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Zitierungen und Referenzen (5)
Invitrogen™
Pro-Q™ Diamond Phosphoprotein Blot Stain Kit
Das Pro-Q Diamond Phosphoprotein-Blot-Färbekit bietet eine schnelle und einfache Methode zum direkten Nachweis von Phosphoproteinen auf Polyvinylidendifluorid- (PVDF) oder Nitrozellulose-Membranen.Weitere Informationen
| Katalognummer | Menge |
|---|---|
| P33356 | 1 Kit |
Katalognummer P33356
Preis (EUR)
596,00
Each
Menge:
1 Kit
Preis (EUR)
596,00
Each
Das Pro-Q Diamond Phosphoprotein-Blot-Färbekit bietet eine schnelle und einfache Methode zum direkten Nachweis von Phosphoproteinen auf Polyvinylidendifluorid- (PVDF) oder Nitrozellulose-Membranen. Die fluoreszierende Färbung bindet selektiv an den Phosphat-Anteil und ist unabhängig vom Aminosäure-Sequenzkontext. Da es sich um ein direktes Färbemittel handelt, benötigen Sie keine teuren Antikörper oder Radioisotope. Das Pro-Q Diamond Phosphoprotein-Blot-Färbekit kann zur Analyse des nativen Phosphorylierungszustands von Proteinen verwendet werden, die aus Gewebeproben oder Körperflüssigkeiten gewonnen werden.
Nur für Forschungszwecke. Nicht zur Verwendung bei diagnostischen Verfahren.
Specifications
DetektionsstelleIn-Blot-Nachweis
NachweisverfahrenFluoreszent
Menge1 Kit
Haltbarkeit6 Monate
ZielmolekülProteine (Phosphoproteine)
Marker oder FarbstoffPro-Q Diamond
ProduktliniePRO-Q
ProdukttypPhosphoprotein-Blot-Färbekit
Unit SizeEach
Zitierungen und Referenzen (5)
Zitierungen und Referenzen
Abstract
The human mitochondrial transcription termination factor (mTERF) is fully active in vitro in the non-phosphorylated form.
Journal:J Biol Chem
PubMed ID:15899902
'The human mitochondrial transcription termination factor (mTERF) is a 39-kDa protein that terminates transcription at the 3''-end of the 16 S rRNA gene and thereby controls expression of the ribosomal transcription unit of mitochondrial DNA. The transcription termination activity of human mTERF has been notoriously difficult to study in vitro,
Ca(2+)-related signaling and protein phosphorylation abnormalities play central roles in a new experimental model of electrical storm.
Journal:Circulation
PubMed ID:21555709
Electrical storm (ES), characterized by recurrent ventricular tachycardia/fibrillation, typically occurs in implantable cardioverter-defibrillator patients and adversely affects prognosis. However, the underlying molecular basis is poorly understood. In the present study, we report a new experimental model featuring repetitive episodes of implantable cardioverter-defibrillator firing for recurrent ventricular fibrillation (VF), in which
Pin1 promotes histone H1 dephosphorylation and stabilizes its binding to chromatin.
Journal:
PubMed ID:24100296
Histone H1 plays a crucial role in stabilizing higher order chromatin structure. Transcriptional activation, DNA replication, and chromosome condensation all require changes in chromatin structure and are correlated with the phosphorylation of histone H1. In this study, we describe a novel interaction between Pin1, a phosphorylation-specific prolyl isomerase, and phosphorylated
Quantitative analysis of protein phosphorylation status and protein kinase activity on microarrays using a novel fluorescent phosphorylation sensor dye.
Journal:Proteomics
PubMed ID:12872225
Ultrasensitive detection of minute amounts of phosphorylated proteins and peptides is a key requirement for unraveling many of the most important signal transduction pathways in mammalian systems. Protein microarrays are potentially useful tools for sensitive screening of global protein expression and post-translational modifications, such as phosphorylation. However, the analysis of
Detection of phosphoproteins on electroblot membranes using a small-molecule organic fluorophore.
Journal:Electrophoresis
PubMed ID:15300773
A new formulation of the small-molecule organic fluorophore, Pro-Q Diamond dye, has been developed that permits rapid and simple detection of phosphoproteins directly on polyvinylidene difluoride (PVDF) or nitrocellulose membranes (electroblots). Protein samples are first separated by electrophoresis and then electroblotted to membranes, stained and destained, in an analogous manner