Analytical Data
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Gene name
RUVBL1
- Application
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Alternative Names
TRRAP;PAF400;Transformation/transcription domain-associated Protein
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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
Q9Y265
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Expression Region
1-456aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMKIEEVKSTTKTQRIASHSHVKGLGLDESG LAKQAASGLVGQENAREACGVIVELIKSKKMAGRAVLLAGPPGTGKTALA LAIAQELGSKVPFCPMVGSEVYSTEIKKTEVLMENFRRAIGLRIKETKEV YEGEVTELTPCETENPMGGYGKTISHVIIGLKTAKGTKQLKLDPSIFESL QKERVEAGDVIYIEANSGAVKRQGRCDTYATEFDLEAEEYVPLPKGDVHK KKEIIQDVTLHDLDVANARPQGGQDILSMMGQLMKPKKTEITDKLRGEIN KVVNKYIDQGIAELVPGVLFVDEVHMLDIECFTYLHRALESSIAPIVIFA SNRGNCVIRGTEDITSPHGIPLDLLDRVMIIRTMLYTPQEMKQIIKIRAQ TEGINISEEALNHLGEIGTKTTLRYSVQLLTPANLLAKINGKDSIEKEHV EEISELFYDAKSSAKILADQQDKYMK
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Molecular Weight
52 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
RUVBL1, a member of the RuvB-like (RUVBL) family of ATPases, plays a crucial role in various cellular processes, including DNA repair, chromatin remodeling, and regulation of gene expression. Its involvement in crucial cellular mechanisms has attracted significant attention from researchers, particularly due to its overexpression in various cancers, which suggests it may function as an oncogene. Studies have indicated that RUVBL1 is essential for the assembly of protein complexes that modulate transcription and the repair of DNA double-strand breaks, thus highlighting its importance in maintaining genomic stability. Moreover, recent findings have implicated RUVBL1 in the regulation of cell proliferation, apoptosis, and even the response to cellular stress. Given its pivotal roles, RUVBL1 is considered a potential target for cancer therapy, and understanding its structure and function through recombinant protein studies can provide insights into its mechanistic role in disease. Research focusing on the purification and characterization of RUVBL1 recombinant protein has the potential to facilitate the development of novel therapeutic strategies aimed at inhibiting its function in oncogenesis. These insights could lead to the identification of new biomarkers for cancer diagnosis and prognosis, highlighting the relevance of RUVBL1 as a promising target in oncology.
