Analytical Data
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Gene name
SNRNP70
- Application
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Alternative Names
SNRNP70；RNPU1Z；RPU1；SNRP70；U1 small nuclear ribonucleoProtein 70 kDa
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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
P08621
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Expression Region
1-210aa
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AA Sequence
MTQFLPPNLLALFAPRDPIPYLPPLEKLPHEKHHNQPYCGIAPYIREFEDPRDAPPPTRAETREERMERKRREKIERRQQEVETELKMWDPHNDPNAQGDAFKTLFVARVNYDTTESKLRREFEVYGPIKRIHMVYSKRSGKPRGYAFIEYEHERDMHSAYKHADGKKIDGRRVLVDVERGRTVKGWRPRRLGGGLGGTRRGGADVNIRH
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Molecular Weight
28.7 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
SNRNP70 is a vital component of the spliceosomal machinery, playing a key role in pre-mRNA splicing by forming part of the U1 small nuclear ribonucleoprotein (snRNP) complex. This protein is crucial for the recognition of 5' splice sites in intron-containing pre-mRNAs, facilitating their excision and the subsequent ligation of exons. Research on SNRNP70 has gained momentum due to its implications in various cellular processes and its potential links to disease. Abnormalities in splicing are associated with a range of disorders, including cancer and neurodegenerative diseases, making SNRNP70 a significant focus for understanding the mechanistic underpinnings of such conditions. Furthermore, the study of SNRNP70 and its interactions with other spliceosomal proteins can unveil the intricate regulatory networks governing gene expression. Recombinant production of SNRNP70 allows for detailed structural and functional analyses, providing insights into splicing dynamics and the development of therapeutic strategies targeting splicing-related diseases. Overall, the investigation of SNRNP70 is crucial for advancing our understanding of gene regulation and its consequences on human health.
