providing the necessary building blocks for DNA synthesis. Research on RBKS has gained significant attention due to its pivotal role in cellular proliferation and the maintenance of genomic stability. Dysregulation of RBKS activity is linked to various cancer types, where it contributes to the malignancy by supporting uncontrolled cell division. Understanding the structure and function of RBKS can provide insights into its mechanism of action and facilitate the development of targeted therapies for cancers associated with its overexpression or mutation. Recent studies have focused on the characterization of its enzymatic properties, regulatory mechanisms, and interactions with other cellular components, aiming to elucidate its role in pathophysiological processes. The integration of advanced techniques such as structural biology, molecular dynamics simulations, and high-throughput screening has opened new avenues for exploring pharmacological inhibitors and modulators of RBKS, potentially leading to novel cancer treatments. Overall, the research on RBKS is critical not only for basic biological understanding but also for its therapeutic implications in oncology.
