Analytical Data
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Gene name
NPY1R
- Application
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Alternative Names
NPYR; NPYY1
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P25929
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Expression Region
Phe282~Ile384
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Molecular Weight
16kDa
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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 research on NVL (nuclear vesicle-like) recombinant proteins has gained significant attention in the field of molecular biology and biotechnology due to their potential roles in regulating cellular functions and their implications in various diseases. NVL proteins are part of the broader family of nucleocytoplasmic transport proteins, which are crucial for the exchange of molecules between the nucleus and the cytoplasm. Dysregulation of these proteins has been linked to several pathologies, including cancer and neurodegenerative disorders. Understanding the structure and function of NVL proteins can provide insights into their involvement in key cellular processes such as gene expression, cell cycle regulation, and apoptosis. The development of recombinant NVL proteins enables researchers to explore their biochemical properties, interactions with other cellular components, and potential therapeutic applications. Moreover, advancements in protein engineering techniques and structural biology have facilitated the production of these recombinant proteins in vitro, allowing for detailed studies on their functionalities. This research not only contributes to the fundamental understanding of cellular mechanisms but also opens avenues for the design of novel therapeutic strategies targeting diseases associated with NVL protein dysfunction. As a result, the investigation of NVL recombinant proteins represents a promising frontier in biomedical research, with the potential to impact both basic science and clinical applications.
