Analytical Data
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Gene name
RCP9
- Application
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Alternative Names
Calcitonin gene related peptide receptor component; Calcitonin gene related peptide receptor component protein; Calcitonin gene-related peptide-receptor component protein; CGRP receptor component protein; CGRP-RCP; CGRP-receptor component protein; CGRPRCP; CRCP; DNA-directed RNA polymerase III subunit RPC9; HsC17; RCP; RCP9 ; RNA polymerase III subunit C9; RPC9_HUMAN
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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
O75575
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Expression Region
1-148 aa
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AA Sequence
MEVKDANSAL LSNYEVFQLL TDLKEQRKES GKNKHSSGQQ NLNTITYETL KYISKTPCRH QSPEIVREFL TALKSHKLTK AEKLQLLNHR PVTAVEIQLM VEESEERLTE EQIEALLHTV TSILPAEPEA EQKKNTNSNV AMDEEDPA
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Molecular Weight
16.8 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
RCP9, or Regulator of Chaperone Protein 9, has emerged as a significant protein of interest in the field of molecular biology and biochemistry due to its potential role in cellular stress responses and protein homeostasis. The study of RCP9 is particularly relevant in the context of diseases characterized by protein misfolding and aggregation, such as neurodegenerative disorders. Researchers have discovered that RCP9 interacts with various molecular chaperones, facilitating protein folding and preventing aggregation under stress conditions. This interaction underscores its critical role in maintaining cellular function during proteotoxic stress. Investigating RCP9 not only enhances our understanding of fundamental cellular processes but also opens new avenues for therapeutic interventions in diseases linked to protein misfolding. Moreover, advancements in recombinant protein technology have enabled researchers to produce RCP9 in vitro, allowing for detailed studies of its structure, function, and interaction with other proteins. As such, RCP9 stands as a promising target for developing novel strategies to combat proteotoxicity and improve cellular resilience, making it an appealing candidate for further research within the biomedical field.
