Analytical Data
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Gene name
RGS5
- Application
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Alternative Names
MST092; MST106; MST129; MSTP032; MSTP092; MSTP106; MSTP129; Regulator of G Protein Signalling 5; Regulator of G-protein signaling 5; RGS 5; RGS5; RGS5_HUMAN
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O15539
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Expression Region
1-181aa
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Molecular Weight
47.9 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
RBBP4 (Retinoblastoma Binding Protein 4) is a crucial protein involved in the regulation of various cellular processes, including cell cycle control, chromatin remodeling, and gene expression. Initially identified as a binding partner of the retinoblastoma tumor suppressor protein, RBBP4 is now recognized for its role in epigenetic regulation and the maintenance of genome stability. The research surrounding RBBP4 has gained momentum due to its potential implications in cancer biology and developmental disorders. Notably, alterations in RBBP4 expression levels have been associated with various malignancies, underscoring its importance as a biomarker and potential therapeutic target. The study of recombinantly produced RBBP4 proteins enables detailed investigations into its structure-function relationships, interaction networks, and the mechanisms by which it exerts its regulatory effects. By utilizing techniques such as X-ray crystallography and nuclear magnetic resonance (NMR), researchers aim to unravel the precise molecular functions of RBBP4 and how its dysregulation contributes to oncogenic processes. Additionally, the functional characterization of RBBP4 through reconstitution experiments in cellular models provides insights into its role in chromatin dynamics and transcriptional regulation. Ultimately, the comprehensive understanding of RBBP4's mechanisms could pave the way for novel therapeutic strategies in targeting its pathways in cancer and other diseases linked to its dysfunction.
