Analytical Data
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Gene name
NDN
- Application
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Alternative Names
NDN；Necdin
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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
Q99608
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Expression Region
1-321aa
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AA Sequence
MSEQSKDLSD PNFAAEAPNS EVHSSPGVSE GVPPSATLAE PQSPPLGPTA APQAAPPPQA PNDEGDPKAL QQAAEEGRAH QAPSAAQPGP APPAPAQLVQ KAHELMWYVL VKDQKKMIIW FPDMVKDVIG SYKKWCRSIL RRTSLILARV FGLHLRLTSL HTMEFALVKA LEPEELDRVA LSNRMPMTGL LLMILSLIYV KGRGARESAV WNVLRILGLR PWKKHSTFGD VRKLITEEFV QMNYLKYQRV PYVEPPEYEF FWGSRASREI TKMQIMEFLA RVFKKDPQAW PSRYREALEE ARALREANPT AHYPRSSVSE D
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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 study of recombinant proteins, particularly those derived from Nucleic Acid-Driven Networks (NDN), has gained significant attention in biotechnology and molecular biology. NDNs are complex networks of nucleic acids that play critical roles in cellular processes and can be engineered to express specific recombinant proteins. With the advancement of molecular cloning techniques and expression systems, the production of these proteins has become more efficient and scalable, enabling researchers to explore their functions, interactions, and potential therapeutic applications. The significance of NDN recombinant proteins extends to various fields, including vaccine development, diagnostic tools, and enzyme engineering. Additionally, the ability to customize protein structures and functions through genetic engineering has opened new avenues for innovative treatments and synthetic biology applications. As the demand for high-quality recombinant proteins increases, understanding the underlying mechanisms of NDNs and optimizing their expression continues to be a pivotal area of research, paving the way for breakthroughs in medicine and biotechnology.
