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PRKR-like Endoplasmic Reticulum Kinase Antikörper

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PRKR-like Endoplasmic Reticulum Kinase

Synonyme Pek, Perk, AI427929
Klonalität Polyklonal
Wirt

Kaninchen

Reaktivität

Maus, Human, Ratte (Rattus)

Applikation
Immunhistochemie (IHC), ELISA, Western Blot (WB), Immunpräzipitation (IP)
1 Publikation vorhanden
Produktnummer ABIN233768
Menge 100ul  (85 mg/ml (by Refractometry))
Preis 315,11 €   Zzgl. Versandkosten €20,00 und MWSt
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Verfügbarkeit Lieferung in 5 Werktagen

Produktbeschreibung

Weitere Bezeichnung PKR-like Endoplasmic Reticulum Kinase (PERK)
Gen-ID AAH54809
Swiss-Prot Q9Z2B5
Immunogen This whole rabbit serum was prepared by repeated immunizations with a recombinant fusion protein from amino acids 601-1115 of mouse deltaN PERK (see link below for the full length sequence of the mouse gene product).
Format Liquid (sterile filtered)
Beschreibung The PKR-like endoplasmic reticulum kinase (PERK, also know as Eukaryotic translation initiation factor 2-alpha kinase 3) is a type I transmembrane protein localized to the endoplasmic reticulum (ER). PERK consists of an N-terminal ER luminal domain, a membrane-spanning region, and a cytosolic C-terminal serine/threonine kinase domain (1). The luminal domain of PERK is bound to the ER chaperone GRP78 in unstressed cells (2). PERK activation occurs upon accumulation of misfolded proteins and the ER lumen, which triggers GRP78 dissociation from PERK thereby allowing PERK dimerization and autophosphorylation (3, 4). PERK phosphorylates two established targets: the eukaryotic translation initiation factor 2 alpha (eIF2 alpha , (1)) and the Nrf2 transcription factor (5). Phosphorylation of eIF2 alpha results in attenuation of translation initiation (6). The translational block also contributes to cell cycle arrest due to loss of the G1 regulatory protein, cyclin D1 (7). PERK-dependent phosphorylation of Nrf2 promotes transcription of phase II detoxifying enzymes which is critically important for elimination of intracellular reactive oxygen species (8). Thus, while inhibiting new protein synthesis and thereby decreasing the ER protein load PERK simultaneously induces expression of genes that help restore cellular redox homeostasis and promote survival.
Spezifität This antiserum is directed against PERK and reacts with the PERK from mouse tissues. Reactivity to other species is unknown.

Anwendungen

Applikationshinweise Recommended Dilutions: IMMUNOPRECIPITATION 10-30ul WESTERN BLOT 1:500 to 1:3000 IF MICROSCOPY User Optimized OTHER APPLICATIONS User Optimized. Note: ): This antiserum has been tested for use in western blotting, immunoprecipitation and immunohistochemistry. Specific conditions for reactivity should be optimized by the end user. Expect bands approximately 150kDa by western blotting in the appropriate cell lysate or extract.
Konzentration 85 mg/ml (by Refractometry)
Buffer Stabilizer: None. Preservative: 0.01% (w/v) Sodium Azide. Buffer: 0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2.
Lagerung Store vial at -20° C or below prior to opening. Dilute only prior to immediate use. Aliquot contents and freeze at -20° C or below. Avoid cycles of freezing and thawing. Expiration date is six (6) months from date of opening product. Figure 1. Western blot analysis using Immuno-chemicals anti-PERK to detect PERK in cell lysates. 300ug PERK over-expressing 293T cell lysate (lanes 1 & 2), or 800ug wild type (Lanes 3 & 4), and PERK knock out (lanes 5 & 6) MEF cell lysate were immunoprecipated with 15ul anti-PERK, followed by immunobloting with 1:1000 dilution of anti-PERK in 5% milk/TBST buffer. Lane 1, 293T cells over-expressing Myc-PERK wt, Lane 2 , 293T cells over-expressing Myc-PERK K618A. Personal Communication. A, Diehl, Univ. of Pennsylvania, Philadelphia, PA. wt MEFKO MEF-+ -+ (2 µg/ml Tunic)1 2 3 4 5 6wt MEFKO MEF-+ -+ (2 µg/ml Tunic)1 2 3 4 5 6
Beschränkungen Nur für Forschungszwecke einsetzbar

Publikationen

Publikationen Huang, Wu, Chen et al.: "Aquatic birnavirus-induced ER stress-mediated death signaling contribute to downregulation of Bcl-2 family proteins in salmon embryo cells." in: PLoS ONE, Vol. 6, Issue 8, pp. e22935, 2011 (PubMed).