I6785

Sigma-Aldrich

Anti-IRE1α antibody produced in rabbit

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

Synonym(s):
Anti-Endoplasmic reticulum to nucleus signaling 1, Anti-IRE1P, Anti-Inositol-requiring enzyme-1, Anti-ERN1, Anti-IRE1, Anti-Serine/threonine-protein kinase/endoribonuclease IRE1
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~110 kDa

species reactivity

human

concentration

~1 mg/mL

application(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

conjugate

unconjugated

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

Gene Information

human ... ERN1(2081)

General description

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.

Biochem/physiol Actions

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.

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.

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves

RIDADR

NONH for all modes of transport

WGK Germany

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

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)
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)
The unfolded protein response signals through high-order assembly of Ire1
Korennykh AV, et al.
Nature, 457(7230), 687-687 (2009)
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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