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SAB4200115

Sigma-Aldrich

Anti-Reptin antibody, Mouse monoclonal

clone 2E9-5, purified from hybridoma cell culture

Synonyme(s) :

Anti-CGI-46, Anti-ECP51 (Erythrocyte cytosolic protein, 51-KD), Anti-INO80J, Anti-RUVBL2 (RuvB-like 2), Anti-RVB2, Anti-TIH2, Anti-TIP48 (TATA box-binding protein-interacting protein, 48-KD), Anti-TIP49B

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Conjugué

unconjugated

Forme d'anticorps

purified from hybridoma cell culture

Type de produit anticorps

primary antibodies

Clone

2E9-5, monoclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~51 kDa

Espèces réactives

human, rat, mouse

Conditionnement

antibody small pack of 25 μL

Concentration

~1.0 mg/mL

Technique(s)

western blot: 0.5-1.0 μg/mL using whole extract of human MCF-7 cells

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... RUVBL2(10856)

Description générale

Monoclonal Anti-Reptin (mouse IgG1 isotype) is derived from the hybridoma 2E9-5 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a human Reptin fusion protein.
Reptin, also known as RuvB-like 2 RUVBL2, is encoded by the gene mapped to human chromosome 19q13.33. The encoded protein belongs to the AAA+ family of DNA helicases.

Immunogène

a human Reptin fusion protein. The corresponding sequence differs by one amino acid in mouse.

Application

Monoclonal Anti-Reptin antibody produced in mouse has been used in:
  • immunoblotting
  • immunoprecipitation
  • immunofluorescence
  • confocal microscopy

Actions biochimiques/physiologiques

Reptin and pontin are associated with several chromatin-remodeling complexes and are involved in multiple biological processes including chromatin remodeling, DNA damage repair, telomerase activity, transcriptional regulation, apoptosis and cancer metastasis. Both proteins are also involved in cellular transformation by β-catenin and c-myc through their chromatin remodeling function.
Reptin has been involved in various cellular processes, including the response to DNA double-strand breaks and the control of gene expression. The encoded protein plays a vital role in repression of specific β-catenin and nuclear factor-κB targets. Elevated expression of the gene leads to the development of hepatocellular carcinomas (HCC) and renal cell carcinoma (RCC). Thus, reptin can be considered as a potential therapeutic target for HCC and RCC.

Forme physique

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


Certificats d'analyse (COA)

Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

The histidine triad protein Hint1 interacts with Pontin and Reptin and inhibits TCF-beta-catenin-mediated transcription
Weiske J and Huber O
Journal of Cell Science, 118(14), 3117-3129 (2005)
Pontin and reptin, two related ATPases with multiple roles in cancer
Huber O, et al.
Cancer Research, 68(17), 6873-6876 (2008)
DNAAF1 links heart laterality with the AAA+ ATPase RUVBL1 and ciliary intraflagellar transport
Hartill VL, et al.
Human Molecular Genetics, 27(3), 529-545 (2017)
Reptin and Pontin oligomerization and activity are modulated through histone H3 N-terminal tail interaction
Queval R, et al.
The Journal of Biological Chemistry, 289(49), 33999-34012 (2014)
Control of transcription by Pontin and Reptin.
Gallant P
Trends in Cell Biology, 17, 187-192 (2007)

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