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>   首页   >   产品   >   一抗   >   精选抗体   >   Mouse Ern1 Antibody (C-term)   

Mouse Ern1 Antibody (C-term)

Affinity Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - Mouse Ern1 Antibody (C-term) AP14250b
    All lanes : Anti-Mouse Ern1 Antibody (C-term) at 1:1000 dilution Lane 1: mouse liver lysate Lane 2: mouse thymus lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 110 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession Q9EQY0
Other Accession NP_076402.1
Reactivity Mouse
Host Rabbit
Clonality Polyclonal
Isotype Rabbit IgG
Calculated MW 110185 Da
Antigen Region 827-855 aa
Additional Information
Gene ID 78943
Other Names Serine/threonine-protein kinase/endoribonuclease IRE1, Endoplasmic reticulum-to-nucleus signaling 1, Inositol-requiring protein 1, Ire1-alpha, IRE1a, Serine/threonine-protein kinase, Endoribonuclease, 3126-, Ern1 {ECO:0000312|MGI:MGI:1930134}
Target/Specificity This Mouse Ern1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 827-855 amino acids from the C-terminal region of mouse Ern1.
Dilution WB~~1:1000
E~~Use at an assay dependent concentration.
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsMouse Ern1 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name Ern1 {ECO:0000312|MGI:MGI:1930134}
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).
Cellular Location Endoplasmic reticulum membrane; Single-pass type I membrane protein
Tissue Location Expressed in liver (at protein level) (PubMed:30118681). Ubiquitously expressed (PubMed:11146108). High levels in thymus, liver and lung. In the brain, preferentially expressed in cortical, hippocampal and olfactory neurons (PubMed:11146108).
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

Ern1 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 XBP1 mRNA to generate a new C-terminus, converting it into a potent unfolded-protein response transcriptional activator and triggering growth arrest and apoptosis.

REFERENCES

Li, H., et al. Proc. Natl. Acad. Sci. U.S.A. 107(37):16113-16118(2010)
Auf, G., et al. Proc. Natl. Acad. Sci. U.S.A. 107(35):15553-15558(2010)
Oikawa, D., et al. FEBS Lett. 584(5):1066-1070(2010)
Yang, L., et al. PLoS ONE 5 (7), E11621 (2010) :
Ghosh, R., et al. PLoS ONE 5 (3), E9575 (2010) :

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