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Recombinant Saccharomyces cerevisiae Serine/threonine-protein kinase/endoribonuclease IRE1 (IRE1), partial

Recombinant Saccharomyces cerevisiae Serine/threonine-protein kinase/endoribonuclease IRE1 (IRE1), partial

Code	CSB-YP007795SVG
MSDS	MSDS
Size	Pls inquire
Source	Yeast
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Code	CSB-EP007795SVG
MSDS	MSDS
Size	Pls inquire
Source	E.coli
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Code	CSB-EP007795SVG-B
MSDS	MSDS
Size	Pls inquire
Source	E.coli
Conjugate	Avi-tag Biotinylated E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code	CSB-BP007795SVG
MSDS	MSDS
Size	Pls inquire
Source	Baculovirus
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Code	CSB-MP007795SVG
MSDS	MSDS
Size	Pls inquire
Source	Mammalian cell
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Product Details
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Customer Reviews and Q&A
Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

IRE1

Uniprot No.

P32361

Alternative Names

IRE1; ERN1; YHR079C; Serine/threonine-protein kinase/endoribonuclease IRE1; Endoplasmic reticulum-to-nucleus signaling 1) [Includes: Serine/threonine-protein kinase; EC 2.7.11.1); Endoribonuclease; EC 3.1.26.-)]

Species

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Protein Length

Partial

Tag Info

Tag type will be determined during the manufacturing process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose, pH 8.0

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet

Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function

Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto-activation. The active endoribonuclease domain splices HAC1 precursor mRNA to produce the mature form which then induces transcription of UPR target genes.

Gene References into Functions

The most conserved transducer of ER stress, Ire1, uses an amphipathic helix to sense membrane aberrancies and control unfolded protein response activity. PMID: 28689662
Here we show that in yeast cells, the ER-stress sensor Ire1 was activated upon zinc deficiency PMID: 23748779
Under ER stress, Ire1 molecules exist in activated and Bip-associated state. PMID: 23387983
Results show that the kinase domain autophosphorylatse the auto-inhibitory region in order to relieve auto-inhibition and that ADP acts as a switch to activate the kinase extension nuclease domain-catalyzed HAC1 mRNA cleavage. PMID: 23541589
the cytosolic or transmembrane domain of Ire1 senses membrane aberrancy PMID: 21775630
core ER-lumenal domain (cLD) of Ire1 binds to unfolded proteins in yeast and to peptides in vitro; peptide binding caused Ire1 cLD oligomerization in vitro, suggesting direct binding to unfolded proteins activates unfolded protein response PMID: 21852455
Flavonol activation defines an unanticipated ligand-binding site in the kinase-RNase domain of IRE1. PMID: 20417606
although its sequence is little conserved evolutionarily, subregion IV plays an essential role to promote Ire1 dimer formation PMID: 15954865
Our results are consistent with de-phosphorylation of Ire1 being a mechanism for antagonizing UPR signalling. PMID: 16990850
The capacity of a highly basic sequence in the linker region of Ire1p to function as a nuclear localization sequence (NLS) both in vivo and in vitro, was analyzed. PMID: 17035634
Observations indicate that in addition to BiP dissociation and self-association of Ire1, another unknown change on the luminal side is crucial for Ire1 activation. PMID: 17452628
Upon endoplasmic reticulum (ER) stress, Ire1 clusters and actually interacts with unfolded proteins. PMID: 17923530
We have determined the crystal structure of the dual catalytic region of Ire1at 2.4 A resolution, revealing the fusion of a domain, which we term the KEN domain, to the protein kinase domain. PMID: 18191223
oligomerization is central to Ire1 function and is an intrinsic attribute of its cytosolic domains; 3.2-A crystal structure of the oligomer of the Ire1 cytosolic domains in complex with a kinase inhibitor PMID: 19079236