PRMT1 Human

Protein Arginine Methyltransferase 1 Human Recombinant
Cat. No.
BT12388
Source
Escherichia Coli.
Synonyms

ANM1, HCP1, HRMT1L2, IR1B4, INF receptor 1-bound protein 4, EC 2.1.1, Protein arginine N-methyltransferase 1, PRMT1, HMT2.

Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description

PRMT1 Human Recombinant (a.a. 1-353) fused with His-MBP tag at N-terminus produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 750 amino acids and having a molecular mass of 84 kDa.
The PRMT1 is purified by proprietary chromatographic techniques.

Product Specs

Introduction
PRMT1 is a protein arginine methyltransferase that methylates the guanidino nitrogens of arginine residues. It specifically targets arginine residues within glycine and arginine-rich domains, such as those found in HNRNPA1 and histones. PRMT1 exhibits dual methylation activity, catalyzing both mono- and asymmetric dimethylation. Notably, it methylates SUPT5H and acts as a histone methyltransferase specific for H4. PRMT1 plays a crucial role in oncogenesis, making it a potential therapeutic target for cancer. Its methylation activity positively regulates the IR/IRS-1/PI3K pathway and glucose uptake in skeletal muscle cells. CAF1 has been identified as a regulator of PRMT1-dependent arginine methylation. Additionally, PRMT1 methylates MRE11, thereby influencing the activity of the MRE11-RAD50-NBS1 complex during the intra-S-phase DNA damage checkpoint response. PRMT1 exerts post-translational control over transcriptional activity. While predominantly localized in the cytoplasm, a fraction of PRMT1 is also found in the nucleus.
Description
PRMT1 Human Recombinant, spanning amino acids 1 to 353, is expressed in E.Coli with an N-terminal His-MBP tag. This non-glycosylated polypeptide chain consists of 750 amino acids, resulting in a molecular weight of 84 kDa. Purification is achieved using proprietary chromatographic techniques.
Physical Appearance
Clear, colorless solution that has been sterilized by filtration.
Formulation
The PRMT1 solution is formulated in a buffer consisting of 40mM Tris-HCl (pH 8.0), 100mM NaCl, 4mM MgCl2, 2mM DTT, and 40% glycerol.
Stability
For short-term storage (up to 4 weeks), the PRMT1 solution can be stored at 4°C. For extended storage, it is recommended to freeze the solution at -20°C. To further enhance long-term stability, the addition of a carrier protein (0.1% HSA or BSA) is advised. Repeated freezing and thawing should be avoided.
Purity
The purity of PRMT1 is greater than 90%, as determined by SDS-PAGE analysis.
Unit Definition
One unit of PRMT1 activity is defined as the amount of enzyme required to transfer 1 picomole of methyl group to a synthetic peptide substrate derived from histone H4 in 10 minutes at a temperature of 37°C.
Specific Activity
The specific activity of PRMT1 is 10,000 Units/ml.
Synonyms

ANM1, HCP1, HRMT1L2, IR1B4, INF receptor 1-bound protein 4, EC 2.1.1, Protein arginine N-methyltransferase 1, PRMT1, HMT2.

Source
Escherichia Coli.
Amino Acid Sequence
MHHHHHHMKI EEGKLVIWIN GDKGYNGLAE VGKKFEKDTG IKVTVEHPDK LEEKFPQVAA TGDGPDIIFW AHDRFGGYAQ SGLLAEITPD KAFQDKLYPF TWDAVRYNGK LIAYPIAVEA LSLIYNKDLL PNPPKTWEEI PALDKELKAK GKSALMFNLQ EPYFTWPLIA ADGGYAFKYE NGKYDIKDVG VDNAGAKAGL TFLVDLIKNK HMNADTDYSI AEAAFNKGET AMTINGPWAW SNIDTSKVNY GVTVLPTFKG QPSKPFVGVL SAGINAASPN KELAKEFLEN YLLTDEGLEA VNKDKPLGAV ALKSYEEELA KDPRIAATME NAQKGEIMPN IPQMSAFWYA VRTAVINAAS GRQTVDEALK DAQTNSSSNN NNNNNNNNLG IEGRGSHMAA AEAANCIMEV SCGQAESSEKPNAEDMTSKD YYFDSYAHFG IHEEMLKDEV RTLTYRNSMF HNRHLFKDKV VLDVGSGTGI LCMFAAKAGA RKVIGIECSS ISDYAVKIVK ANKLDHVVTI IKGKVEEVEL PVEKVDIIIS EWMGYCLFYE SMLNTVLYAR DKWLAPDGLI FPDRATLYVT AIEDRQYKDY KIHWWENVYG FDMSCIKDVA IKEPLVDVVD PKQLVTNACL IKEVDIYTVK VEDLTFTSPF CLQVKRNDYV HALVAYFNIE FTRCHKRTGF STSPESPYTH WKQTVFYMED YLTVKTGEEI FGTIGMRPNA KNNRDLDFTI DLDFKGQLCE LSCSTDYRMR.

Product Science Overview

Structure and Function

PRMT1 is a type I methyltransferase that transfers a methyl group from S-adenosylmethionine to the guanidino nitrogens of arginine residues, forming monomethylarginine and asymmetric dimethylarginine . This enzyme is predominantly located in the nucleus and cytoplasm of human cells . PRMT1 is the major arginine methyltransferase in mammals, accounting for more than 85% of the arginine methylation activity .

Biological Roles

PRMT1 is involved in a wide range of cellular processes, including:

  • Transcriptional Regulation: PRMT1 acts as a histone methyltransferase specific for histone H4, which is crucial for chromatin remodeling and gene expression .
  • Cell Signaling: It plays a role in various signaling pathways, including the p38MAPK cascade .
  • RNA Processing: PRMT1 is involved in RNA splicing and processing .
  • DNA Repair: It participates in the DNA damage response, particularly in signal transduction by p53 class mediators .
Interaction and Regulation

PRMT1 interacts with several proteins that regulate its activity. For instance, the antiproliferative protein BTG1 (B-cell translocation gene 1) and hCAF1 (CCR4-associated factor 1) have been shown to modulate PRMT1 activity . These interactions highlight the enzyme’s role in the crosstalk between transcription and RNA processing .

Clinical Significance

Given its involvement in critical cellular processes, dysregulation of PRMT1 has been implicated in various diseases, including cancer. PRMT1’s role in hematopoiesis and tumorigenesis underscores its potential as a therapeutic target .

Recombinant PRMT1

Recombinant PRMT1 is a form of the enzyme produced through recombinant DNA technology, allowing for its use in research and therapeutic applications. This recombinant form retains the enzyme’s functional properties, making it a valuable tool for studying arginine methylation and its biological implications.

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