TRA2B Protein, Human (Baculovirus, His-Myc)

The TRA2B protein is a sequence-specific RNA-binding factor that complexly regulates pre-mRNA splicing and modulates exon inclusion. It cooperates with RBMX to promote the inclusion of exon 7 in SMN2, demonstrating diverse regulatory functions. TRA2B Protein, Human (Baculovirus, His-Myc) is the recombinant human-derived TRA2B protein, expressed by Sf9 insect cells , with N-10*His, C-Myc labeled tag. The total length of TRA2B Protein, Human (Baculovirus, His-Myc) is 287 a.a., with molecular weight of ~37.6 kDa.

TRA2B protein, a sequence-specific RNA-binding factor, intricately modulates pre-mRNA splicing, exhibiting the capability to either activate or suppress exon inclusion. In collaboration with RBMX, it plays a pivotal role in promoting exon 7 inclusion of the survival motor neuron SMN2, showcasing its diverse regulatory functions. Additionally, TRA2B takes part in the splicing of MAPT/Tau exon 10, showcasing its involvement in shaping pre-mRNA splicing patterns. By counteracting the effects of splicing regulators like RBMX and binding to the AG-rich SE2 domain in SMN exon 7 RNA, TRA2B exerts a nuanced influence on RNA processing. It is an integral part of a pre-mRNA exonic splicing enhancer (ESE) complex, alongside TRA2B/SFRS10, SNRNP70, SNRPA1, and SRRM1. Further interactions with A3 enhancer proteins SFRS4, SFRS5, SFRS6, and SFRS9, as well as binding to CPSF6, RBMY1A1, RBMX, RNPS1, and phosphorylated SFRS13A, underscore the intricate network through which TRA2B modulates splicing. Its interactions with SAFB/SAFB1, ILDR1, and ILDR2 further contribute to the multifaceted regulatory landscape of TRA2B in RNA processing.

Human

Sf9 insect cells

N-10*His;C-Myc

P62995 (S2-Y288)

6434  [NCBI]

SDSGEQNYGERESRSASRSGSAHGSGKSARHTPARSRSKEDSRRSRSKSRSRSESRSRSRRSSRRHYTRSRSRSRSHRRSRSRSYSRDYRRRHSHSHSPMSTRRRHVGNRANPDPNCCLGVFGLSLYTTERDLREVFSKYGPIADVSIVYDQQSRRSRGFAFVYFENVDDAKEAKERANGMELDGRRIRVDFSITKRPHTPTPGIYMGRPTYGSSRRRDYYDRGYDRGYDDRDYYSRSYRGGGGGGGGWRAAQDRDQIYRRRSPSPYYSRGGYRSRSRSRSYSPRRY

Approximately 37.6 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.