Analytical Data
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Gene name
RB1
- Application
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Alternative Names
Retinoblastoma-associated protein; p105-Rb; p110-RB1; pRb; Rb; pp110; RB1; Homo sapiens; Human; Rb; Chromatin regulator; DNA-binding; Repressor
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Species
Human
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Source
E. coli
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Tag
C-StrepⅡ
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P06400
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Expression Region
S773-K928
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Protein Length
Partial
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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
RB1, or retinoblastoma protein, is a crucial tumor suppressor that plays a vital role in regulating the cell cycle and maintaining genomic stability. Mutations or dysfunction of the RB1 gene are implicated in various cancers, particularly retinoblastoma, a rare pediatric eye tumor. The study of RB1 recombinantly expressed proteins has gained significant attention due to its potential applications in cancer therapy and gene therapy. Recombinant RB1 proteins can be used to elucidate the molecular mechanisms underlying its tumor-suppressive functions and interactions with other cellular proteins, including E2F transcription factors and cyclins. This research also assists in exploring the biological effects of RB1 in normal and cancerous cells, offering insights into how restoring RB1 function might inhibit tumor growth. Additionally, expressing RB1 in a recombinant system allows for the production of large quantities of the protein, facilitating structural and functional studies necessary for drug development. This has led to an increased interest in developing RB1-based therapeutic strategies, such as gene therapy approaches that aim to restore normal RB1 function in tumors where it is lost or mutated. Overall, the understanding of RB1 through recombinant protein studies is pivotal for advancing cancer treatment modalities and improving patient outcomes.
