WDR77 Protein, Human (His-SUMO)

WDR77 is a non-catalytic component of the methylosome complex with PRMT5 and CLNS1A and regulates arginine to dimethylarginine in spliceosomal Sm proteins and histones. This modification directs Sm proteins to SMN complexes, helping them assemble into small nuclear ribonucleoprotein core particles. WDR77 Protein, Human (His-SUMO) is the recombinant human-derived WDR77 protein, expressed by E. coli , with N-His, N-SUMO labeled tag. The total length of WDR77 Protein, Human (His-SUMO) is 312 a.a., with molecular weight of ~49.6 kDa.

WDR77 functions as a non-catalytic component within the methylosome complex, alongside PRMT5 and CLNS1A, orchestrating the modification of specific arginines to dimethylarginines in spliceosomal Sm proteins and histones. This modification directs Sm proteins to the survival of motor neurons (SMN) complex, facilitating their assembly into small nuclear ribonucleoprotein core particles. Beyond its role in RNA processing, WDR77 may play a part in transcription regulation. The methylosome complex extends its methylating activity to Piwi proteins (PIWIL1, PIWIL2, and PIWIL4), essential for their interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage. WDR77 engages in a complex interplay with other components such as PRMT1, ERH, and CLNS1A, with specific interactions observed with PRMT5, various Sm proteins, SUZ12, histone H2A, CTDP1, LSM11, APEX1, AR, NKX3-1, CHTOP, FAM47E, and TSC22D2. Its intricate network of interactions underscores WDR77's multifaceted involvement in epigenetic modifications and regulatory pathways.

Human

E. coli

N-His;N-SUMO

Q9BQA1 (1M-312L)

79084  [NCBI]

MRKETPPPLVPPAAREWNLPPNAPACMERQLEAARYRSDGALLLGASSLSGRCWAGSLWLFKDPCAAPNEGFCSAGVQTEAGVADLTWVGERGILVASDSGAVELWELDENETLIVSKFCKYEHDDIVSTVSVLSSGTQAVSGSKDICIKVWDLAQQVVLSSYRAHAAQVTCVAASPHKDSVFLSCSEDNRILLWDTRCPKPASQIGCSAPGYLPTSLAWHPQQSEVFVFGDENGTVSLVDTKSTSCVLSSAVHSQCVTGLVFSPHSVPFLASLSEDCSLAVLDSSLSELFRSQAHRDFVRDATWSPLNHSL

Approximately 49.6 kDa

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

<1 EU/μg, determined by LAL method.