PRMT5 Protein, Human (HEK293, His-Flag)

PRMT5 protein, an enzyme from the methyltransferase family, methylates arginine in target proteins like histones, p53, and transcription factors. It regulates transcription and small nuclear ribonucleoprotein assembly. Alternative splicing generates diverse PRMT5 transcript variants. It is widely expressed, particularly in the thyroid, ovary, and other tissues, emphasizing its crucial role in cellular processes. PRMT5 Protein, Human (HEK293, His-Flag) is the recombinant human-derived PRMT5, expressed by HEK293, with N-Flag, C-His labeled tag.

PRMT5 encodes an enzyme belonging to the methyltransferase family, responsible for catalyzing the transfer of methyl groups to the amino acid arginine in various target proteins, such as histones, transcriptional elongation factors, and the tumor suppressor p53. The gene plays a crucial role in diverse cellular processes, including transcriptional regulation and the assembly of small nuclear ribonucleoproteins. Additionally, alternative splicing events give rise to multiple transcript variants, contributing to the functional diversity of PRMT5. This enzyme exhibits ubiquitous expression across various tissues, with notable presence in the thyroid, ovary, and numerous other tissues, underscoring its importance in fundamental cellular functions.

Human

HEK293

N-Flag;C-His

NP_006100.2 (A2-L637)

10419  [NCBI]

Full Length of Mature Protein

AMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFIQEPAKNRPGPQTRSDLLLSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPEDLRDDIIENAPTTHTEEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNKKGFPVLSKMHQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPLQPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNVQVLMVLGAGRGPLVNASLRAAKQADRRIKLYAVEKNPNAVVTLENWQFEEWGSQVTVVSSDMREWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFLAPISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFAGYFETVLYQDITLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICVRFWRCSNSKKVWYEWAVTAPVCSAIHNPTGRSYTIGL

Approximately 65 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation .

≥ 90%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.