Name :
Recombinant Human PRMT3 Protein (GST Tag)
Biological Activity :
Background :
Protein arginine methyltransferase 3, also known as PRMT3, is one of four type I protein arginine methyltransferases (PRMT) that in humans is encoded by the PRMT3 gene. Methylation of arginine residues is a widespread post-translational modification of proteins catalyzed by a small family of PRMTs. The modification appears to regulate protein functions and interactions that affect gene regulation, signalling and subcellular localization of proteins and nucleic acids. In human cells, the PRMT family consists of eight canonical members. PRMTs have been classified into two groups based on the end product. Certain PRMTs display different subcellular localization in different cell types, implicating cell- and tissue-specific mechanisms for regulating PRMT functions. PRMT3 is unique in that its N-terminus harbours a C2H2 zinc-finger domain that is proposed to confer substrate specificity. Besides, PRMT3 is the only type I enzyme that is restricted to the cytoplasm. A large proportion of this cystosolic PRMT3 is found associated with ribosomes. It is tethered to the ribosomes through its interaction with rpS2, which is also its substrate.
Biological Activity :
Testing in progress
Expression Host :
Human
Source :
E. coli
Tag :
Protein Accession No. :
NP_005779.1
NCBI Gene ID :
Synonyms :
Synonyms :
protein arginine methyltransferase 3
Amino Acid Sequence :
Molecular Weight :
The recombinant human PRMT3/GST chimera consists of 754 amino acids and predicts a molecular mass of 85.7 kDa. It migrates as an approxiamtely 65 kDa band in SDS-PAGE under reducing conditions.
Purity :
> 65 % as determined by SDS-PAGE
State of Matter :
Product Concentration :
Storage and Stability :
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.
Endotoxin Level :
Please contact us for more information.
Protein Construction :
A DNA sequence encoding the human PRMT3 (NP_005779.1) (Cys 2-Gln 531) was fused with the GST tag at the N-terminus.
Buffer Solution :
Lyophilized from sterile 20mM Tris, 150mM NaCl, 0.5mM GSH, pH 7.0Please contact us for any concerns or special requirements. Normally 5 % – 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. Please refer to the specific buffer information in the hardcopy of datasheet.
Shipping :
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Redissolution :
A hardcopy of datasheet with reconstitution instructions is sent along with the products. Please refer to it for detailed information.
Synonyms :
HRMT1L3 Protein, Human PRMT3 背景信息 Protein arginine methyltransferase 3, also known as PRMT3, is one of four type I protein arginine methyltransferases (PRMT) that in humans is encoded by the PRMT3 gene. Methylation of arginine residues is a widespread post-translational modification of proteins catalyzed by a small family of PRMTs. The modification appears to regulate protein functions and interactions that affect gene regulation, signalling and subcellular localization of proteins and nucleic acids. In human cells, the PRMT family consists of eight canonical members. PRMTs have been classified into two groups based on the end product. Certain PRMTs display different subcellular localization in different cell types, implicating cell- and tissue-specific mechanisms for regulating PRMT functions. PRMT3 is unique in that its N-terminus harbours a C2H2 zinc-finger domain that is proposed to confer substrate specificity. Besides, PRMT3 is the only type I enzyme that is restricted to the cytoplasm. A large proportion of this cystosolic PRMT3 is found associated with ribosomes. It is tethered to the ribosomes through its interaction with rpS2, which is also its substrate.
References & Citations :
Swiercz, R. et al., 2005, Biochem J. 386 (Pt 1): 85-91. Iwasaki, H., 2008, Biochem Biophys Res Commun 372 (2): 314-9. Lei, NZ. et al., 2009, Nucleic acids Res 37 (3): 832-48. Fan, Q. et al., 2009, Biochem J. 421 (1): 107-18. Herrmann, FJ. et al., 2009, Cell Sci. 122 (Pt 5): 667-77. Kölbel, K. J Biol Chem 2009, 284 (13): 8274-82.
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