R3251
D-Ribulose-5-phosphate 3-Epimerase from baker′s yeast (S. cerevisiae)
lyophilized powder, 50-100 units/mg protein (modified Warburg-Christian)
Autenticatiper visualizzare i prezzi riservati alla tua organizzazione & contrattuali
About This Item
Numero CAS:
Numero MDL:
Codice UNSPSC:
12352204
Prodotti consigliati
Origine biologica
bakers yeast
Stato
lyophilized powder
Attività specifica
50-100 units/mg protein (modified Warburg-Christian)
Attività estranea
phosphoriboisomerase, alcohol dehydrogenase, transketolase, and transaldolase <0.1%
Temperatura di conservazione
−20°C
Applicazioni
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.
Azioni biochim/fisiol
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].
Definizione di unità
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.
Stato fisico
Lyophilized and essentially sulfate-free; contains approx. 35% citrate buffer salts
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Dispositivi di protezione individuale
Eyeshields, Gloves, type N95 (US)
Scegli una delle versioni più recenti:
Possiedi già questo prodotto?
I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.
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
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
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
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
Filtri attivi
Il team dei nostri ricercatori vanta grande esperienza in tutte le aree della ricerca quali Life Science, scienza dei materiali, sintesi chimica, cromatografia, discipline analitiche, ecc..
Contatta l'Assistenza Tecnica.
