2-Nitro-5-thiocyanatobenzoic Acid

2-Nitro-5-thiocyanatobenzoic Acid Structure
2-Nitro-5-thiocyanatobenzoic Acid structure
Common Name 2-Nitro-5-thiocyanatobenzoic Acid
CAS Number 30211-77-9 Molecular Weight 224.19300
Density 1.63g/cm3 Boiling Point 449ºC at 760mmHg
Molecular Formula C8H4N2O4S Melting Point 156-157ºC(lit.)
MSDS Chinese USA Flash Point 225.4ºC
Symbol GHS07
GHS07
Signal Word Warning

EPOR-Based Purification and Analysis of Erythropoietin Mimetic Peptides from Human Urine by Cys-Specific Cleavage and LC/MS/MS.

J. Am. Soc. Mass Spectrom. 26 , 1617-25, (2015)

The development of a new class of erythropoietin mimetic agents (EMA) for treating anemic conditions has been initiated with the discovery of oligopeptides capable of dimerizing the erythropoietin (EPO) receptor and thus stimulating erythropoiesis. The most p...

Probing the electrostatics of active site microenvironments along the catalytic cycle for Escherichia coli dihydrofolate reductase.

J. Am. Chem. Soc. 136(29) , 10349-60, (2014)

Electrostatic interactions play an important role in enzyme catalysis by guiding ligand binding and facilitating chemical reactions. These electrostatic interactions are modulated by conformational changes occurring over the catalytic cycle. Herein, the chang...

Nonradioactive, ultrasensitive site-specific protein-protein photocrosslinking: interactions of alpha-helix 2 of TATA-binding protein with general transcription factor TFIIA and transcriptional repressor NC2.

Nucleic Acids Res. 36(19) , 6143-54, (2008)

We have developed an approach that enables nonradioactive, ultrasensitive (attamole sensitivity) site-specific protein-protein photocrosslinking, and we have applied the approach to the analysis of interactions of alpha-helix 2 (H2) of human TATA-element bind...

Identification of the cyclosporin-binding site in P-glycoprotein.

Biochemistry 37(51) , 18110-8, (1998)

The binding site of cyclosporin A to P-glycoprotein was characterized by using a multidrug-resistant Chinese hamster ovary cell line. P-glycoprotein photolabeled with diazirine-cyclosporin A analogue was purified by a two-step process involving continuous elu...

Chelator-facilitated chemical modification of IMP-1 metallo-beta-lactamase and its consequences on metal binding.

Biochem. Biophys. Res. Commun. 381(1) , 107-11, (2009)

A method involving the reversible chemical modification of an active site, zinc-binding cysteine residue (Cys221) for the specific removal of one of the two zinc ions in the metallo-beta-lactamase IMP-1 was explored. Covalent modification of Cys221 by 5,5'-di...

Mass spectrometric determination of the cleavage sites in Escherichia coli dihydroorotase induced by a cysteine-specific reagent.

J. Biol. Chem. 272(43) , 26934-9, (1997)

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...

Effects of differential sulfhydryl group-specific labeling on the rhodopsin and guanine nucleotide binding activities of transducin.

Arch. Biochem. Biophys. 387(2) , 233-42, (2001)

The role of transducin sulfhydryl groups was examined by chemical modification with four different reagents: 4-acetamido-4'-maleimidyl-stilbene-2, 2' disulfonic acid (AMDA); 4-vinyl pyridine (VP); 2-nitro-5-thiocyano benzoic acid (NTCBA); and 2, 5-dimethoxyst...

In vivo phosphorylation of human erythrocyte spectrin occurs in a sequential manner.

Biochemistry 43(14) , 4251-62, (2004)

Spectrin is the major component of the erythrocyte membrane skeleton and exists as a 526 kDa alphabeta heterodimer. The 246 kDa beta-chain of human spectrin is phosphorylated near the C-terminus, but the exact phosphorylation sites are unknown and the role of...

Nitro-thiocyanobenzoic acid (NTCB) reactivity of cysteines beta100 and beta110 in porcine luteinizing hormone: metastability and hypothetical isomerization of the two disulfide bridges of its beta-subunit seatbelt.

Mol. Cell. Endocrinol. 247(1-2) , 175-82, (2006)

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 arou...

Pressure-induced perturbation on the active site of beta-amylase monitored from the sulfhydryl reaction.

Biochemistry 40(20) , 5914-20, (2001)

We investigated the pressure effect on the conformation of beta-amylase by monitoring the chemical reaction of the unpaired cysteine. Sweet potato beta-amylase is composed of four identical subunits, each of which contains six cysteine residues. These residue...