Recombinant mouse IRE1 protein (Active) is a Mouse Fragment protein, in the 469 to 977 aa range, expressed in Baculovirus infected Sf9, with >90% purity and suitable for SDS-PAGE, FuncS.
Images
Key facts
- Purity
- >90% SDS-PAGE
- Expression system
- Baculovirus infected Sf9 cells
- Tags
- GST tag N-Terminus
- Applications
- SDS-PAGE, FuncS
- Biologically active
- Yes
Amino acid sequence
S V H Q Q R Q L Q H Q Q F Q K E L E K I Q L L Q Q Q Q L P F H P H G D L T Q D P E F L D S S G P F S E S S G T S S P S P S P R A S N H S L H P S S S A S R A G T S P S L E Q D D E D E E T R M V I V G K I S F C P K D V L G H G A E G T I V Y K G M F D N R D V A V K R I L P E C F S F A D R E V Q L L R E S D E H P N V I R Y F C T E K D R Q F Q Y I A I E L C A A T L Q E Y V E Q K D F A H L G L E P I T L L H Q T T S G L A H L H S L N I V H R D L K P H N I L L S M P N A H G R I K A M I S D F G L C K K L A V G R H S F S R R S G V P G T E G W I A P E M L S E D C K D N P T Y T V D I F S A G C V F Y Y V I S E G N H P F G K S L Q R Q A N I L L G A C N L D C F H S D K H E D V I A R E L I E K M I A M D P Q Q R P S A K H V L K H P F F W S L E K Q L Q F F Q D V S D R I E K E A L D G P I V R Q L E R G G R A V V K M D W R E N I T V P L Q T D L R K F R T Y K G G S V R D L L R A M R N K K H H Y R E L P V E V Q E T L G S I P D D F V R Y F T S R F P H L L S H T Y Q A M E L C R H E R L F Q T Y Y W H E P T E P Q P P V I P Y A L
Reactivity data
| Application | Reactivity | Dilution info | Notes |
|---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Target data
Function
Serine/threonine-protein kinase and endoribonuclease that acts as a key sensor for the endoplasmic reticulum unfolded protein response (UPR) (PubMed:11850408, PubMed:25164867). In unstressed cells, the endoplasmic reticulum luminal domain is maintained in its inactive monomeric state by binding to the endoplasmic reticulum chaperone HSPA5/BiP. Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP, allowing the luminal domain to homodimerize, promoting autophosphorylation of the kinase domain and subsequent activation of the endoribonuclease activity (PubMed:25164867). The endoribonuclease activity is specific for XBP1 mRNA and excises 26 nucleotides from XBP1 mRNA (PubMed:11850408, PubMed:25164867). The resulting spliced transcript of XBP1 encodes a transcriptional activator protein that up-regulates expression of UPR target genes (PubMed:11850408, PubMed:25164867). Acts as an upstream signal for ER stress-induced GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of CFTR to cell membrane by modulating the expression and localization of SEC16A (By similarity).
Alternative names
Ire1, Ern1, Serine/threonine-protein kinase/endoribonuclease IRE1, Endoplasmic reticulum-to-nucleus signaling 1, Inositol-requiring protein 1, Ire1-alpha, IRE1a
Recommended products
Recombinant mouse IRE1 protein (Active) is a Mouse Fragment protein, in the 469 to 977 aa range, expressed in Baculovirus infected Sf9, with >90% purity and suitable for SDS-PAGE, FuncS.
Key facts
- Purity
- >90% SDS-PAGE
- Expression system
- Baculovirus infected Sf9 cells
- Tags
- GST tag N-Terminus
- Applications
- SDS-PAGE, FuncS
- Biologically active
- Yes
- Biological activity
- The specific acivity of ab268540 was 34 nmol/min/mg in a kinase assay using myelin basic protein as substrate.
- Accession
- Q9EQY0-1
- Animal free
- No
- Species
- Mouse
- Concentration
- Storage buffer
pH: 7.5
Constituents: 25% Glycerol (glycerin, glycerine), 0.87% Sodium chloride, 0.79% Tris HCl, 0.31% Glutathione, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.003% EDTA, 0.002% PMSF
Sequence info
Amino acid sequence
- S V H Q Q R Q L Q H Q Q F Q K E L E K I Q L L Q Q Q Q L P F H P H G D L T Q D P E F L D S S G P F S E S S G T S S P S P S P R A S N H S L H P S S S A S R A G T S P S L E Q D D E D E E T R M V I V G K I S F C P K D V L G H G A E G T I V Y K G M F D N R D V A V K R I L P E C F S F A D R E V Q L L R E S D E H P N V I R Y F C T E K D R Q F Q Y I A I E L C A A T L Q E Y V E Q K D F A H L G L E P I T L L H Q T T S G L A H L H S L N I V H R D L K P H N I L L S M P N A H G R I K A M I S D F G L C K K L A V G R H S F S R R S G V P G T E G W I A P E M L S E D C K D N P T Y T V D I F S A G C V F Y Y V I S E G N H P F G K S L Q R Q A N I L L G A C N L D C F H S D K H E D V I A R E L I E K M I A M D P Q Q R P S A K H V L K H P F F W S L E K Q L Q F F Q D V S D R I E K E A L D G P I V R Q L E R G G R A V V K M D W R E N I T V P L Q T D L R K F R T Y K G G S V R D L L R A M R N K K H H Y R E L P V E V Q E T L G S I P D D F V R Y F T S R F P H L L S H T Y Q A M E L C R H E R L F Q T Y Y W H E P T E P Q P P V I P Y A L
- Accession
- Q9EQY0
- Protein length
- Fragment
- Amino acids
- 469 to 977
- Nature
- Recombinant
- Tags
- GST tag N-Terminus
Specifications
- Form
- Liquid
- Additional notes
Affinity purified.
