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10850

Millipore

D-(−)-Arabinose

suitable for microbiology, ≥99.0%

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About This Item

Empirical Formula (Hill Notation):
C5H10O5
CAS Number:
Molecular Weight:
150.13
Beilstein:
1723079
EC Number:
MDL number:
UNSPSC Code:
41106212
PubChem Substance ID:
NACRES:
NA.85

Pricing and availability is not currently available.

Quality Level

Assay

≥99.0% (sum of enantiomers, HPLC)
≥99.0%

form

powder

optical activity

[α]20/D −104±2.0°, 24 hr, c = 10% in H2O

ign. residue

≤0.1% (as SO4)

loss

≤0.1% loss on drying, 20 °C (HV)

mp

162-164 °C (lit.)

anion traces

chloride (Cl-): ≤50 mg/kg
sulfate (SO42-): ≤50 mg/kg

cation traces

As: ≤0.1 mg/kg
Ca: ≤500 mg/kg
Cd: ≤5 mg/kg
Co: ≤5 mg/kg
Cr: ≤5 mg/kg
Cu: ≤25 mg/kg
Fe: ≤17 mg/kg
K: ≤50 mg/kg
Mg: ≤10 mg/kg
Mn: ≤5 mg/kg
Na: ≤50 mg/kg
Ni: ≤5 mg/kg
Pb: ≤5 mg/kg
Zn: ≤15 mg/kg

application(s)

microbiology

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1 of 4

This Item
A3131PHR210010839
Quality Level

200

Quality Level

200

Quality Level

300

Quality Level

100

form

powder

form

powder

form

-

form

powder

mp

162-164 °C (lit.)

mp

162-164 °C (lit.)

mp

162-164 °C (lit.)

mp

155-159 °C, 160-163 °C (lit.)

cation traces

As: ≤0.1 mg/kg, Cd: ≤5 mg/kg, Cr: ≤5 mg/kg, Fe: ≤17 mg/kg, Mg: ≤10 mg/kg, Na: ≤50 mg/kg, Pb: ≤5 mg/kg

cation traces

-

cation traces

-

cation traces

Al: ≤5 mg/kg, As: ≤0.1 mg/kg, Ba: ≤5 mg/kg, Bi: ≤5 mg/kg, Ca: ≤200 mg/kg, Cd: ≤5 mg/kg, Co: ≤5 mg/kg, Cr: ≤5 mg/kg, Cu: ≤5 mg/kg, Fe: ≤5 mg/kg, K: ≤50 mg/kg, Li: ≤5 mg/kg, Mg: ≤5 mg/kg, Mn: ≤5 mg/kg, Mo: ≤5 mg/kg, Na: ≤50 mg/kg, Ni: ≤5 mg/kg, Pb: ≤5 mg/kg, Sr: ≤5 mg/kg, Zn: ≤5 mg/kg

optical activity

[α]20/D −104±2.0°, 24 hr, c = 10% in H2O

optical activity

[α]20/D -105 to -103 °, c = 4% (w/v) in water

optical activity

-

optical activity

[α]20/D +104.0±2.0°, 24 hr, c = 10% in H2O

General description

D-Arabinose is a rare aldopentose, and is rarely utilized by enteric bacteria as a source of carbon and energy. It is also found in the aloins of the plant genus Aloe and as a constituent of the polysaccharide of the bacterial genus Mycobacterium. Some of the enteric bacteria like Escherichia coli K-12 can mutate to utilize D-arabinose.[1]

Application

D-(-)-Arabinose has been used as an inducer of λ-RED recombinant gene expression.[2]

Biochem/physiol Actions

D-Arabinose is a reducing sugar. It is a pentose analog of D-ribose that is a constituent of mycobacterial cell wall arabinogalactans. It is also a substrate for D-erythroascorbic acid synthesis in yeast.

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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    The Evolution of Metabolic Function.
    Mortlock RP.
    Science, 16-17 (1992)
    Engineering complex biological systems in bacteria through recombinase-assisted genome engineering.
    Santos CN and Yoshikuni Y2
    Nature Protocols, 9, 1320-1336 (2014)
    A Hasegawa et al.
    Carbohydrate research, 52, 137-149 (1976-12-01)
    Prumycin (1) and related compounds have been synthesized from benzyl 2-(benzyloxycarbonyl)amino-2-deoxy-5,6-O-isopropylidene-beta-D-glucofuranoside (4). Benzoylation of 4, followed by deisopropylidenation, gave benzyl 3-O-benzoyl-2-(benzyloxycarbonyl)amino-2-deoxy-beta-D-glucofuranoside (6), which was converted, via oxidative cleavage at C-5-C-6 and subsequent reduction, into the related benzyl beta-D-xylofuranoside derivative (7).
    Nobuhiro Yamagata et al.
    Proceedings of the National Academy of Sciences of the United States of America, 112(2), 578-583 (2014-12-31)
    Drosophila melanogaster can acquire a stable appetitive olfactory memory when the presentation of a sugar reward and an odor are paired. However, the neuronal mechanisms by which a single training induces long-term memory are poorly understood. Here we show that
    Agustina Llanos et al.
    Microbial cell factories, 18(1), 14-14 (2019-01-30)
    Research on filamentous fungi emphasized the remarkable redundancy in genes encoding hydrolytic enzymes, the similarities but also the large differences in their expression, especially through the role of the XlnR/XYR1 transcriptional activator. The purpose of this study was to evaluate

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