Analytical Data
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Gene name
CCSER2
- Application
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Alternative Names
CCSER2；FAM190B；KIAA1128；Serine-rich coiled-coil domain-containing Protein 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
Q9H7U1
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Expression Region
231-328aa
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AA Sequence
SFLPPSSITRSHSFNRAVDLTKPYQNQQLSIRVPLRSSMLTRNSRQPEVLNGNEHLGYGFNRPYAAGGKKLALPNGPGVTSTLGYRMVHPSLLKSSRS
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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, or Coiled-Coil-Structure-Enhancer Protein 2, is a crucial protein that has garnered attention due to its potential roles in various biological processes, including cell signaling, proliferation, and apoptosis. Research into CCSER2 has expanded significantly as it is implicated in several diseases, particularly cancers, where its expression levels can influence tumor progression and patient prognosis. Understanding the structure and function of CCSER2 at the molecular level is essential for elucidating its biological roles and developing targeted therapies. Recent advances in recombinant protein technology have enabled researchers to produce and purify CCSER2, facilitating detailed investigations into its interactions with other proteins and cellular components. Studies using recombinant CCSER2 have revealed insights into its structural properties, functional domains, and involvement in cellular pathways, paving the way for novel therapeutic strategies. As ongoing research continues to explore the multifaceted roles of CCSER2, this protein stands out as a promising subject for both basic science and clinical applications, potentially leading to breakthroughs in the treatment of diseases where CCSER2 is a critical player.
