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Key Documents

CdO/CdA

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

Sinonimo/i:

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

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About This Item

Codice UNSPSC:

12352203

NACRES:

NA.41

Origine biologica

mouse

Livello qualitativo

100

Coniugato

unconjugated

Forma dell’anticorpo

purified immunoglobulin

Tipo di anticorpo

primary antibodies

Clone

3F1, monoclonal

Forma fisica

buffered aqueous solution

Reattività contro le specie

human

tecniche

indirect ELISA: suitable

Isotipo

IgG1κ

N° accesso Genebanck

BC011999

N° accesso UniProt

Q96RS0

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... TGS1(96764)

Descrizione generale

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).

Immunogeno

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

Azioni biochim/fisiol

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.

Stato fisico

Solution in phosphate buffered saline, pH 7.4

Note legali

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

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Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

nwg

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable

Dispositivi di protezione individuale

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

Certificati d'analisi (COA)

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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

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