Analytical Data
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Gene name
U1A/SNRPA
- Application
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Alternative Names
U1 small nuclear ribonucleoprotein A
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Species
Human
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Source
HEK293
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Tag
C-6*His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P09012
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Expression Region
M1-K282
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AA Sequence
MAVPETRPNHTIYINNLNEKIKKDELKKSLYAIFSQFGQILDILVSRSLKMRGQAFVIFKEVSSATNALRSMQGFPFYDKPMRIQYAKTDSDIIAKMKGTFVERDRKREKRKPKSQETPATKKAVQGGGATPVVGAVQGPVPGMPPMTQAPRIMHHMPGQPPYMPPPGMIPPPGLAPGQIPPGAMPPQQLMPGQMPPAQPLSENPPNHILFLTNLPEETNELMLSMLFNQFPGFKEVRLVPGRHDIAFVEFDNEVQAGAARDALQGFKITQNNAMKISFAKK
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Protein Length
Full Length
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Molecular Weight
35-40 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
U1A and SNRPA are essential proteins involved in the regulation of alternative splicing and the assembly of spliceosomal complexes in eukaryotic cells. U1A is a component of the U1 small nuclear ribonucleoprotein (snRNP), which plays a crucial role in the recognition of 5' splice sites during pre-mRNA splicing, ensuring the accurate removal of introns. SNRPA, on the other hand, is part of the U2 snRNP, performing similar regulatory roles but primarily interacting with branch points and aiding in the selection of intron-exon boundaries. The study of U1A/SNRPA recombinant proteins is significant for understanding the molecular mechanisms underlying splicing regulation and its implications for gene expression diversity. Aberrations in splicing mechanisms are often associated with various diseases, including cancer and genetic disorders, making these proteins also critical targets for therapeutic interventions. In addition, their interactions and modifications can serve as potential biomarkers for disease progression. By investigating the structural and functional characteristics of U1A/SNRPA recombinant proteins, researchers aim to elucidate their specific roles in spliceosomal function and to explore their potential applications in biotechnology and medicine. Understanding how U1A and SNRPA interact with RNA and each other could provide insights into the complexity of splicing mechanisms and contribute to the development of novel strategies for the manipulation of gene expression. Thus, the research on U1A and SNRPA not only enriches our fundamental knowledge of molecular biology but also opens avenues for therapeutic innovations targeting splicing dysregulation.
