Analytical Data
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Gene name
CCSER2
- Application
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Alternative Names
(Coiled-coil serine-rich protein 2)(Protein GCAP14 homolog)
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9H7U1
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Expression Region
231-328aa
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Molecular Weight
16.9 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
CCSER2 (Cysteine-Containing Serine-Rich Protein 2) is a protein of increasing interest in the field of molecular biology due to its potential roles in various cellular functions and disease mechanisms. Initially identified as a component of ribonucleoprotein complexes, CCSER2 is implicated in processes such as RNA metabolism and cellular stress response. Research has shown that it may play a crucial role in maintaining cellular homeostasis and regulating gene expression, which is vital for normal cellular function. Alterations in CCSER2 expression have been observed in several diseases, including cancer, where it may contribute to tumorigenesis and cancer progression. Understanding the structural and functional properties of CCSER2 through recombinant protein studies is essential for elucidating its biological roles and determining its potential as a therapeutic target. Additionally, the reconstitution of CCSER2 in vitro allows for the exploration of its interactions with other cellular components, providing insights into its mechanisms of action and revealing novel pathways that could be exploited for clinical applications. This research could enhance our understanding of the molecular underpinnings of diseases linked to CCSER2 and pave the way for the development of innovative treatments.
