Skip to Content
Merck
CN

83895

D-Ribulose 1,5-bisphosphate sodium salt hydrate

≥99.0% (TLC)

Synonym(s):

D-erythro-2-Pentulose, 1,5-bis(dihydrogen phosphate), D-Ribulose 1,5-diphosphate, RuDP

Sign In to View Organizational & Contract Pricing.

Select a Size

About This Item

Empirical Formula (Hill Notation):
C5H12O11P2 · xNa+ · yH2O
CAS Number:
1897433-92-9
Molecular Weight:
310.09 (anhydrous free acid basis)
MDL number:
MFCD35146021
UNSPSC Code:
12352201
NACRES:
NA.25

Key Documents

View All Documentation
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist

Product Name

D-Ribulose 1,5-bisphosphate sodium salt hydrate, ≥99.0% (TLC)

SMILES string

[P](=O)(OC[C@@H](O)[C@@H](O)C(=O)CO[P](=O)(O)O)(O)O

InChI

1S/C5H12O11P2/c6-3(1-15-17(9,10)11)5(8)4(7)2-16-18(12,13)14/h3,5-6,8H,1-2H2,(H2,9,10,11)(H2,12,13,14)/t3-,5-/m1/s1

InChI key

YAHZABJORDUQGO-NQXXGFSBSA-N

assay

≥99.0% (TLC)

form

powder

color

white

solubility

H2O: 50 mg/mL, clear, colorless to light yellow

storage temp.

−20°C

Quality Level

100

Looking for similar products? Visit Product Comparison Guide

Related Categories

Application

Ribulose-1,5-bisphosphate (RuBP) is a component of the Calvin cycle that is metabolized into glycerate 3-phosphate (G3P) by the enzyme ribulose bisphosphate carboxylase/oxygenase (RuBisCO). RuBP is used to identify, differentiate and characterize ribulose bisphosphate carboxylase(s)/oxygenase(s) (RuBisCO).

Other Notes

Active site studies with ribulose-1,5-biphosphate carboxylase
To gain a comprehensive understanding of our extensive range of Monosaccharides for your research, we encourage you to visit our Carbohydrates Category page.

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Faceshields, Gloves, type P2 (EN 143) respirator cartridges

Regulatory Information

涉药品监管产品
This item has

Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number
BCCM9619
BCCM8599
BCCM7953
BCCL9302
BCCK4544

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Search for a COA

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

S N Mogel et al.
Biochemistry, 28(13), 5428-5431 (1989-06-27)
Irradiation of ribulose-1,5-bisphosphate carboxylase/oxygenase from spinach in the presence of vanadate at 4 degrees C resulted in rapid loss of carboxylase activity. The inactivation was light and vanadate dependent. When the enzyme was irradiated in the presence of the substrate
M Willemoës et al.
Biochemistry, 36(16), 5078-5083 (1997-04-22)
The mechanism of binding of the substrates Mg x ATP and ribose 5-phosphate as well as Mg2+ to the enzyme 5-phospho-D-ribosyl (alpha-1-diphosphate synthetase from Escherichia coli has been analyzed. By use of the competive inhibitors of ATP and ribose 5-phosphate
T Kawaguchi et al.
The Journal of biological chemistry, 276(30), 28554-28561 (2001-05-25)
Macrophages can adapt to the absence of oxygen by switching to anaerobic glycolysis. In this study, we investigated (a) the roles of fructose 2,6-bisphosphate (Fru-2,6-P2) and ribose 1,5-bisphosphate (Rib-1,5-P2), potent activators of phosphofructokinase, (b) the enzymes responsible for the synthesis
Takaaki Sato et al.
Science (New York, N.Y.), 315(5814), 1003-1006 (2007-02-17)
The type III ribulose-1,5-bisphosphate carboxylase-oxygenase (RuBisCO) present in the archaeon Thermococcus kodakaraensis was found to participate in adenosine 5'-monophosphate (AMP) metabolism, a role that is distinct from that of classical RuBisCOs of the Calvin-Benson-Bassham cycle. Genes annotated as thymidine phosphorylase
S Ogushi et al.
The Journal of biological chemistry, 265(19), 10943-10949 (1990-07-05)
The tissue contents of previously known allosteric effectors of brain phosphofructokinase (EC 2.7.1.11) (PFK) and the kinetic behavior of isolated PFK were investigated during the initiation of rapid glycolytic flux in freeze-blown rat brain. Comparing 0- with 5-s brains revealed
View All Related Papers

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service