Analytical Data
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Gene name
RBL2
- Application
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Alternative Names
130 kDa retinoblastoma-associated protein (p130) (Retinoblastoma-related protein 2) (RBR-2) (pRb2) (RB2)
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q08999
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Expression Region
417-616aa
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Molecular Weight
27.4 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
RBL2, also known as Retinoblastoma-like protein 2, is a critical member of the retinoblastoma family of proteins, which play essential roles in cell cycle regulation and tumor suppression. Research into RBL2 has garnered significant interest due to its involvement in various cellular processes, including differentiation, apoptosis, and responses to DNA damage. Unlike its more famous counterpart, Rb1, which is often studied in the context of retinoblastoma and other cancers, RBL2 has been less characterized, though it is believed to have overlapping functionalities. The protein exhibits a high degree of conservation across species, indicating its fundamental role in maintaining cellular integrity. Studies have demonstrated that RBL2 can interact with numerous transcription factors and other signaling molecules, suggesting it may act as a crucial modulator of gene expression in response to cellular stress and proliferation signals. Furthermore, aberrations in RBL2 expression and function are linked to various malignancies, highlighting its potential as a therapeutic target. Recent advances in recombinant protein technology have enabled researchers to produce RBL2 in sufficient quantities for detailed functional studies, paving the way for further exploration of its biological roles and the mechanisms underlying its tumor-suppressive functions. Understanding RBL2's precise role in cellular processes could provide new insights into cancer biology and lead to the development of innovative strategies for cancer therapy. Thus, the research on RBL2 recombinant proteins not only enhances our molecular comprehension of this vital protein but also signifies its potential clinical relevance.
