All Photos(1)

Key Documents

COO/COA

WH0096764M1

Monoclonal Anti-NCOA6IP antibody produced in mouse

Name: Monoclonal Anti-NCOA6IP antibody produced in mouse
Brand: SIGMA

clone 3F1, purified immunoglobulin, buffered aqueous solution

Synonym(s):

Anti-FLJ22995, Anti-PIMT, Anti-PIPMT, Anti-nuclear receptor coactivator 6 interacting protein

Sign Into View Organizational & Contract Pricing

All Photos(1)

About This Item

UNSPSC Code:

12352203

NACRES:

NA.41

biological source

mouse

Quality Level

100

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

3F1, monoclonal

form

buffered aqueous solution

species reactivity

human

technique(s)

indirect ELISA: suitable

isotype

IgG1κ

GenBank accession no.

BC011999

UniProt accession no.

Q96RS0

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... TGS1(96764)

General description

The gene TGS1 (trimethylguanosine synthase 1) is mapped to human chromosome 8q11. The encoded protein has a methyltransferase domain, a K-homology domain for RNA binding, and a motif for SmB and SmD1 (small nuclear ribonucleoproteins) binding. The protein has a long form which localize in the cytoplasm and a short form which is present in the nucleus. It interacts with PRIP (proliferator-activated receptor-interacting protein).

Immunogen

NCOA6IP (AAH11999, 1 a.a. ~ 141 a.a) full-length recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.

Sequence
MRVIAIDIDPVKIALARNNAEVYGIADKIEFICGDFLLLASFLKADVVFLSPPWGGPDYATAETFDIRTMMSPDGFEIFRLSKKITNNIVYFLPRNADIDQVASLAGPGGQVEIEQNFLNNKLKTITAYFGDLIRRPASET

Biochem/physiol Actions

TGS1 (trimethylguanosine synthase 1) is responsible for the methylation of the m7G (7-methylguanylate) cap of RNA polymerase II transcribed snRNAs (small nuclear RNAs) and snoRNAs (small nucleolar RNAs), leading to the formation of 2,2,7-trimethylguanosine cap. In mice, absence of TGS1 activity causes embryonic lethality. It is also involved in gene regulation by interacting with proteins of cytoskeletal network and nuclear factors.

Physical form

Solution in phosphate buffered saline, pH 7.4

Legal Information

GenBank is a registered trademark of United States Department of Health and Human Services

Not finding the right product?

Try our Product Selector Tool.

Storage Class Code

10 - Combustible liquids

WGK

nwg

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

Chemical approaches for structure and function of RNA in postgenomic era.

Tae Suk Ro-Choi et al.

Journal of nucleic acids, 2012, 369058-369058 (2012-02-22)

In the study of cellular RNA chemistry, a major thrust of research focused upon sequence determinations for decades. Structures of snRNAs (4.5S RNA I (Alu), U1, U2, U3, U4, U5, and U6) were determined at Baylor College of Medicine, Houston

Self-association of Trimethylguanosine Synthase Tgs1 is required for efficient snRNA/snoRNA trimethylation and pre-rRNA processing.

Kum-Loong Boon et al.

Scientific reports, 5, 11282-11282 (2015-06-16)

Trimethylguanosine Synthase catalyses transfer of two methyl groups to the m(7)G cap of RNA polymerase II transcribed snRNAs, snoRNAs, and telomerase RNA TLC1 to form a 2,2,7-trimethylguanosine cap. While in vitro studies indicate that Tgs1 functions as a monomer and

Different isoforms of PRIP-interacting protein with methyltransferase domain/trimethylguanosine synthase localizes to the cytoplasm and nucleus.

Izzet Enünlü et al.

Biochemical and biophysical research communications, 309(1), 44-51 (2003-08-29)

A protein family including the recently identified PIMT/Tgs1 (PRIP-interacting protein with methyltransferase domain/trimethylguanosine synthase) was identified by searching databases for homologues of a newly identified Drosophila protein with RNA-binding activity and methyltransferase domain. Antibodies raised against a short peptide of

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