Analytical Data
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Gene name
LYAR
- Application
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Alternative Names
Cell growth regulating nucleolar protein; Cell growth-regulating nucleolar protein; Likely ortholog of mouse Ly1 reactive clone ; Ly1 reactive; Ly1 reactive homolog (mouse) ; Ly1 reactive homolog; LYAR; LYAR_HUMAN; ZC2HC2; ZLYAR
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Species
Human
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Source
Yeast
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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
Q9NX58
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Expression Region
1-379aa
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Molecular Weight
45.6 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
LYAR (Lysine-rich nucleolar protein) is a highly conserved protein that plays a significant role in ribosome biogenesis and cellular stress responses. The research into LYAR has intensified due to its involvement in critical cellular processes, including gene regulation, cell proliferation, and apoptosis. Notably, LYAR is implicated in various diseases, particularly cancer, where its expression levels are often altered, suggesting a potential role in tumorigenesis and a possible target for therapeutic interventions. Studies have shown that LYAR interacts with various nucleolar and chromatin-associated proteins, influencing RNA synthesis and ribosome assembly. Additionally, its lysine-rich domain allows for post-translational modifications, which can modulate its function and stability. Understanding the molecular mechanisms governing LYAR's action may pave the way for novel cancer treatments and improve our overall knowledge of nucleolar dynamics. The ongoing research aims to unravel LYAR's exact roles in these cellular processes, the regulation of its expression, and the implications of its dysregulation in disease contexts. Overall, LYAR represents an intriguing subject in molecular biology with potential applications in therapeutic strategies against various pathologies.
