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Principaux documents

N7009

Sigma-Aldrich

2-Nitro-5-thiocyanatobenzoic acid

≥98% (HPLC)

Synonyme(s) :

2-Nitro-5-thiocyanobenzoic acid, NTCB

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About This Item

Formule linéaire :
O2NC6H3(SCN)CO2H
Numéro CAS:
Poids moléculaire :
224.19
Beilstein:
2124001
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352209
ID de substance PubChem :
Nomenclature NACRES :
NA.26

Nom du produit

2-Nitro-5-thiocyanatobenzoic acid, powder

Essai

≥98% (HPLC)

Niveau de qualité

Forme

powder

Couleur

yellow

Pf

156-157 °C (lit.)

Température de stockage

2-8°C

Chaîne SMILES 

OC(=O)c1cc(SC#N)ccc1[N+]([O-])=O

InChI

1S/C8H4N2O4S/c9-4-15-5-1-2-7(10(13)14)6(3-5)8(11)12/h1-3H,(H,11,12)

Clé InChI

NQUNIMFHIWQQGJ-UHFFFAOYSA-N

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Application


  • Site-Specific Conversion of Cysteine in a Protein to Dehydroalanine Using 2-Nitro-5-thiocyanatobenzoic Acid: This research demonstrates the use of 2-Nitro-5-thiocyanatobenzoic acid in protein engineering to modify cysteine residues, which is critical for developing therapeutic proteins and understanding protein structure-function relationships (Qiao et al., 2021).

  • Scrapie prion protein structural constraints obtained by limited proteolysis and mass spectrometry: Highlights the utility of 2-Nitro-5-thiocyanatobenzoic acid in the study of prion proteins, providing insights into protein misfolding diseases which can lead to novel therapeutic approaches (Sajnani et al., 2008).

  • Localization of a substrate binding domain of the human reduced folate carrier to transmembrane domain 11 by radioaffinity labeling and cysteine-substituted accessibility methods: Utilizes 2-Nitro-5-thiocyanatobenzoic acid in biochemical assays to understand transporter proteins, essential for drug delivery and targeting (Hou et al., 2005).

  • A novel procedure for the preparation of biologically active recombinant peptides using a cyanylation reaction: Describes a method using 2-Nitro-5-thiocyanatobenzoic acid for peptide synthesis, beneficial for the development of peptide-based pharmaceuticals (Koyama et al., 1994).

Actions biochimiques/physiologiques

2-nitro-5-thiocyanatobenzoic acid (NTCB) is commonly used to cyanylate and cleave proteins at cysteine residues.

Conditionnement

Bottomless glass bottle. Contents are inside inserted fused cone.

Pictogrammes

Exclamation mark

Mention d'avertissement

Warning

Mentions de danger

Classification des risques

Eye Irrit. 2 - Skin Irrit. 2 - STOT SE 3

Organes cibles

Respiratory system

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

dust mask type N95 (US), Eyeshields, Gloves


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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

R Daniel et al.
The Journal of biological chemistry, 272(43), 26934-26939 (1997-10-27)
Escherichia coli dihydroorotase contains six cysteines/subunit, which are potential ligands of structural and catalytic zinc metals at protein sites of the enzyme. Specific thiol reagents modify, in nondenaturing conditions only, two of these cysteines; these two residues are thought to
J M Litersky et al.
The Biochemical journal, 316 ( Pt 2), 655-660 (1996-06-01)
Phosphorylation of tau protein at Ser-262 has been shown to diminish its ability to bind to taxol-stabilized microtubules. The paired helical filaments (PHFs) found in Alzheimer's disease brain are composed of PHF-tau, which is hyperphosphorylated at multiple sites including Ser-262.
Maya Belghazi et al.
Molecular and cellular endocrinology, 247(1-2), 175-182 (2006-02-07)
Luteinizing hormone (LH) like all other glycoprotein hormones is composed of two dissimilar subunits, alpha and beta, that are non-covalently associated. The heterodimer is stabilized by a region of the beta-subunit called the "seatbelt" because it wraps around the alpha-subunit
J Wu et al.
Analytical biochemistry, 235(2), 161-174 (1996-03-15)
A simple methodology has been developed to characterize the number and location of free cysteine and cystine groups in peptides and proteins, using chemical modification and matrix-assisted laser desorption/ ionization time-of flight mass spectrometry (MALDITOF MS). This new approach employs
D Bonnet et al.
Journal of biochemistry, 130(2), 227-233 (2001-08-02)
There is growing evidence in the literature emphasizing the significance of the post-translational modification of cysteine thiols to sulfenic acids (SOH), which have been found in a number of proteins. Crystallographic and mass spectrometric evidence has shown the presence of

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