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Key Documents

HPA012669

Sigma-Aldrich

Anti-UBXN1 antibody produced in rabbit

Prestige Antibodies® Powered by Atlas Antibodies, affinity isolated antibody, buffered aqueous glycerol solution

Sinónimos:

Anti-SAPK substrate protein 1, Anti-UBA/UBX 33.3 kDa protein, Anti-UBX domain-containing protein 1

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About This Item

UNSPSC Code:
12352203
Human Protein Atlas Number:
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

product line

Prestige Antibodies® Powered by Atlas Antibodies

form

buffered aqueous glycerol solution

species reactivity

human, rat, mouse

technique(s)

immunoblotting: 0.04-0.4 μg/mL
immunofluorescence: 0.25-2 μg/mL
immunohistochemistry: 1:200-1:500

immunogen sequence

MAELTALESLIEMGFPRGRAEKALALTGNQGIEAAMDWLMEHEDDPDVDEPLETPLGHILGREPTSSEQGGLEGSGSAAGEGKPALSEEERQEQTKRMLELVAQKQREREEREEREALERERQRRRQGQELSAARQRLQEDEMRRAAEER

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... UBXN1(51035)

Categorías relacionadas

General description

UBX domain-containing protein 1 (UBXN1) contains a ubiquitin-associated (UBA) motif and a ubiquitin regulatory X (UBX) domain.

Immunogen

UBX domain-containing protein 1 recombinant protein epitope signature tag (PrEST)

Application

All Prestige Antibodies Powered by Atlas Antibodies are developed and validated by the Human Protein Atlas (HPA) project and as a result, are supported by the most extensive characterization in the industry.

The Human Protein Atlas project can be subdivided into three efforts: Human Tissue Atlas, Cancer Atlas, and Human Cell Atlas. The antibodies that have been generated in support of the Tissue and Cancer Atlas projects have been tested by immunohistochemistry against hundreds of normal and disease tissues and through the recent efforts of the Human Cell Atlas project, many have been characterized by immunofluorescence to map the human proteome not only at the tissue level but now at the subcellular level. These images and the collection of this vast data set can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. We also provide Prestige Antibodies® protocols and other useful information.

Biochem/physiol Actions

UBX domain-containing protein 1 (UBXN1) recognizes breast cancer 1 (BRCA1) which is autoubiquitinated. This takes place by the binding of the ubiquitin-associated (UBA) domain of UBXN1 to the K6-linked polyubiquitin chains linked to BRCA1. The C-terminal sequences of UBXN1 also bind to the BRCA1/ BRCA1 associated RING domain 1 (BARD1) heterodimer. It then reduces the E3 ligase activity of BRCA1/BARD1 which is dependent on the ubiquitination status of BRCA1. It also functions as a negative regulator of tumor necrosis factor α (TNFα)-mediated nuclear factor kappa B (NF-κB) activation. UBXN1 interacts with the cellular inhibitors of apoptosis proteins (cIAPs) and with E3 ubiquitin ligases, which are a part of receptor-interacting protein 1 (RIP1) in the TNFα receptor complex. It tightly binds to cIAP1, blocks its recruitment to TNFR1 and inhibits the RIP1 polyubiquitination in response to TNFα.

Features and Benefits

Prestige Antibodies® are highly characterized and extensively validated antibodies with the added benefit of all available characterization data for each target being accessible via the Human Protein Atlas portal linked just below the product name at the top of this page. The uniqueness and low cross-reactivity of the Prestige Antibodies® to other proteins are due to a thorough selection of antigen regions, affinity purification, and stringent selection. Prestige antigen controls are available for every corresponding Prestige Antibody and can be found in the linkage section.

Every Prestige Antibody is tested in the following ways:
  • IHC tissue array of 44 normal human tissues and 20 of the most common cancer type tissues.
  • Protein array of 364 human recombinant protein fragments.

Linkage

Corresponding Antigen APREST70262

Physical form

Solution in phosphate-buffered saline, pH 7.2, containing 40% glycerol and 0.02% sodium azide

Legal Information

Prestige Antibodies is a registered trademark of Merck KGaA, Darmstadt, Germany

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

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Visite la Librería de documentos

Foon Wu-Baer et al.
Molecular and cellular biology, 30(11), 2787-2798 (2010-03-31)
Although the BRCA1 tumor suppressor has been implicated in many cellular processes, the biochemical mechanisms by which it influences these diverse pathways are poorly understood. The only known enzymatic function of BRCA1 is the E3 ubiquitin ligase activity mediated by
Yu-Bo Wang et al.
The Journal of biological chemistry, 290(16), 10395-10405 (2015-02-15)
Excessive nuclear factor κB (NF-κB) activation should be precisely controlled as it contributes to multiple immune and inflammatory diseases. However, the negative regulatory mechanisms of NF-κB activation still need to be elucidated. Various types of polyubiquitin chains have proved to
Yani Hu et al.
PLoS pathogens, 13(2), e1006187-e1006187 (2017-02-06)
UBXN proteins likely participate in the global regulation of protein turnover, and we have shown that UBXN1 interferes with RIG-I-like receptor (RLR) signaling by interacting with MAVS and impeding its downstream effector functions. Here we demonstrate that over-expression of multiple

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