Coomassie Fluor™ Orange Protein Gel Stain (Ready-To-Use Solution)
Citations et références (8)
Invitrogen™
Coomassie Fluor™ Orange Protein Gel Stain (Ready-To-Use Solution)
Le colorant exclusif de gel de protéines Coomassie Fluor Orange de Molecular Probes permet une coloration rapide, simple et sensibleAfficher plus
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Quantité
C33250
1 l
Référence C33250
Prix (EUR)
243,00
Each
Ajouter au panier
Quantité:
1 l
Grand volume ou format personnalisé
Prix (EUR)
243,00
Each
Ajouter au panier
Le colorant exclusif de gel de protéines Coomassie Fluor Orange de Molecular Probes permet une coloration rapide, simple et sensible des protéines séparées par SDS-PAGE. Après l’électrophorèse, le gel est coloré, rincé et photographié. La coloration est terminée en moins d’une heure : aucune étape de fixation ou de décoloration n’est nécessaire, et il n’y a aucun risque de surcoloration du gel. Les protéines colorées peuvent être visualisées à l’aide d’un transilluminateur UV standard de 300 nm ou d’un scanner laser. La coloration par gel de protéines Coomassie Fluor Orange est également disponible au format 5 litres (Réf. n° C-33251).
Usage exclusivement réservé à la recherche. Ne pas utiliser pour des procédures de diagnostic.
Spécifications
Emplacement de détectionDétection sur gel
Méthode de détectionFluorescent
Excitation / émission300, 470/570 nm
Gamme de produitsCoomassie Fluor
Type de produitColoration sur gel des protéines
Quantité1 l
Conditions d’expéditionTempérature ambiante
Molécule cibleProtéine
Marqueur ou colorantCoomassie Fluor Orange
Unit SizeEach
Contenu et stockage
Stocker à température ambiante et à l’abri de la lumière.
Citations et références (8)
Citations et références
Abstract
Molecular mechanism of the inhibitory effect of cobalt ion on thermolysin activity and the suppressive effect of calcium ion on the cobalt ion-dependent inactivation of thermolysin.
Authors:Hashida Y, Inouye K,
Journal:J Biochem
PubMed ID:17405797
'Thermolysin activity in the hydrolysis of N-[3-(2-furyl)acryloyl]-glycyl-l-leucine amide (FAGLA) and FA-l-leucyl-l-alanine amide (FALAA) was examined at various Co(2+) and Ca(2+) concentrations. It decreased to 28% with increasing [Co(2+)] up to 18 mM. The Co(2+)-dependent inactivation was in part suppressed by adding Ca(2+) ion up to 0.5 mM, but 33% of ... More
Covalently dimerized SecA is functional in protein translocation.
Authors:de Keyzer J, van der Sluis EO, Spelbrink RE, Nijstad N, de Kruijff B, Nouwen N, van der Does C, Driessen AJ,
Journal:J Biol Chem
PubMed ID:16115882
'The ATPase SecA provides the driving force for the transport of secretory proteins across the cytoplasmic membrane of Escherichia coli. SecA exists as a dimer in solution, but the exact oligomeric state of SecA during membrane binding and preprotein translocation is a topic of debate. To study the requirements of ... More
Recombinant human immunodeficiency virus type 1 integrase exhibits a capacity for full-site integration in vitro that is comparable to that of purified preintegration complexes from virus-infected cells.
Authors:Sinha S, Grandgenett DP,
Journal:J Virol
PubMed ID:15956566
Retrovirus preintegration complexes (PIC) in virus-infected cells contain the linear viral DNA genome (approximately 10 kbp), viral proteins including integrase (IN), and cellular proteins. After transport of the PIC into the nucleus, IN catalyzes the concerted insertion of the two viral DNA ends into the host chromosome. This successful insertion ... More
Genetic determinants of Silicibacter sp. TM1040 motility.
Authors:Belas R, Horikawa E, Aizawa S, Suvanasuthi R,
Journal:J Bacteriol
PubMed ID:19482930
Silicibacter sp. TM1040 is a member of the marine Roseobacter clade of Alphaproteobacteria that forms symbioses with unicellular eukaryotic phytoplankton, such as dinoflagellates. The symbiosis is complex and involves a series of steps that physiologically change highly motile bacteria into cells that readily form biofilms on the surface of the ... More
Role for leptin in promoting glucose mobilization during acute hyperosmotic stress in teleost fishes.
Authors:Baltzegar DA, Reading BJ, Douros JD, Borski RJ,
Journal:
PubMed ID:24194509
Osmoregulation is critical for survival in all vertebrates, yet the endocrine regulation of this metabolically expensive process is not fully understood. Specifically, the function of leptin in the regulation of energy expenditure in fishes, and among ectotherms, in general, remains unresolved. In this study, we examined the effects of acute ... More