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11149

Sigma-Aldrich

L-Asparagine

BioUltra, ≥99.5% (NT)

Synonym(s):

(S)-2-Aminosuccinic acid 4-amide, L-Aspartic acid 4-amide

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About This Item

Linear Formula:
H2NCOCH2CH(NH2)CO2H
CAS Number:
70-47-3
Molecular Weight:
132.12
Beilstein/REAXYS Number:
1723527
EC Number:
200-735-9
MDL number:
MFCD00064401
UNSPSC Code:
12352200
eCl@ss:
32160406
PubChem Substance ID:
24847033

product line

BioUltra

assay

≥99.5% (NT)

optical activity

[α]20/D +35.0±0.5°, c = 5% in 5 M HCl

impurities

insoluble matter, passes filter test
≤1% foreign amino acids

ign. residue

≤0.05% (as SO4)

pH

4.0-5.5 (25 °C, 0.1 M in H2O)

mp

235 °C (dec.) (lit.)

solubility

H2O: 0.1 M at 20 °C, clear, colorless

anion traces

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

cation traces

Al: ≤5 mg/kg
As: ≤0.1 mg/kg
Ba: ≤5 mg/kg
Bi: ≤5 mg/kg
Ca: ≤50 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: ≤50 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

λ

0.1 M in H2O

UV absorption

λ: 260 nm Amax: 0.07
λ: 280 nm Amax: 0.06

SMILES string

N[C@@H](CC(N)=O)C(O)=O

InChI

1S/C4H8N2O3/c5-2(4(8)9)1-3(6)7/h2H,1,5H2,(H2,6,7)(H,8,9)/t2-/m0/s1

InChI key

DCXYFEDJOCDNAF-REOHCLBHSA-N

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Other Notes

As spacer in isotachophoresis[1][2]; Growth requirement of various microorganisms[3].

Storage Class

13 - Non Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

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Certificates of Analysis (COA)

Lot/Batch Number
BCBB5642
1371739
1410830

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P.W. Lange
Anal. Chem. Symp. Ser., 5, 187-187 (1980)
CRC Handbook of Microbiology, 4, 1-1 (1974)
T. Yagi et al. et al.
Electrophoresis ?83, 503-503 (1984)
Christopher E Berndsen et al.
Nature chemical biology, 9(3), 154-156 (2013-01-08)
It is widely accepted that ubiquitin-conjugating enzymes contain an active site asparagine that serves as an oxyanion hole, thereby stabilizing a negatively charged transition state intermediate and promoting ubiquitin transfer. Using structural and biochemical approaches to study the role of
Halina R Novak et al.
The FEBS journal, 280(7), 1664-1680 (2013-02-07)
The putative L-haloacid dehalogenase gene (DehRhb) from a marine Rhodobacteraceae family was cloned and overexpressed in Escherichia coli. The DehRhb protein was shown to be an L-haloacid dehalogenase with highest activity towards brominated substrates with short carbon chains (≤ C3).
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Chromatograms

application for HPLC

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