Analytical Data
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Gene name
SERF2
- Application
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Alternative Names
SERF2;FAM2C;Small EDRK-rich factor 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
P84101
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Expression Region
1-59aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMTRGNQRELARQKNMKKQSDSVKGKRR DDGLSAAARKQRDSEIMQQKQKKANEKKEEPK
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Molecular Weight
9 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
SERF2 (Small Expressed Protein 2) is a member of the SERF family, known for its role in regulating cellular processes related to protein folding and stress responses. Recent research has highlighted its significance in the modulation of cellular homeostasis, particularly under stress conditions such as oxidative stress and heat shock. SERF2 is implicated in various physiological functions, including the regulation of molecular chaperones and enhancers, thereby influencing protein quality control mechanisms. Its association with neurodegenerative diseases, cancer, and other pathologies underscores the importance of understanding SERF2's functional dynamics. The recombinant expression of SERF2 in various model systems has enabled researchers to dissect its roles at a molecular level, facilitating investigations into its interaction partners and downstream signaling pathways. The study of SERF2 as a recombinant protein is crucial for elucidating its structure-function relationships, providing insights that may lead to novel therapeutic strategies that harness its protective roles in cellular stress responses. Given the increasing interest in targeted therapies and protein-based agents in biomedical research, SERF2 emerges as a promising candidate for further exploration, potentially offering avenues for intervention in diseases characterized by protein misfolding and cellular dysregulation.
