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SAB4200005

Sigma-Aldrich

Anti-UVRAG antibody ,Mouse monoclonal

clone UVRAG-11, purified from hybridoma cell culture

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Synonym(s):
Anti-DHTX, Anti-UV radiation resistance-associated gene protein, Anti-p63

biological source

mouse

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

UVRAG-11, monoclonal

form

buffered aqueous solution

mol wt

antigen ~90 kDa

species reactivity

mouse, human

concentration

~1.0 mg/mL

technique(s)

immunoprecipitation (IP): suitable
western blot: 2-4 μg/mL using whole extract of human G361 cells

isotype

IgG1

UniProt accession no.

Q9P2Y5

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... UVRAG(7405)
mouse ... Uvrag(78610)

General description

Monoclonal Anti-UVRAG (mouse IgG1 isotype) is derived from the hybridoma UVRAG-11 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a synthetic peptide corresponding to a fragment of human UVRAG.
Ultraviolet irradiation resistance-associated gene (UVRAG) is a crucial autophagic tumor suppressor, encoded by the gene mapped to human chromosome 11q13.5. The encoded protein is characterized with four functional domains, such as proline-rich domain, a lipid-binding C2 domain, a Beclin1-binding coiled-coil domain (CCD) and a C-terminal domain involved in centrosome integrity and DNA damage repair.

Application

Monoclonal Anti-UVRAG antibody produced in mouse has been used in immunoprecipitation.
Monoclonal Anti-UVRAG antibody produced in mouse has been used in western blotting and immunohistochemistry.

Biochem/physiol Actions

UVRAG is positive regulator of the Beclin 1- class III phosphatidylinositol 3-kinase (PI(3)KC3) complex. The tumor suppressor Beclin 1 forms a complex with PI(3)KC3, promoting autophagosome formation. UVRAG interacts with Beclin 1 through their coiled-coil domains and induces autophagy resultin in suppression of proliferation and tumorigenicity of human colon cancer cells. UVRAG is a tumor suppressor candidate.
Ultraviolet irradiation resistance-associated gene (UVRAG) is implicated in the regulation of intracellular membrane trafficking, including autophagy and chromosomal stability. The encoded protein regulates apoptosis by suppressing the BCL2-associated X protein (Bax) activity. Mutation in the gene has been observed in various types of human cancers, including microsatellite unstable colon carcinomas.

Target description

Anti-UVRAG, UV radiation resistance associated gene, complements the ultraviolet sensitivity of xeroderma pigmentosum group C cells and encodes a protein with a C2 domain. The protein activates the Beclin1-PI(3)KC3 complex, promoting autophagy and suppres

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.

Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Autophagic and tumour suppressor activity of a novel Beclin1-binding protein UVRAG
Liang C, et al.
Nature Cell Biology, 8(7), 688-688 (2006)
UV irradiation resistance-associated gene suppresses apoptosis by interfering with BAX activation.
Yin X
EMBO Reports (2011)
The genomic and transcriptomic architecture of 2,000 breast tumours reveals novel subgroups
Christina Curtis
Nature (2012)
Truncating mutation in the autophagy gene UVRAG confers oncogenic properties and chemosensitivity in colorectal cancers
Shanshan He
Nature Communications (2015)
Kenta Kuramoto et al.
Cell reports, 35(8), 109184-109184 (2021-05-27)
Autophagy dysregulation is implicated in metabolic diseases, including type 2 diabetes. However, the mechanism by which the autophagy machinery regulates metabolism is largely unknown. Autophagy is generally considered a degradation process via lysosomes. Here, we unveil a metabolically important non-cell-autonomous
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