Analytical Data
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Gene name
CCT2
- Application
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Alternative Names
CCT2；Cyclin-T2
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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
P78371-1
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Expression Region
2-535aa
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AA Sequence
ASLSLAPVNIFKAGADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKI LLSSGRDASLMVTNDGATILKNIGVDNPAAKVLVDMSRVQDDEVGDGTTS VTVLAAELLREAESLIAKKIHPQTIIAGWREATKAAREALLSSAVDHGSD EVKFRQDLMNIAGTTLSSKLLTHHKDHFTKLAVEAVLRLKGSGNLEAIHI IKKLGGSLADSYLDEGFLLDKKIGVNQPKRIENAKILIANTGMDTDKIKI FGSRVRVDSTAKVAEIEHAEKEKMKEKVERILKHGINCFINRQLIYNYPE QLFGAAGVMAIEHADFAGVERLALVTGGEIASTFDHPELVKLGSCKLIEE VMIGEDKLIHFSGVALGEACTIVLRGATQQILDEAERSLHDALCVLAQTV KDSRTVYGGGCSEMLMAHAVTQLANRTPGKEAVAMESYAKALRMLPTIIA DNAGYDSADLVAQLRAAHSEGNTTAGLDMREGTIGDMAILGITESFQVKR QVLLSAAEAAEVILRVDNIIKAAPRKRVPDHHPC
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Molecular Weight
73 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
CCT2 (Chaperonin Containing TCP1 Subunit 2) is a vital component of the chaperonin complex, playing a crucial role in the proper folding of nascent polypeptides and maintaining cellular protein homeostasis. Research into CCT2 is primarily focused on its implications in various cellular processes, including protein assembly, stress responses, and cellular differentiation. Dysregulation of CCT2 has been linked to several diseases, including cancer and neurodegenerative disorders, where the accumulation of misfolded proteins leads to cellular dysfunction. The significance of CCT2 in physiological and pathological contexts stimulates interest in its structure and function, as understanding its mechanistic roles could unveil potential therapeutic targets. Furthermore, recombinant CCT2 protein is being produced for structural and functional studies, facilitating insights into its interactions with substrate proteins and other chaperones within the cytosolic environment. These studies employ advanced techniques such as cryo-electron microscopy and X-ray crystallography, aiming to elucidate the conformational changes of CCT2 during substrate processing. Ultimately, the study of recombinant CCT2 not only enhances our understanding of protein folding mechanisms but also contributes to the development of strategies to combat diseases associated with protein misfolding and aggregation.
