N3627

4-Nitrophenyl stearate

Name: 4-Nitrophenyl stearate
Brand: SIGMA
Price: 414 USD

lipase substrate

Synonym(s):

4-Nitrophenyl octadecanoate, Octadecanoic acid 4-nitrophenyl ester

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1 G

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About This Item

Empirical Formula (Hill Notation):

C₂₄H₃₉NO₄

CAS Number:

14617-86-8

Molecular Weight:

405.57

Beilstein/REAXYS Number:

2013000

MDL number:

MFCD00047733

UNSPSC Code:

12352204

PubChem Substance ID:

24897653

NACRES:

NA.83

Key Documents

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Quality Level

200

assay

≥90% (TLC)

form

powder

solubility

chloroform: 100 mg/mL, clear to slightly hazy, colorless to light yellow

storage temp.

−20°C

SMILES string

CCCCCCCCCCCCCCCCCC(=O)Oc1ccc(cc1)[N+]([O-])=O

InChI

1S/C24H39NO4/c1-2-3-4-5-6-7-8-9-10-11-12-13-14-15-16-17-24(26)29-23-20-18-22(19-21-23)25(27)28/h18-21H,2-17H2,1H3

InChI key

HAIZAZONHOVLEK-UHFFFAOYSA-N

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This Item	N0252	70124	61716
Sigma-Aldrich N3627 4-Nitrophenyl stearate	Sigma-Aldrich N0252 4-Nitrophenyl decanoate	Sigma-Aldrich 70124 4-Nitrophenyl myristate	Sigma-Aldrich 61716 4-Nitrophenyl dodecanoate
assay ≥90% (TLC)	assay ≥98% (TLC)	assay ≥95.0% (HPLC)	assay ≥98.0% (GC)
solubility chloroform: 100 mg/mL, clear to slightly hazy, colorless to light yellow	solubility chloroform: soluble 100 mg/mL, colorless to faintly yellow	solubility chloroform: 50 mg/mL, clear to very slightly hazy, colorless to dark yellow	solubility chloroform: 1 g/10 mL, clear, colorless to faintly greenish-yellow
Quality Level 200	Quality Level 200	Quality Level 100	Quality Level 100
form powder	form powder	form powder	form -
storage temp. −20°C	storage temp. −20°C	storage temp. −20°C	storage temp. 2-8°C

pictograms

GHS07

signalword

Warning

hcodes

H317

pcodes

P280

Hazard Classifications

Skin Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

dust mask type N95 (US), Eyeshields, Faceshields, Gloves

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Atypical organic-solvent tolerant bacterial hormone sensitive lipase-like homologue EstAG1 from Staphylococcus saprophyticus AG1: Synthesis and characterization.

Alisa Gricajeva et al.

International journal of biological macromolecules, 130, 253-265 (2019-02-24)

Biocatalysts exerting activity against ester bonds have a broad range of applications in modern biotechnology. Some of the most industrially relevant enzymes of this type are lipolytic and their market is predicted to uphold leadership up till 2024. In this

Covalent immobilization of a halophilic, alkalithermostable lipase LipR2 on Florisil® nanoparticles for production of alkyl levulinates.

Noha M Mesbah

Archives of biochemistry and biophysics, 667, 22-29 (2019-04-26)

A novel halophilic, alkalithermostable lipase LipR2 from Alkalispirillum sp. NM-ROO2 was cloned and expressed. LipR2 was covalently immobilized on Florisil® functionalized with glutaraldehyde. Protein binding efficiency of functionalized Florisil® was 94.7%. Immobilized LipR2 retained 97.5% of specific activity of the

Identification and Characterization of a Novel Thermostable GDSL-Type Lipase from Geobacillus thermocatenulatus.

Eunhye Jo et al.

Journal of microbiology and biotechnology, 31(3), 483-491 (2021-02-25)

Two putative genes, lip29 and est29, encoding lipolytic enzymes from the thermophilic bacterium Geobacillus thermocatenulatus KCTC 3921 were cloned and overexpressed in Escherichia coli. The recombinant Lip29 and Est29 were purified 67.3-fold to homogeneity with specific activity of 2.27 U/mg

Enhanced expression of lipase I from Galactomyces geotrichum by codon optimisation in Pichia pastoris.

Hanzhen Qiao et al.

Protein expression and purification, 138, 34-45 (2017-06-07)

Relatively poor heterologous protein yields have limited the commerical applications of Galactomyces geotrichum lipase I (GGl I) efficacy trials. To address this, we have redesigned the GGl I gene to preferentially match codon frequencies of Pichia pastoris (P. pastoris) while retaining

Optimisation of combi-lipases from Aspergillus niger for the synergistic and efficient hydrolysis of soybean oil.

Hanzhen Qiao et al.

Animal science journal = Nihon chikusan Gakkaiho, 88(5), 772-780 (2016-10-06)

The enzymatic properties of four lipases (A, B, C and D) from different strains of Aspergillus niger, were investigated, and a 3-factor mixture design and triangular surface analysis were performed to screen the optimal combi-lipase by observing synergistic effects. Lipases

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4-Nitrophenyl stearate