Analytical Data
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Gene name
PFDN2
- Application
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Alternative Names
PFDN2;PFD2;Prefoldin subunit 2
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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
Q9UHV9
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Expression Region
1-154aa
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AA Sequence
MAENSGRAGK SSGSGAGKGA VSAEQVIAGF NRLRQEQRGL ASKAAELEME LNEHSLVIDT LKEVDETRKC YRMVGGVLVE RTVKEVLPAL ENNKEQIQKI IETLTQQLQA KGKELNEFRE KHNIRLMGED EKPAAKENSE GAGAKASSAG VLVS
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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
PFDN2, or Prefoldin 2, is a member of the Prefoldin family, which plays a crucial role in protein folding and assembly in eukaryotic cells. This multi-subunit protein complex is involved in the transport and proper folding of cytosolic proteins, particularly those that are critical for cellular functions, such as enzymes and structural proteins. Research has shown that PFDN2 is essential for the stabilization of newly synthesized polypeptides, preventing their aggregation and facilitating their interaction with chaperones. Dysregulation of PFDN2 has been linked to various diseases, including cancer and neurodegenerative disorders, making it a significant focus of investigation in biomedical research. The study of recombinant PFDN2 proteins allows researchers to explore the structural and functional characteristics of this protein, leading to a better understanding of its mechanisms. Furthermore, recombinant PFDN2 can be utilized in various applications, including drug discovery and therapeutic development, particularly in the context of diseases where protein misfolding plays a critical role. With advancements in recombinant DNA technology and protein expression systems, the production of PFDN2 in vitro has become more feasible, enabling detailed biochemical and biophysical studies. This has the potential to reveal novel insights into protein quality control mechanisms and pave the way for targeted therapies aimed at restoring proper protein function in disease contexts. The ongoing research on PFDN2 not only emphasizes its biological importance but also highlights its potential as a therapeutic target and a model for understanding protein folding disorders.
