Analytical Data
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Gene name
RAVER2
- Application
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Alternative Names
RAVER2；KIAA1579；RibonucleoProtein PTB-binding 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
Q9HCJ3
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Expression Region
1-140aa
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AA Sequence
MAAAAGDGGGEGGAGLGSAAGLGPGPGLRGQGPSAEAHEGAPDPMPAALHPEEVAARLQRMQRELSNRRKILVKNLPQDSNCQEVHDLLKDYDLKYCYVDRNKRTAFVTLLNGEQAQNAIQMFHQYSFRGKDLIVQLQPT
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Molecular Weight
17.0 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
RAVER2, or RNA-binding protein RAVER2, is an essential protein involved in the regulation of mRNA splicing and stability. It interacts with various splicing factors and RNA components, playing a crucial role in the post-transcriptional regulation of gene expression. Research has shown that RAVER2 is implicated in various cellular processes, including stress responses and cell proliferation. Abnormalities in RAVER2 function have been associated with several diseases, including cancer, highlighting its potential as a therapeutic target. Understanding the structure and function of RAVER2 through recombinant protein studies can shed light on its mechanisms of action and interactions with other cellular molecules. Advances in recombinant protein techniques, such as cloning, expression, and purification, enable scientists to produce RAVER2 in sufficient quantities for functional assays and structural analyses. By investigating the biochemical properties and binding dynamics of RAVER2, researchers aim to elucidate its role in RNA metabolism and its contribution to disease pathogenesis, laying the groundwork for novel interventions.
