Analytical Data
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Gene name
UQCC
- Application
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Alternative Names
UQCC1; BZFB; C20orf44; UQCC; Ubiquinol-cytochrome-c reductase complex assembly factor 1; Basic FGF-repressed Zic-binding Protein; bFGF-repressed Zic-binding Protein; bFZb; Ubiquinol-cytochrome c reductase complex chaperone CBP3 homolog
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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
Q9NVA1
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Expression Region
1-299 aa
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AA Sequence
MALLVRVLRN QTSISQWVPV CSRLIPVSPT QGQGDRALSR TSQWPQMSQS RACGGSEQIP GIDIQLNRKY HTTRKLSTTK DSPQPVEEKV GAFTKIIEAM GFTGPLKYSK WKIKIAALRM YTSCVEKTDF EEFFLRCQMP DTFNSWFLIT LLHVWMCLVR MKQEGRSGKY MCRIIVHFMW EDVQQRGRVM GVNPYILKKN MILMTNHFYA AILGYDEGIL SDDHGLAAAL WRTFFNRKCE DPRHLELLVE YVRKQIQYLD SMNGEDLLLT GEVSWRPLVE KNPQSILKPH SPTYNDEGL
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Molecular Weight
34.6 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
UQCC (Ubiquitin-Associated Protein Co-Chaperone) is a protein complex that plays a crucial role in maintaining cellular homeostasis by regulating protein folding and degradation processes. Research on UQCC has gained prominence due to its involvement in various cellular pathways, including those related to stress responses and proteostasis. Disruption in UQCC functions has been implicated in numerous diseases, including cancer and neurodegenerative disorders, highlighting its potential as a therapeutic target. The study of recombinant UQCC proteins allows for detailed investigations into their molecular mechanisms, interaction partners, and functional roles within the cell. By expressing UQCC proteins in various expression systems, researchers aim to elucidate their structure-function relationships and examine how they contribute to maintaining cellular protein quality control. This research is essential for understanding the biochemical underpinnings of diseases associated with protein misfolding and degradation, ultimately paving the way for the development of novel therapeutic strategies. Additionally, the advanced techniques employed in protein engineering and expression, such as CRISPR and advanced purification methods, provide researchers with the tools necessary to dissect the complex interactions and pathways that UQCC regulates. As the field evolves, understanding UQCC's role in cellular functions and disease mechanisms is becoming increasingly vital, offering insights that could lead to groundbreaking discoveries in protein pathology and potential interventions.
