Analytical Data
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Gene name
NE
- Application
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Alternative Names
NE；LEM 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
P01583
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Expression Region
113-271aa
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AA Sequence
SAPFSFLSNV KYNFMRIIKY EFILNDALNQ SIIRANDQYL TAAALHNLDE AVKFDMGAYK SSKDDAKITV ILRISKTQLY VTAQDEDQPV LLKEMPEIPK TITGSETNLL FFWETHGTKN YFTSVAHPNL FIATKQDYWV CLAGGPPSIT DFQILENQA
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Molecular Weight
18.0 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
NE (Nuclear Envelope) recombinant proteins have garnered significant attention in molecular and cellular biology due to their essential roles in cell structure and function. The nuclear envelope is a double membrane structure that encloses the nucleus, serving as a barrier that regulates the exchange of substances between the nucleus and cytoplasm, while also maintaining genome integrity. Understanding NE composition, including integral membrane proteins and peripheral proteins, is crucial for elucidating various cellular processes such as gene expression, cell cycle regulation, and apoptosis. Advances in recombinant DNA technology have enabled the production of NE proteins in heterologous systems, facilitating detailed studies of their biochemical properties and interactions. This research is vital not only for understanding fundamental cellular mechanisms but also for investigating disease states, such as cancer and neurodegenerative disorders, where nuclear envelope integrity is compromised. Additionally, the study of NE proteins can lead to novel therapeutic strategies aimed at restoring normal cellular function or developing targeted drug delivery systems. The integration of structural biology techniques and high-throughput screening has further accelerated the discovery of NE protein functions, making this area of research a dynamic and promising field. Through the synthesis and characterization of NE recombinant proteins, scientists aim to unravel the complexities of nuclear dynamics and their implications in health and disease.
