Analytical Data
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Gene name
NRM
- Application
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Alternative Names
NRM; NRM29; UNQ555/PRO1112; Nurim; Nuclear envelope membrane protein; Nuclear rim protein
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8IXM6
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Expression Region
1-262 aa
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AA Sequence
MAPALLLIPAALASFILAFGTGVEFVRFTSLRPLLGGIPESGGPDARQGWLAALQDRSILAPLAWDLGLLLLFVGQHSLMAAERVKAWTSRYFGVLQRSLYVACTALALQLVMRYWEPIPKGPVLWEARAEPWATWVPLLCFVLHVISWLLIFSILLVFDYAELMGLKQVYYHVLGLGEPLALKSPRALRLFSHLRHPVCVELLTVLWVVPTLGTDRLLLAFLLTLYLGLAHGLDQQDLRYLRAQLQRKLHLLSRPQDGEAE
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Molecular Weight
55.8 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
The study of NRM (Nuclear Receptor Modulators) recombinant proteins has gained significant interest in the field of molecular biology and pharmacology due to their essential role in regulating gene expression and cellular functions. NRM, a subclass of nuclear receptors, are pivotal in mediating the effects of various hormones, including steroid hormones, thyroid hormones, and retinoids. Their ability to act as transcription factors means that they influence numerous biological processes, including development, metabolism, and homeostasis. The recombinant production of NRM proteins provides valuable tools for understanding their structural characteristics, functional mechanisms, and interactions with ligands and co-regulators. Advances in recombinant DNA technology, including the use of bacterial, yeast, or mammalian expression systems, have facilitated the generation of functionally active NRM proteins. This allows researchers to investigate their roles in specific signaling pathways and disease contexts, notably in cancer and metabolic disorders. Furthermore, the elucidation of the 3D structures of these proteins through techniques like X-ray crystallography and cryo-electron microscopy has enhanced drug design efforts aimed at modulating their activity. Consequently, the ongoing research on NRM recombinant proteins not only contributes to the fundamental understanding of cellular regulation but also holds promise for the development of novel therapeutics targeting various diseases tied to nuclear receptor dysregulation.











