Alle Fotos(1)
Wichtige Dokumente
R3251
D-Ribulose-5-phosphate 3-Epimerase from baker′s yeast (S. cerevisiae)
lyophilized powder, 50-100 units/mg protein (modified Warburg-Christian)
Anmeldenzur Ansicht organisationsspezifischer und vertraglich vereinbarter Preise
Alle Fotos(1)
About This Item
Empfohlene Produkte
Biologische Quelle
bakers yeast
Form
lyophilized powder
Spezifische Aktivität
50-100 units/mg protein (modified Warburg-Christian)
Fremdaktivität
phosphoriboisomerase, alcohol dehydrogenase, transketolase, and transaldolase <0.1%
Lagertemp.
−20°C
Anwendung
D-Ribulose-5-phosphate 3-Epimerase is an enzyme that converts the reversible conversion of D-ribulose 5-phosphate into D-xylulose 5-phosphate, which is important for the cellular response against oxidative stress [1]. D-Ribulose-5-phosphate 3-Epimerase is involved in the pentose phosphate pathway, pentose and glucuronate interconversions and carbon fixation. Product R3251 is from baker′s yeast and is provided as a lyophilized powder. It is useful in enzyme systems requiring low sulfate.
Biochem./physiol. Wirkung
RPE is a metalloenzyme and has been shown to use the divalent Zn2+ ion predominantly for catalysis. Human D-ribulose-5-phosphate 3-epimerase (hRPE) has been shown to use Fe2+ for catalysis [1].
Einheitendefinition
One unit will convert 1 μmole of D-ribulose 5-phosphate to D-xylulose 5-phosphate per min at pH 7.7 at 25°C when coupled with transketolase, α-glycerophosphate dehydrogenase, and triosephosphate isomerase.
Physikalische Form
Lyophilized and essentially sulfate-free; contains approx. 35% citrate buffer salts
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves, type N95 (US)
Hier finden Sie alle aktuellen Versionen:
Besitzen Sie dieses Produkt bereits?
In der Dokumentenbibliothek finden Sie die Dokumentation zu den Produkten, die Sie kürzlich erworben haben.
M Teige et al.
FEBS letters, 377(3), 349-352 (1995-12-27)
A cDNA clone encoding the chloroplast enzyme pentose-5-phosphate 3-epimerase (EC 5.1.3.1) in potato (Solanum tuberosum) was isolated and sequenced. The deduced sequence of 235 amino acids is similar to protein sequences of bacterial epimerases. Northern blot analysis showed the highest
Matthew B Rogers et al.
BMC evolutionary biology, 7, 89-89 (2007-06-15)
Lateral gene transfer is increasingly invoked to explain phylogenetic results that conflict with our understanding of organismal relationships. In eukaryotes, the most common observation interpreted in this way is the appearance of a bacterial gene (one that is not clearly
J Caruthers et al.
Proteins, 62(2), 338-342 (2005-11-24)
The crystal structure of Pfal009167AAA, a putative ribulose 5-phosphate 3-epimerase (PfalRPE) from Plasmodium falciparum, has been determined to 2 A resolution. RPE represents an exciting potential drug target for developing antimalarials because it is involved in the shikimate and the
Kui K Chan et al.
Biochemistry, 47(36), 9608-9617 (2008-08-15)
Enzymes that share the (beta/alpha) 8-barrel fold catalyze a diverse range of reactions. Many utilize phosphorylated substrates and share a conserved C-terminal (beta/alpha) 2-quarter barrel subdomain that provides a binding motif for the dianionic phosphate group. We recently reported functional
Helena Sävenstrand et al.
Plant & cell physiology, 43(4), 402-410 (2002-04-30)
Suppression subtractive hybridisation was used to isolate genes differentially regulated by low levels (UV-B(BE,300) 0.13 W m(-2)) of ultraviolet-B radiation (UV-B; 290-320 nm) in Pisum sativum. Six genes were regulated, two of which were novel. The mRNA levels for these
Active Filters
Unser Team von Wissenschaftlern verfügt über Erfahrung in allen Forschungsbereichen einschließlich Life Science, Materialwissenschaften, chemischer Synthese, Chromatographie, Analytik und vielen mehr..
Setzen Sie sich mit dem technischen Dienst in Verbindung.
