Analytical Data
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Gene name
NCBP2
- Application
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Alternative Names
NCBP2;CBP20;Nuclear cap-binding Protein subunit 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
P52298
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Expression Region
1-156aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MSGGLLKALR SDSYVELSQY RDQHFRGDNE EQEKLLKKSC TLYVGNLSFY TTEEQIYELF SKSGDIKKII MGLDKMKKTA CGFCFVEYYS RADAENAMRY INGTRLDDRI IRTDWDAGFK EGRQYGRGRS GGQVRDEYRQ DYDAGRGGYG KLAQNQ
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Molecular Weight
20 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
Related Products
Protein Description
NCBP2 (Nuclear Cap Binding Protein 2) is a protein that plays a crucial role in various cellular processes, including RNA metabolism and regulation. It is part of the cap-binding complex, which is essential for the stability and translation of mRNA molecules. The study of NCBP2 has gained significant interest due to its involvement in the regulation of gene expression and its potential link to various diseases, including cancer. Aberrant expression or mutations of NCBP2 can disrupt normal cellular functions, leading to pathological conditions. Recent research has focused on the biochemical characterization of NCBP2 and the effects of its interactions with other cellular proteins and RNA substrates. Understanding the structure and function of NCBP2 is vital for elucidating its role in cellular homeostasis and disease mechanisms. Furthermore, recombinant NCBP2 proteins have become instrumental in advancing our knowledge of its biological functions and therapeutic potential, as they allow for in-depth studies of the protein's activity and interaction networks. Thus, the exploration of recombinant NCBP2 proteins not only enhances our understanding of RNA biology but also paves the way for developing targeted therapies against diseases associated with its dysregulation.
