Analytical Data
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Gene name
Sap130
- Application
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Alternative Names
Sap130；Histone deacetylase complex subunit SAP130
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Species
Mouse
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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
Q8BIH0
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Expression Region
845-1057aa
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AA Sequence
PRKQQHVISTEEGDMMETNSTDDEKSAAKSLLVKAEKRKSPPKEYIDEEGVRYVPVRPRPPITLLRHYRNPWKAAYHHFQRYSDVRVKEEKKAMLQEIANQKGVSCRAQGWKVHLCAAQLLQLTNLEHDVYERLTNLQEGIIPKKKAATDDDLHRINELIQGNMQRCKLVMDQISEARDSMLKVLDHKDRVLKLLNKNGTVKKVSKLKRKEKV
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Molecular Weight
26.8 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
Sap130 is a crucial component of the spliceosome, a complex molecular machine responsible for the removal of introns from pre-mRNA in eukaryotic cells. As a part of the SR protein family, Sap130 plays an integral role in regulating alternative splicing, which is vital for generating protein diversity and influencing various cellular processes. Research into the recombinant expression of Sap130 has gained momentum due to its implications in understanding splicing mechanisms and its potential links to various diseases, including cancer and genetic disorders. By producing recombinant Sap130, scientists aim to investigate its structural properties and interactions with other spliceosomal components, which could reveal insights into the intricacies of RNA processing. Moreover, understanding the functional roles of Sap130 at a molecular level can elucidate how disruptions in splicing contribute to disease pathology, thereby offering potential avenues for therapeutic intervention. Given the increasing recognition of alternative splicing as a key regulatory mechanism in gene expression, studies on Sap130 and its functionalities are poised to significantly advance our knowledge in molecular biology, genetics, and disease mechanisms.
