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Key Documents

T0825

Sigma-Aldrich

Anti-Transportin 1 antibody, Mouse monoclonal

clone D45, purified from hybridoma cell culture

Synonym(s):

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

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About This Item

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

biological source

mouse

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

D45, monoclonal

form

buffered aqueous solution

mol wt

antigen ~90 kDa

species reactivity

mouse, canine, rat, human, bovine

technique(s)

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

isotype

IgG1

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

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

General description

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)

Immunogen

recombinant human transportin 1.

Application

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

Biochem/physiol Actions

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.

Target description

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

Physical form

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

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Storage Class Code

10 - Combustible liquids

WGK

WGK 2

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


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’.

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microRNA miR-128 represses LINE-1 retrotransposition by downregulating the nuclear import factor TNPO1
Idica A, et al.
The Journal of Biological Chemistry, 28(1), jbc-M117 (2017)
Transcriptional regulation of importin-alpha1 by JunD modulates subcellular localization of RNA-binding protein HuR in intestinal epithelial cells
Xu Y, et al.
American Journal of Physiology. Cell Physiology, 311(6), C874-C883 (2016)
Structural basis for substrate recognition and dissociation by human transportin 1
Imasaki T, et al.
Molecular Cell, 28(1), 57-67 (2007)
Imke Baade et al.
The Journal of biological chemistry, 296, 100659-100659 (2021-04-16)
Fused in sarcoma (FUS) is a predominantly nuclear RNA-binding protein with key functions in RNA processing and DNA damage repair. Defects in nuclear import of FUS have been linked to severe neurodegenerative diseases; hence, it is of great interest to
IPO3 mediated nonclassical nuclear import of NEMO drives DNA damage-dependent NF-kappaB activation
Hwang B, et al.
The Journal of Biological Chemistry, jbc-M115 (2015)

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