Skip to Content
Merck
All Photos(1)

Key Documents

P6871

Sigma-Aldrich

Anti-PRMT1 antibody produced in rabbit

~1 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-Protein Arginine Methyl Transferase 1 (NQ-15)

Sign Into View Organizational & Contract Pricing


About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~42 kDa

species reactivity

human

concentration

~1 mg/mL

technique(s)

indirect immunofluorescence: 2.5-5.0 μg/mL using paraformaldehyde-fixed 293T cells
microarray: suitable
western blot: 0.25-0.5 μg/mL using 293T cell extracts

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... PRMT1(3276)
mouse ... Prmt1(15469)

General description

PRMT1 belongs to the family of protein arginine methyl transferases (PRMT). These enzymes transfer the methyl group from S-adenosyl-L methionine to the guanidino nitrogen atoms of an arginine residue. PRMTs are divided in two major types, I and II. It is also known as HRMT1L2 and IR1B4. PRMT1 was isolated through its interaction with BTG1 and TIS2, proteins that are important in cell quiescence. It is a 361 amino acids protein; its splicing variants differ at the N-terminus, giving rise to three isoforms (variants 1, 2 and 3).

Immunogen

synthetic peptide corresponding to amino acids 326-341 of mouse PRMT1, conjugated to KLH via an N-terminal added cysteine residue. The sequence is conserved in human, and differs by one amino acid from the rat sequence.

Application

Anti-PRMT1 antibody produced in rabbit has been used in immunoblotting.

Biochem/physiol Actions

PRMT type 1 and 2 catalyze the formation of monomethylarginine, but differs in that Type I (including PRMT1, 3, 4, and 6) catalyzes the formation of asymmetric dimethylarginine, whereas type II (PRMT5) catalyzes the formation of symmetric dimethylarginine.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Not finding the right product?  

Try our Product Selector Tool.

Storage Class Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

PRMT1 promotes mitosis of cancer cells through arginine methylation of INCENP
Deng X, et al.
Oncotarget, 6(34), 35173-35173 (2015)
Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizing protein, by CARM1
Li H, et al.
The Journal of biological chemistry, 277(47), 44623-44630 (2002)
Prmt5, which forms distinct homo-oligomers, is a member of the protein-arginine methyltransferase family
Rho J, et al.
The Journal of biological chemistry, 276(14), 11393-11401 (2001)
The novel human protein arginine N-methyltransferase PRMT6 is a nuclear enzyme displaying unique substrate specificity.
Frankel A
The Journal of Biological Chemistry, 277(5), 3537-3543 (2002)
Xiaolan Deng et al.
Oncotarget, 6(34), 35173-35182 (2015-10-16)
Inner centromere protein (INCENP) is a part of a protein complex known as the chromosomal passenger complex (CPC) that is essential for correcting non-bipolar chromosome attachments and for cytokinesis. We here demonstrate that a protein arginine methyltransferase PRMT1, which are

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service