Analytical Data
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Gene name
PREB
- Application
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Alternative Names
Mammalian guanine nucleotide exchange factor mSec12
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Species
Human
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9HCU5
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Expression Region
1-388aa
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Molecular Weight
49.8 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
PREB (Proline-rich protein EBR) is a newly identified protein that plays a significant role in various biological processes, including cell signaling, protein-protein interactions, and cellular metabolism. Research on PREB has gained momentum due to its potential implications in diseases such as cancer and metabolic disorders. The protein’s unique structure, characterized by proline-rich regions, allows it to engage in multiple interactions within the cellular environment, influencing diverse pathways. As a result, understanding the functional properties and mechanisms of PREB is crucial for elucidating its role in health and disease. Recent studies have focused on the recombinant expression of PREB to investigate its functions in vitro and in vivo. By producing PREB in a controlled laboratory setting, researchers can examine its interactions with other proteins, assess its stability, and explore its potential as a therapeutic target. Additionally, the manipulation of PREB expression levels could pave the way for innovative strategies in drug development and targeted therapies. With the rapid advancements in biotechnology and molecular biology, the elucidation of PREB's structure-function relationship will not only enhance our understanding of its biological significance but also contribute to the identification of novel biomarkers and therapeutic approaches for diseases linked to its dysregulation. The ongoing research into PREB holds promise for unveiling new insights into cellular mechanisms and the potential for developing transformative medical interventions.
