Analytical Data
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Gene name
CCNY
- Application
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Alternative Names
CCNY；C10orf9；CBCP1；CFP1；Cyclin-Y
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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
Q8ND76
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Expression Region
2-341aa
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AA Sequence
GNTTSCCVS SSPKLRRNAH SRLESYRPDT DLSREDTGCN LQHISDRENI DDLNMEFNPS DHPRASTIFL SKSQTDVREK RKSLFINHHP PGQIARKYSS CSTIFLDDST VSQPNLKYTI KCVALAIYYH IKNRDPDGRM LLDIFDENLH PLSKSEVPPD YDKHNPEQKQ IYRFVRTLFS AAQLTAECAI VTLVYLERLL TYAEIDICPA NWKRIVLGAI LLASKVWDDQ AVWNVDYCQI LKDITVEDMN ELERQFLELL QFNINVPSSV YAKYYFDLRS LAEANNLSFP LEPLSRERAH KLEAISRLCE DKYKDLRRSA RKRSASADNL TLPRWSPAII S
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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
Related Products
Protein Description
The research on recombinant proteins at the City College of New York (CCNY) has evolved as a vital area of study, driven by the burgeoning need for biopharmaceuticals and innovative therapeutic solutions in the biomedical field. Recombinant proteins, which are produced through the expression of genetically engineered DNA in host cells, offer significant advantages, including high specificity, reduced immunogenicity, and the capability to incorporate post-translational modifications similar to those found in natural proteins. CCNY's research focuses on optimizing the expression and purification processes for various recombinant proteins, including enzymes, hormones, and antibodies, which hold therapeutic potential for diseases ranging from cancer to metabolic disorders. The institution's commitment to integrating cutting-edge biotechnological techniques, such as CRISPR and synthetic biology, aims to enhance protein yield and functionality. Moreover, multidisciplinary collaborations within CCNY leverage knowledge from genetics, bioengineering, and biochemistry, contributing to advancements in protein design and application. By exploring diverse expression systems, including bacterial, yeast, and mammalian cells, CCNY researchers strive to establish more efficient and cost-effective methods for protein production, addressing industry demands and paving the way for novel therapeutic strategies. Through this work, CCNY not only contributes to the fundamental understanding of protein biology but also plays a critical role in the development of next-generation biopharmaceuticals, thereby impacting healthcare on a global scale.
