Analytical Data
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Gene name
sip
- Application
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Alternative Names
sip；KIAA0569；SIP1；ZFHX1B；Zinc finger E-box-binding homeobox 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
Q9EU98
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Expression Region
26-434aa
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AA Sequence
QETDTTWTARTVSEVKADLVKQDNKSSYTVKYGDTLSVISEAMSIDMNVLAKINNIADINLIYPETTLTVTYDQKSHTATSMKIETPATNAAGQTTATVDLKTNQVFVADQKVSLNTISEGMTPEAATTIVSPMKTYSSAPALKSKEVLAQEQAVSQVAANEQVSPAPVKSITSEVPAAKEEVKPTQTSVSQLTTVSPASVAAETPAPVAKVAPVRTVAAPRVASAKVVTPKVETGASPEHVSAPAVPVTTTSPATDSKLQATEVKSVPVAQKAPTATPVAQPASTTNAVAAHPENAGLQPHVAAYKEKVASTYGVNEFSTYRAGDPGDHGKGLAVDFIVGKNQALGNEVAQYSTQNMAANNISYVIWQQKFYSNTNSIYGPANTWNAMPDRGGVTANHYDHVHVSFNK
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Molecular Weight
50.5 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
SIP (SIP isomerization protein) is a pivotal component in the study of protein folding and structural dynamics, crucial for understanding various physiological processes. In recent years, research has increasingly focused on the role of SIP in cellular functions, particularly in relation to stress responses and the maintenance of protein homeostasis. Protein misfolding and aggregation are linked to numerous diseases, including neurodegenerative disorders like Alzheimer's and Parkinson's diseases. By investigating SIP's mechanism of action, researchers aim to elucidate how it influences protein conformation, stability, and interactions under different cellular conditions. The exploration of SIP's role in protein quality control also opens potential therapeutic avenues for tackling diseases caused by misfolded proteins. This research not only enhances our fundamental understanding of protein biology but also emphasizes the significance of SIP in potential clinical applications, including the development of drugs that target protein misfolding pathways. As protein engineering and synthetic biology evolve, elucidating the functions and mechanisms of SIP is becoming increasingly relevant, suggesting promising directions for future studies in biomedical research and therapeutic interventions.
