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P6996

Sigma-Aldrich

Anti-PRMT1 (TK-16) antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

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Synonym(s):
Anti-Protein Arginine Methyl Transferase 1
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

monkey, hamster, mouse, rat, human

technique(s)

immunoprecipitation (IP): 2.5-5 μg using extracts of 293T cells
microarray: suitable
western blot: 1-2 μg/mL using total extracts of 293T cells

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

Protein arginine methyl transferase 1 (PRMT1) is a 361 amino acid protein; its splicing variants differ at the N-terminus, giving rise to three isoforms of 343, 361, and 347 amino acids (variants 1, 2, and 3 respectively).
The PRMT1 gene is mapped on the human chromosome at 19q13.33.

Specificity

Anti-PRMT1 (Protein Arginine Methyl Transferase 1) (TK-16) recognizes PRMT1 (approx. 42 kDa) from human, rat, mouse, monkey, and hamster origin.

Immunogen

synthetic peptide corresponding to amino acids 309-324 of rat PRMT1 conjugated to KLH via an N-terminal added cysteine residue. This sequence is conserved in human and rat.

Application

Anti-PRMT1 (TK-16) antibody produced in rabbit may be used in immunoblotting and immunoprecipitation.

Biochem/physiol Actions

Protein arginine methyl transferase (PRMT) family of enzymes catalyzes the methylation of arginine during post translational modification. 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. Both types 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. Proteins involved in the metabolism of RNA like 68-kDa Src-associated substrate in mitosis (Sam68) are substrates for PRMT1.

Physical form

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

Storage and Stability

For continuous use, store at 2-8 °C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing is not recommended. Storage in frost-free freezers is also not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilu-tions should be discarded if not used within 12 hours.

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.

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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Ahmad Miremadi et al.
Human molecular genetics, 16 Spec No 1, R28-R49 (2007-09-26)
The cancer epigenome is characterised by specific DNA methylation and chromatin modification patterns. The proteins that mediate these changes are encoded by the epigenetics genes here defined as: DNA methyltransferases (DNMT), methyl-CpG-binding domain (MBD) proteins, histone acetyltransferases (HAT), histone deacetylases
Protein arginine methylation of non-histone proteins and its role in diseases.
Wei H, et al.
Cell Cycle, 13(1), 32-41 (2014)
The role of protein arginine methyltransferases in inflammatory responses.
Kim JH, et al.
Mediators of Inflammation, 2016(1), 32-41 (2016)
The effect of PRMT1-mediated arginine methylation on the subcellular localization, stress granules, and detergent-insoluble aggregates of FUS/TLS.
Yamaguchi A and Kitajo K
Testing, 7(11), e49267-e49267 (2012)

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