Analytical Data
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Gene name
NOLA2
- Application
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Alternative Names
DKCB2; FLJ20479; H/ACA ribonucleoprotein complex subunit 2; NHP2; NHP2 like protein; NHP2 ribonucleoprotein; NHP2 ribonucleoprotein homolog (yeast) 1; NHP2 ribonucleoprotein homolog; NHP2; S. cerevisiae; homolog of; NHP2_HUMAN; NHP2P; NOLA2; Nucleolar protein family A member 2 (H/ACA small nucleolar RNPs); Nucleolar protein family A member 2; snoRNP protein NHP2
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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
1-153 aa
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AA Sequence
MTKIKADPDG PEAQAEACSG ERTYQELLVN QNPIAQPLAS RRLTRKLYKC IKKAVKQKQI RRGVKEVQKF VNKGEKGIMV LAGDTLPIEV YCHLPVMCED RNLPYVYIPS KTDLGAAAGS KRPTCVIMVK PHEEYQEAYD ECLEEVQSLP LPL
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Molecular Weight
17.2 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
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Protein Description
NOLA2, a member of the nucleolar protein family, plays a crucial role in ribosome biogenesis and has been implicated in various cellular processes, including cell growth and response to stress. Its importance in maintaining cellular homeostasis and its potential involvement in disease mechanisms, particularly cancer, have led to increased interest in understanding its structure and function. Recent studies have suggested that NOLA2 interacts with other nucleolar proteins and RNA, contributing to the regulation of ribosomal RNA (rRNA) processing and assembly. Given its pivotal role in nucleolar function, researchers have focused on the recombinant production of NOLA2 to elucidate its biochemical properties, interactions, and regulatory mechanisms. This approach allows for detailed characterization of the protein, enabling the exploration of its function in cellular systems and its potential as a therapeutic target. The characterization of NOLA2 through recombinant techniques may also shed light on its role in translational control and its contributions to the pathogenesis of ribosomopathies and other diseases linked to nucleolar dysfunction. As research progresses, understanding NOLA2's structure-function relationship could provide insights into its biological significance and open new avenues for therapeutic intervention.
