Analytical Data
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Gene name
NHP2
- Application
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Alternative Names
NHP2;NOLA2;H/ACA ribonucleoProtein complex subunit 2
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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
Q9NX24
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Expression Region
1-153aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMTKIKADPDGPEAQAEACSGERTYQELLVN QNPIAQPLASRRLTRKLYKCIKKAVKQKQIRRGVKEVQKFVNKGEKGIMV LAGDTLPIEVYCHLPVMCEDRNLPYVYIPSKTDLGAAAGSKRPTCVIMVK PHEEYQEAYDECLEEVQSLPLPL
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Molecular Weight
19 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
NHP2, or Nuclear Histone Protein 2, is a critical component involved in various cellular processes, particularly in the assembly and maintenance of the ribonucleoprotein complexes essential for RNA biogenesis and processing. Research into NHP2 has garnered attention due to its essential role in the biogenesis of the telomerase complex, which maintains telomere integrity and function in eukaryotic cells. Dysfunctional telomeres are implicated in aging and various diseases, including cancer. The study of NHP2 recombinant proteins has become increasingly relevant as scientists seek to understand its structural and functional properties. By producing NHP2 in a recombinant form, researchers can investigate its interactions with other telomeric proteins and RNA components, providing insights into the molecular mechanisms governing telomere maintenance and RNA metabolism. Additionally, characterizing the structural features of NHP2 through techniques such as X-ray crystallography and nuclear magnetic resonance (NMR) can aid in identifying potential therapeutic targets for diseases associated with telomere dysfunction. Overall, the exploration of NHP2 and its recombinant protein forms not only enhances our understanding of fundamental biological processes but also opens avenues for innovative approaches in cancer therapy and regenerative medicine.
