Analytical Data
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Gene name
U3A/SNRPA
- Application
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Alternative Names
fc19d01; Mud1; small nuclear ribonucleoprotein polypeptide A; snRNP A; snRNP protein A; SNRPA; SNRPA_HUMAN; U1 small nuclear ribonucleoprotein A; U1 small nuclear RNP specific A; U1 snRNP A; U1 snRNP specific protein A; U1-A; U1A; wu:fc19d01; zgc:77810
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P09012
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Expression Region
8-278aa
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Molecular Weight
57 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
U3A/SNRPA, a pivotal RNA-binding protein, plays a critical role in the maturation of pre-mRNA and the assembly of small nuclear ribonucleoproteins (snRNPs). This protein is an essential component of the spliceosome, the complex responsible for pre-mRNA splicing, wherein introns are removed, and exons are joined to form a mature mRNA. Research into U3A/SNRPA has gained momentum due to its significance in gene regulation and its potential implications in various diseases, including cancer. Aberrant splicing processes, often linked to the malfunctioning of spliceosomal components such as U3A/SNRPA, can lead to the production of dysfunctional proteins that disrupt normal cell functions. Studies have shown that mutations or altered expression levels of U3A/SNRPA can influence oncogenic pathways, thereby highlighting its role in tumorigenesis. Additionally, understanding the structural and functional properties of U3A/SNRPA can provide insights into therapeutic strategies aimed at correcting splicing defects. Ongoing research focuses on elucidating the molecular mechanisms by which U3A/SNRPA interacts with RNA and other protein partners, as well as its regulation during cellular stress or development. As the field of RNA biology evolves, U3A/SNRPA remains a compelling target for investigations into novel treatments for diseases characterized by splicing irregularities, offering potential avenues for innovative interventions and improved patient outcomes.
