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Key Documents

I6785

Sigma-Aldrich

Anti-IRE1α antibody produced in rabbit

~1 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonyme(s) :

Anti-ERN1, Anti-Endoplasmic reticulum to nucleus signaling 1, Anti-IRE1, Anti-IRE1P, Anti-Inositol-requiring enzyme-1, Anti-Serine/threonine-protein kinase/endoribonuclease IRE1

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Niveau de qualité

Conjugué

unconjugated

Forme d'anticorps

affinity isolated antibody

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~110 kDa

Espèces réactives

human

Concentration

~1 mg/mL

Technique(s)

immunoprecipitation (IP): 2-5 μg using lysate of HEk-293T cells expressing human IRE1α
indirect immunofluorescence: suitable
western blot: 1-2 μg/mL using whole extract of HEK-293T cells expressing human IRE1α

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 ... ERN1(2081)

Description générale

Inositol-requiring enzyme-1 (IRE1), consists of an N-terminal endoplasmic reticulum (ER) luminal domain, a transmembrane domain, and a C-terminal cytoplasmic region composed of a Ser/Thr protein kinase domain and a site-specific endoribonuclease (RNase) domain.
The gene ERN1 (endoplasmic reticulum to nucleus signaling 1) encodes an ER transmembrane kinase/endoribonuclease that is also referred to as IRE1α (inositol-requiring transmembrane kinase and endonuclease 1α). The serine-threonine protein kinase encoded by this gene is ubiquitously expressed in cells and tissues.

Application

Anti-IRE1α antibody produced in rabbit has been used in western blotting and immunoprecipitation.

Actions biochimiques/physiologiques

ER transmembrane kinase/endoribonuclease serves as an ER stress sensor that initiates the splicing of the mRNA encoding X-box–binding protein 1 (XBP-1) upon activation. Spliced XBP-1 mRNA produces homeostatic transcription factor XBP1. Under ER stress, the RNase activity of IRE1α cleaves many ER-localized mRNAs associated with apoptosis. The cytosolic motif of the activated form of IRE1α associates with the adaptor protein TRAF2 (tumor necrosis factor (TNF)–associated factor 2). This complex activates the c-Jun N-terminal kinase (JNK) signaling pathway.
Inositol-requiring enzyme-1 (IRE1) is involved in the unfolded protein response (UPR), a transcriptional program induced by endoplasmic reticulum (ER) stress. The endonuclease activity of IRE1 autoregulates its mRNA and is required for the UPR. IRE1 senses the status of luminal protein folding in the ER via its N-terminal luminal domain. Presence of unfolded and misfolded proteins leads to dimerization, trans-autophosphorylation and activation of IRE1.

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

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

The unfolded protein response signals through high-order assembly of Ire1
Korennykh AV, et al.
Nature, 457(7230), 687-687 (2009)
The endoribonuclease activity of mammalian IRE1 autoregulates its mRNA and is required for the unfolded protein response
Tirasophon W, et al.
Genes & Development, 14(21), 2725-2736 (2000)
Depletion of L-arginine induces autophagy as a cytoprotective response to endoplasmic reticulum stress in human T lymphocytes
Garc
Autophagy, 8(11), 1557-1576 (2012)
Measuring ER stress and the unfolded protein response using mammalian tissue culture system
Oslowski CM and Urano F
Methods in Enzymology, 490, 71-92 (2011)
Dan Han et al.
Cell, 138(3), 562-575 (2009-08-12)
During endoplasmic reticulum (ER) stress, homeostatic signaling through the unfolded protein response (UPR) augments ER protein-folding capacity. If homeostasis is not restored, the UPR triggers apoptosis. We found that the ER transmembrane kinase/endoribonuclease (RNase) IRE1alpha is a key component of

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