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この商品について
化学式:
Na2HPO4 · 2H2O
CAS番号:
分子量:
177.99
PubChem Substance ID:
UNSPSC Code:
12161700
NACRES:
NA.25
EC Number:
231-448-7
MDL number:
Assay:
98.5-101% (calc. to the dried substance)
Form:
crystals
Quality Level
agency
meets analytical specifications of BP, meets analytical specifications of Ph. Eur.
assay
98.5-101% (calc. to the dried substance)
form
crystals
quality
meets analytical specification of Ph. Eur., BP
impurities
reducing matter, complies, residual solvents, complies, ≤0.001% heavy metals (as Pb), ≤1% NaH2PO4 (calc. to dried subst.)
loss
19.5-21% loss on drying, 130 °C
pH
9.0-9.4 (20 °C, 1%)
anion traces
chloride (Cl-): ≤50 mg/kg, sulfate (SO42-): ≤100 mg/kg
cation traces
As: ≤2 mg/kg, Fe: ≤10 mg/kg
suitability
complies for appearance of solution
SMILES string
O.O.[Na+].[Na+].OP([O-])([O-])=O
InChI
1S/2Na.H3O4P.2H2O/c;;1-5(2,3)4;;/h;;(H3,1,2,3,4);2*1H2/q2*+1;;;/p-2
InChI key
KDQPSPMLNJTZAL-UHFFFAOYSA-L
Application
Sodium phosphate dibasic dihydrate has been used for isolating DNA and RNA from bacterial samples of human gastrointestinal (GI) tract.
Biochem/physiol Actions
Sodium phosphate dibasic dihydrate is an important component of running buffer of denaturing gel electrophoresis.
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保管分類
13 - Non Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Erwin G Zoetendal et al.
Nature protocols, 1(2), 954-959 (2007-04-05)
The human gastrointestinal (GI) tract contains a complex microbial community that consists of numerous uncultured microbes. Therefore, nucleic-acid-based approaches have been introduced to study microbial diversity and activity, and these depend on the proper isolation of DNA, rRNA and mRNA.
Erwin G Zoetendal et al.
Nature protocols, 1(2), 870-873 (2007-04-05)
The human gastrointestinal (GI) tract contains a complex microbial community that develops in time and space. The most widely used approaches to study microbial diversity and activity are all based on the analysis of nucleic acids, DNA, rRNA and mRNA.
Sohini Mukherjee et al.
Nature communications, 6, 8467-8467 (2015-10-13)
Creating an artificial functional mimic of the mitochondrial enzyme cytochrome c oxidase (CcO) has been a long-term goal of the scientific community as such a mimic will not only add to our fundamental understanding of how CcO works but may