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Merck
CN

ABE1003

Anti-Transportin-3 Antibody

from rabbit, purified by affinity chromatography

别名:

Transportin-3, Importin-12, Imp12, Transportin-SR, TRN-SR, Transportin-3

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UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702

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产品名称

Anti-Transportin-3 Antibody, from rabbit, purified by affinity chromatography

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

purified by

affinity chromatography

species reactivity

human

species reactivity (predicted by homology)

bovine (based on 100% sequence homology), monkey (based on 100% sequence homology), equine (based on 100% sequence homology), mouse (based on 100% sequence homology), sheep (based on 100% sequence homology), rat (based on 100% sequence homology)

technique(s)

western blot: suitable

NCBI accession no.

NP_036602

UniProt accession no.

Q9Y5L0

shipped in

dry ice

target post-translational modification

unmodified

Quality Level

100

Gene Information

human ... TNPO3(23534)

General description

~100 kDa observed
Transportin 3 (UniProt Q9Y5L0; also known as Imp12, Importin 12, Limb girdle muscular dystrophy 1F, Transportin-SR, TRN-SR, TRN-SR2) is encoded by the TNPO3 gene (also known as IPO12, LGMD1F, MTR10A, TRNSR) (Gene ID 23534) in human. The transport of macromolecules between cytoplasm and nucleus is mediated by importins and exportins and is regulated by the small GTPase Ran. Importins bind their cargo in the cytoplasm, and the competitive binding of RanGTP induces cargoes release in the nucleus. Most nuclear importins and exportins, including transportin-3 (importin-12), belong to the beta-karyopherin family of proteins. Transportin-3 associates with and mediates the nuclear import of a wide range of serine/arginine-rich/RS domain-containing proteins, the majority of which are involved in mRNA processing, including the cleavage and polyadenylation specificity factor 6 (CPSF6, CF-Im-68) and the splicing factors alternative splicing factor/splicing factor 2 (ASF/SF2) & SC35. In addition, Transportin-3 also plays a cofactor role in facilitating HIV-1 replication. Phosphorylation of the ASF/SF2 RS domain is required for its interaction with Transprotin-3 HEAT repeat 15. Mutations in the HEAT repeat 15 region of Transprotin-3 likewise are reported to impair its interaction with CPSF6 and its ability to support HIV-1 replication.

Other Notes

Concentration: Please refer to lot specific datasheet.

Physical form

Affinity purified
Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Immunogen

KLH-conjugated linear peptide corresponding to human Transportin-3.

Analysis Note

Evaluated by Western Blotting in Staurosporin treated Jurkat cell lysate.

Western Blotting Analysis: 0.5 µg/mL of this antibody detected Transportin-3 in 10 µg of Staurosporin treated Jurkat cell lysate.

Application

Research Category
Epigenetics & Nuclear Function
Research Sub Category
Nuclear Receptors
This Anti-Transportin-3 Antibody is validated for use in Western Blotting for the detection of Transportin-3 .

Biochem/physiol Actions

Expected to react with all four spliced isoforms.

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.

Preparation Note

Stable for 1 year at 2-8°C from date of receipt.

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存储类别

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

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相关内容

White Paper: Further considerations of antibody validation and usage.
Characterization of Estrogen Receptor α Phosphorylation Sites in Breast Cancer Tissue Using the SNAP i.d® 2.0 System

A major focus of breast cancer research is to understand the mechanisms responsible for disease progression and drug resistance. Toward that end, it has been found that approximately two thirds of all human breast carcinomas overexpress the Estrogen Receptor α (ERα) protein and it remains the primary pharmacological target for endocrine therapy1,2. The normal cellular function of ERα is as a transcription factor that mediates a wide variety of physiological processes, many of which are dependent upon phosphorylation of the receptor at specific amino acid residues3,4. Indeed, ERα is known to be phosphorylated at a multitude of different sites, yet how these all correlate to disease remains unclear5. Here, we interrogated multiple sites of ERα for phosphorylation status by screening an extensive panel of different breast cancer patient samples and other non-breast cancer tissue microarray (TMA) slide samples to determine their relevance to disease.

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