Analytical Data
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Gene name
RALY
- Application
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Alternative Names
RALY;HNRPCL2;P542;RNA-binding Protein Raly
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Species
Human
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Source
E. coli
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Tag
N-6His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UKM9
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Expression Region
1-306aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMSLKLQA SNVTNKNDPK SINSRVFIGN LNTALVKKSD VETIFSKYGR VAGCSVHKGY AFVQYSNERH ARAAVLGENG RVLAGQTLDI NMAGEPKPDR PKGLKRAASA IYSGYIFDYD YYRDDFYDRL FDYRGRLSPV PVPRAVPVKR PRVTVPLVRR VKTNVPVKLF ARSTAVTTSS AKIKLKSSEL QAIKTELTQI KSNIDALLSR LEQIAAEQKA NPDGKKKGDG GGAGGGGGGG GSGGGGSGGG GGGGSSRPPA PQENTTSEAG LPQGEARTRD DGDEEGLLTH SEEELEHSQD TDADDGALQ
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Molecular Weight
34.9 kDa (329aa)
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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
Identification
Protein Description
RALY protein, a member of the ribonucleoprotein family, has garnered significant attention in recent years due to its crucial role in various cellular processes, including RNA metabolism, gene expression regulation, and cellular stress responses. Initially identified for its involvement in splicing and messenger RNA stabilization, RALY has been linked to several essential biological functions that are pivotal in maintaining cellular homeostasis. Aberrations in RALY expression and function have been implicated in diverse pathological conditions, including cancer, neurodegenerative diseases, and autoimmune disorders. Consequently, understanding the molecular mechanisms governing RALY activity and its interactions with RNA and other cellular components is vital for elucidating its potential as a therapeutic target. Research has also focused on the structural dynamics of RALY and its functional domains, revealing insights into how it modulates RNA-protein interactions. These findings contribute to our broader understanding of post-transcriptional regulation and how dysregulation of such processes can lead to disease. As a result, RALY has emerged as a significant focus in molecular biology, with ongoing studies aimed at developing RALY-based interventions that could offer novel strategies for treating diseases associated with its dysfunction.
