Analytical Data
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Gene name
Nesp1
- Application
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Alternative Names
Nesp1；NEDD8-specific protease 1
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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
Q8NF91
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Expression Region
全长
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AA Sequence
full
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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
Nesp1, or novel extracellular matrix protein 1, has garnered significant interest in biomedical research due to its potential role in various physiological and pathological processes. Initially identified for its involvement in bone development and mineralization, Nesp1 has been shown to regulate cellular activities such as proliferation, differentiation, and matrix deposition. Its unique structural features and expression patterns suggest that it may act as a key player in the extracellular matrix, influencing tissue homeostasis and repair. Recent studies have highlighted Nesp1's interactions with signaling pathways related to bone metabolism, making it a candidate for investigating disorders like osteoporosis and other skeletal conditions. Furthermore, its potential implications in cancer biology and regenerative medicine are also being explored, as the modulation of extracellular matrix components is crucial for tumor progression and tissue regeneration. As a recombinant protein, Nesp1 offers a valuable tool for elucidating its biological functions and therapeutic potential, paving the way for future investigations aimed at leveraging its properties for clinical applications. Understanding Nesp1's mechanisms of action could lead to novel strategies for treating degenerative diseases and enhancing tissue repair, making it a critical focus in protein engineering and regenerative medicine.
