Analytical Data
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Gene name
PFDN1
- Application
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Alternative Names
PDF; PFD1
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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 95% as determined by SDS-PAGE.
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Uniprot
O60925
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Expression Region
Met1~Gln122
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Molecular Weight
18kDa
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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
PFDN1, or Prefoldin-1, is a crucial chaperone protein that plays a significant role in the folding of nascent polypeptides in the cytosol. As an essential component of the prefoldin complex, PFDN1 facilitates the transfer of unfolded proteins to the cytosolic chaperonin TRiC/CCT, which is vital for maintaining cellular proteostasis and ensuring proper protein function. Research into PFDN1 has gained momentum due to its involvement in various cellular processes, including stress responses and cell differentiation. Dysregulation of PFDN1 has been implicated in several diseases, including cancer and neurodegenerative disorders, highlighting its potential as a therapeutic target. Studies have focused on characterizing the structural and functional aspects of recombinant PFDN1 to better understand its interactions with client proteins and other molecular chaperones. By producing recombinant PFDN1 protein, researchers aim to elucidate its mechanisms and potential roles in disease states, ultimately advancing our knowledge of protein folding pathways and contributing to the development of novel therapeutic strategies. Additionally, the availability of recombinant PFDN1 opens avenues for high-throughput screening of compounds that may modulate its function or enhance its chaperoning capabilities, offering further insights into its biological significance. The ongoing exploration of PFDN1 in various biological contexts underscores its relevance in cellular health and disease, paving the way for future studies aimed at harnessing its chaperoning functions for therapeutic benefit.
