815-91-8 Usage
Uses
Used in Biochemical Research:
Sedoheptulose 1,7-bisphosphate is utilized as a biochemical marker for studying the Calvin cycle and the mechanisms of photosynthesis. It aids researchers in understanding the complex processes involved in the conversion of light energy into chemical energy within plants.
Used in Agricultural Applications:
In agriculture, sedoheptulose 1,7-bisphosphate can be used as a component in the development of genetically modified crops with enhanced photosynthetic efficiency. This could potentially lead to increased crop yields and improved resistance to environmental stressors.
Used in Pharmaceutical Industry:
Sedoheptulose 1,7-bisphosphate may be employed as a therapeutic agent in the development of drugs targeting metabolic disorders related to glucose metabolism. Its role in the Calvin cycle could provide insights into the regulation of glucose production and utilization in the human body.
Used in Environmental Science:
In environmental science, sedoheptulose 1,7-bisphosphate can be studied to understand the impact of climate change and other environmental factors on the efficiency of photosynthesis. This knowledge can contribute to the development of strategies for mitigating the effects of environmental stress on plant growth and productivity.
Check Digit Verification of cas no
The CAS Registry Mumber 815-91-8 includes 6 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 3 digits, 8,1 and 5 respectively; the second part has 2 digits, 9 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 815-91:
(5*8)+(4*1)+(3*5)+(2*9)+(1*1)=78
78 % 10 = 8
So 815-91-8 is a valid CAS Registry Number.
InChI:InChI=1/C7H16O13P2/c8-3(1-19-21(13,14)15)5(10)7(12)6(11)4(9)2-20-22(16,17)18/h3,5-8,10-12H,1-2H2,(H2,13,14,15)(H2,16,17,18)/t3-,5-,6-,7-/m1/s1
815-91-8Relevant academic research and scientific papers
Tamoi, Masahiro,Nagaoka, Miki,Shigeoka, Shigeru
, p. 848 - 851 (2005)
Here we report on the production of functional recombinant SBPase of Chlamydomonas sp. W80 in Escherichia coli and the one-step purification of a polyhistidine-tagged fusion protein. The polyclonal antibody was raised against purified recombinant enzyme and cross-reacted with crude SBPase from Chlamydomonas, spinach, tobacco, and Arabidopsis leaves. Further, we investigated the levels of protein and activity of SBPase in different tissues of Arabidopsis plants.
