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Key Documents

T0825

Sigma-Aldrich

Anti-Transportin 1 antibody, Mouse monoclonal

clone D45, purified from hybridoma cell culture

Sinonimo/i:

Anti-IPO2, Anti-KPNB2, Anti-MIP, Anti-MIP1, Anti-TRN

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About This Item

Numero MDL:
Codice UNSPSC:
12352203
NACRES:
NA.41

Origine biologica

mouse

Coniugato

unconjugated

Forma dell’anticorpo

purified from hybridoma cell culture

Tipo di anticorpo

primary antibodies

Clone

D45, monoclonal

Forma fisica

buffered aqueous solution

PM

antigen ~90 kDa

Reattività contro le specie

mouse, canine, rat, human, bovine

tecniche

immunocytochemistry: suitable
immunoprecipitation (IP): suitable
microarray: suitable
western blot: 0.1-0.2 μg/mL using HeLa nuclear extract

Isotipo

IgG1

N° accesso UniProt

Condizioni di spedizione

dry ice

Temperatura di conservazione

−20°C

modifica post-traduzionali bersaglio

unmodified

Informazioni sul gene

human ... TNPO1(3842)
mouse ... Tnpo1(238799)
rat ... Tnpo1(309126)

Descrizione generale

Transportin 1 (TNPO1 or TRN1) also known as karyopherin-β2, is a nuclear import protein and belongs to importin-β family. In the human chromosome the TNPO1 gene is localized on 5q13.2.(10)

Immunogeno

recombinant human transportin 1.

Applicazioni

Monoclonal Anti-Transportin 1 antibody produced in mouse has been used in western blotting, immunofluorescence, and immunostaining.

Azioni biochim/fisiol

Transportin 1 (TNPO1 or TRN1) recognizes the nuclear localization signals (NLS) and binds to the nuclear pore complex (NPC) to facilitate the transport of substances from cytoplasm to nucleus. TRN1 transports viral, and ribosomal proteins with the aid of RanGTP (Ras associated nuclear protein-GTP). TRN1 is also known to regulate the key events in the cell cycle assembly like nuclear membrane and nuclear pore. Mutations in TRN1 might cause amyotrophic lateral sclerosis due to mislocalisation of FUS (fused in sarcoma) protein. TRN1 is associated with regulation of circadian rhythm through nuclear localization of PER1 (period circadian protein homolog 1) protein.

Descrizione del bersaglio

Transportin 1 encodes the beta subunit of the karyopherin receptor complex which interacts with nuclear localization signals to target nuclear proteins to the nucleus. The karyopherin receptor complex is a heterodimer of an alpha subunit which recognizes

Stato fisico

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 1% bovine serum albumin and 15 mM sodium azide.

Esclusione di responsabilità

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.

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Codice della classe di stoccaggio

10 - Combustible liquids

Classe di pericolosità dell'acqua (WGK)

WGK 2

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


Certificati d'analisi (COA)

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Genome-wide genetic aberrations of thymoma using cDNA microarray based comparative genomic hybridization
Lee GY, et al.
BMC Genomics, 8(1), 305-305 (2007)
Benjamin Bourgeois et al.
Proceedings of the National Academy of Sciences of the United States of America, 117(15), 8503-8514 (2020-04-03)
The specific interaction of importins with nuclear localization signals (NLSs) of cargo proteins not only mediates nuclear import but also, prevents their aberrant phase separation and stress granule recruitment in the cytoplasm. The importin Transportin-1 (TNPO1) plays a key role
Hypertonic Stress Causes Cytoplasmic Translocation of Neuronal, but Not Astrocytic, FUS due to Impaired Transportin Function
Hock EM, et al.
Cell Reports, 24(4), 987-1000 (2018)
The non-classical nuclear import carrier Transportin 1 modulates circadian rhythms through its effect on PER1 nuclear localization
Korge S, et al.
PLoS Genetics, 14(1), e1007189-e1007189 (2018)
FUS-NLS/Transportin 1 complex structure provides insights into the nuclear targeting mechanism of FUS and the implications in ALS
Niu C, et al.
PLoS ONE, 7(10), e47056-e47056 (2012)

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