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SAB4200115

Sigma-Aldrich

Anti-Reptin antibody, Mouse monoclonal

clone 2E9-5, purified from hybridoma cell culture

Synonym(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

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

2E9-5, monoclonal

form

buffered aqueous solution

mol wt

antigen ~51 kDa

species reactivity

human, rat, mouse

packaging

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

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... RUVBL2(10856)

General description

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.

Immunogen

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

Biochem/physiol Actions

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.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 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

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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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)
Overexpression of reptin in renal cell carcinoma contributes to tumor malignancies and its inhibition triggers senescence of cancer cells.
Ren J
Urologic Oncology, 31, 1358-1366 (2013)
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)
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)

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