General info
- Function
Serine/threonine-protein kinase and endoribonuclease that acts as a key sensor for the endoplasmic reticulum unfolded protein response (UPR) (PubMed:11850408, PubMed:25164867). In unstressed cells, the endoplasmic reticulum luminal domain is maintained in its inactive monomeric state by binding to the endoplasmic reticulum chaperone HSPA5/BiP. Accumulation of misfolded protein in the endoplasmic reticulum causes release of HSPA5/BiP, allowing the luminal domain to homodimerize, promoting autophosphorylation of the kinase domain and subsequent activation of the endoribonuclease activity (PubMed:25164867). The endoribonuclease activity is specific for XBP1 mRNA and excises 26 nucleotides from XBP1 mRNA (PubMed:11850408, PubMed:25164867). The resulting spliced transcript of XBP1 encodes a transcriptional activator protein that up-regulates expression of UPR target genes (PubMed:11850408, PubMed:25164867). Acts as an upstream signal for ER stress-induced GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of CFTR to cell membrane by modulating the expression and localization of SEC16A (By similarity).
- Sequence similarities
Belongs to the protein kinase superfamily. Ser/Thr protein kinase family.
- Post-translational modifications
Autophosphorylated following homodimerization. Autophosphorylation promotes activation of the endoribonuclease domain (PubMed:25164867). In response to ER stress, phosphorylated at Ser-724, Ser-729 and possibly Ser-726; phosphorylation promotes oligomerization and endoribonuclease activity (PubMed:30118681). Dephosphorylated at Ser-724, Ser-729 and possibly Ser-726 by RPAP2 to abort failed ER-stress adaptation and trigger apoptosis (By similarity).
Storage
- Shipped at conditions
- Dry Ice
- Appropriate short-term storage conditions
- -80°C
- Appropriate long-term storage conditions
- -80°C
- Aliquoting information
- Upon delivery aliquot
- Storage information
- Avoid freeze / thaw cycle
This product is an active protein and may elicit a biological response in vivo, handle with caution.
Supplementary info
- This supplementary information is collated from multiple sources and compiled automatically.
- Activity summary
The inositol-requiring enzyme 1 (IRE1) also known as ERN1 or IRE1 alpha is a critical endoplasmic reticulum (ER) stress sensor. It has a molecular weight of approximately 110 kDa. IRE1 is expressed in various cell types and tissues particularly in those subject to a high degree of protein synthesis such as the liver pancreas and secretory cells. This protein plays a dual role as both a RNase and a kinase which enables it to respond swiftly to misfolded proteins accumulating in the ER.
- Biological function summary
IRE1 is an important regulator in the unfolded protein response (UPR) a cellular reaction to stress in the ER. It operates as part of a complex mechanism facilitating the splicing of X-box binding protein 1 (XBP1) mRNA which results in the production of a potent transcription factor. IRE1 activity helps in restoring normal function of the cell by upregulating genes involved in protein folding secretion and degradation. Its actions are important for maintaining cellular homeostasis during stressful conditions.
- Pathways
IRE1 is an integral component of the UPR pathway which works to alleviate ER stress. It interacts closely with other UPR transducers such as activating transcription factor 6 (ATF6) and protein kinase RNA-like ER kinase (PERK). IRE1 connects with the XBP1 pathway facilitating adaptive responses that enhance protein-folding capacity lipid biosynthesis and ER-associated degradation. Altogether these pathways mediate cell survival or apoptosis depending on the severity of the stress.
- Associated diseases and disorders
IRE1 has significant involvement in conditions like diabetes and cancer. In the context of diabetes improper UPR signaling due to chronic ER stress leads to insulin resistance and pancreatic beta-cell dysfunction. In cancer IRE1 modulates tumor microenvironment and promotes cancer cell survival under hypoxic conditions. The XBP1 pathway linked with IRE1 also plays a substantial role in these diseases by influencing cell proliferation and apoptosis. Understanding the mechanisms of IRE1 in these conditions might provide therapeutic insights.
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2 product images
Functional Studies - Recombinant mouse IRE1 protein (Active) (ab268540)
The specific acivity of ab268540 was 34 nmol/min/mg in a kinase assay using myelin basic protein as substrate.
SDS-PAGE - Recombinant mouse IRE1 protein (Active) (ab268540)
SDS-PAGE analysis of ab268540.
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