Analytical Data
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Gene name
PIH1D1
- Application
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Alternative Names
PIH1D1;NOP17;PIH1 domain-containing Protein 1
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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
Q9NWS0
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Expression Region
1-290aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMANPKLL GMGLSEAEAI GADSARFEEL LLQASKELQQ AQTTRPESTQ IQPQPGFCIK TNSSEGKVFI NICHSPSIPP PADVTEEELL QMLEEDQAGF RIPMSLGEPH AELDAKGQGC TAYDVAVNSD FYRRMQNSDF LRELVITIAR EGLEDKYNLQ LNPEWRMMKN RPFMGSISQQ NIRSEQRPRI QELGDLYTPA PGRAESGPEK PHLNLWLEAP DLLLAEVDLP KLDGALGLSL EIGENRLVMG GPQQLYHLDA YIPLQINSHE SKAAFHRKRK QLMVAMPLLP VPS
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Molecular Weight
35 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
PIH1D1, a member of the PIH family of proteins, has gained significant attention in recent years due to its critical role in cellular processes, particularly in the context of protein folding and the maintenance of proteostasis. Understanding the molecular mechanisms underlying PIH1D1 function is essential, as it is implicated in various cellular pathways related to stress responses and adaptation. Research indicates that PIH1D1 interacts with the Hsp90 chaperone complex, suggesting its involvement in the maturation of client proteins and potential implications in cancers and neurodegenerative diseases. The recombinant expression of PIH1D1 provides valuable insight into its structural and functional properties, allowing researchers to explore its interaction dynamics with other molecular partners. This line of inquiry is vital for deciphering the broader biological roles of PIH1D1, paving the way for potential therapeutic applications. Given the importance of proteostasis in health and disease, elucidating the specific functions and regulatory mechanisms associated with PIH1D1 could ultimately contribute to the development of novel strategies for treating diseases characterized by protein misfolding and aggregation. This research not only enhances our understanding of cellular physiology but also underscores the potential of targeting PIH1D1 in clinical interventions.
