Analytical Data
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Gene name
NMP4
- Application
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Alternative Names
ZNF384; CAGH1A; CIZ; NMP4; NP; TNRC1; Zinc Finger Protein 384; Trinucleotide Repeat Containing 1; Nuclear Matrix Transcription Factor 4; CAG repeat protein 1
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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 90% as determined by SDS-PAGE.
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Uniprot
Q8TF68
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Expression Region
Ser307~Pro540
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Molecular Weight
33kDa
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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
NMP4, or Nuclear Matrix Protein 4, has garnered significant attention in recent years due to its pivotal role in cellular processes such as gene expression, DNA replication, and cell differentiation. Its association with the nuclear matrix suggests that NMP4 is integral to maintaining the structural integrity of the nucleus, which in turn influences how genetic material is organized and expressed. Various studies have indicated that NMP4 may have implications in tumorigenesis, as alterations in its expression levels have been observed in various cancer cells, hinting at its potential function as a tumor suppressor or oncogene depending on the cellular context. Additionally, understanding the molecular mechanisms underlying NMP4's action may provide insights into its involvement in diseases characterized by deregulated cell growth and proliferation. Consequently, the recombinant expression and characterization of NMP4 are crucial for elucidating its functionalities, interactions with other nuclear proteins, and its overall contribution to cellular homeostasis. Investigating the properties of recombinant NMP4 can also pave the way for developing therapeutic strategies targeting its pathways, offering potential advancements in cancer treatment and regenerative medicine. Overall, research on NMP4 not only deepens our understanding of nuclear dynamics but also highlights the importance of nuclear architecture in health and disease.
