Analytical Data
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Gene name
NMS
- Application
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Alternative Names
NM-S
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Species
Mouse
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q5H8A1
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Expression Region
Leu31~Gln153
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Molecular Weight
45kDa
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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
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Protein Description
Nuclear Matrix Protein 1 (NMS) has emerged as a significant focus in the field of cellular biology due to its involvement in crucial cellular processes such as gene expression, DNA replication, and cell cycle regulation. The nuclear matrix, a complex structure that organizes the nucleus, comprises various proteins, including NMS, which play critical roles in maintaining the integrity and functionality of genetic material. Research has revealed that NMS is implicated in numerous cellular signaling pathways and may influence cancer progression and other diseases characterized by dysregulated cellular functions. Given its central role in maintaining nuclear architecture, scientists are increasingly interested in characterizing NMS and its interactions with other nuclear components. The recombinant expression of NMS offers a powerful tool for studying its biochemical properties and functional mechanisms in detail. By generating recombinant NMS protein, researchers can explore its structural features, post-translational modifications, and interactions with DNA, RNA, and other nuclear proteins. These studies are essential for elucidating the role of NMS in health and disease, potentially leading to novel therapeutic strategies for conditions associated with nuclear matrix dysfunction. Consequently, the investigation of NMS and its recombinant protein forms serves as a valuable avenue for understanding the complexities of nuclear biology, with implications for tumor biology and therapeutic development.
