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Zitierungen und Referenzen (233)
Invitrogen™
Bis-ANS (4,4'-Dianilino-1,1'-Binapthyl-5,5'-Disulfonsäure, Dipokaliumsalz)
Bis-ANS ist 1-8-ANS als Sonde für unpolare Hohlräume in Proteinen überlegen und bindet sich oft mit einer Affinität, die umWeitere Informationen
| Katalognummer | Menge |
|---|---|
| B153 | 10 mg |
Katalognummer B153
Preis (EUR)
439,56
Sonderangebot
Exklusiv online
Endet: 15-Mar-2026
594,00Ersparnis 154,44 (26%)
Each
Menge:
10 mg
Preis (EUR)
439,56
Sonderangebot
Exklusiv online
Endet: 15-Mar-2026
594,00Ersparnis 154,44 (26%)
Each
Bis-ANS ist 1-8-ANS als Sonde für unpolare Hohlräume in Proteinen überlegen und bindet sich oft mit einer Affinität, die um viele Größenordnungen höher ist. Anilinonaphtalensulfonate (ANS) sind im Wesentlichen nicht fluoreszent in Wasser, werden nur merklich fluoreszent, wenn sie an Membranen gebunden werden. Diese Eigenschaft macht es zu einem empfindlichen Indikator für Proteinfaltung, Konformationsänderungen und andere Prozesse, die die Exposition der Sonde in Wasser verändern.
Nur für Forschungszwecke. Nicht zur Verwendung bei diagnostischen Verfahren.
Specifications
MarkertypAndere Labels oder Farbstoffe
SummenformelC32H22K2N2O6S2.
ProduktlinieMolecular Probes
Menge10 mg
Empfohlene LagerungBei Raumtemperatur lagern und vor Licht schützen.
VersandbedingungRaumtemperatur
Subzelluläre LokalisationZellmembranen & Lipide
Physikalische FormFest
ProdukttypBis-ANS
Unit SizeEach
Zitierungen und Referenzen (233)
Zitierungen und Referenzen
Abstract
Interaction of 1,1'-bi(4-anilino)naphthalene-5,5'-disulfonic acid with alpha-crystallin.
Journal:J Biol Chem
PubMed ID:9535881
'The hydrophobic sites in alpha-crystallin were evaluated using a fluorescent probe 1,1''-bi(4-anilino)naphthalenesulfonic acid (bis-ANS). Approximately one binding site/subunit of alpha-crystallin at 25 degrees C was estimated by equilibrium binding and Scatchard analysis (Kd = 1.1 microM). Based on fluorescence titration, the dissociation constant was 0.95 microM. The number of bis-ANS
Plurality of protein conformations of ribulose-1,5-bisphosphate carboxylase/oxygenase monomers probed by high pressure electrophoresis.
Journal:J Biol Chem
PubMed ID:7902356
'We used hydrostatic pressure in the range of 1 to 2 kbar, coupled with polyacrylamide gel electrophoresis, to investigate the properties of monomers of dimeric ribulose bisphosphate carboxylase/oxygenase. At temperatures below -5 degrees C or pressures above 1.5 kbar, only a diffuse band with low electrophoretic mobility was observed, which
An operator-induced conformational change in the C-terminal domain of the lambda repressor.
Journal:J Biol Chem
PubMed ID:1532575
'4,4''-bis(1-anilino-8-naphthalenesulfonic acid (Bis-ANS), an environment-sensitive fluorescent probe for hydrophobic region of proteins, binds specifically to the C-terminal domain of lambda repressor. The binding is characterized by positive cooperativity, the magnitude of which is dependent on protein concentration in the concentration range where dimeric repressor aggregates to a tetramer. In this
Exploiting new potential targets for anti-hepatitis B virus drugs.
Journal:Curr Drug Targets Infect Disord
PubMed ID:14529356
'Based on the recent studies of HBV strains with different replication efficiency, several new potential targets for anti-HBV replication have been presented. These include the viral and cellular regulatory factors associated with HBV replication and the process for encapsidation of viral genome and budding into endoplasmic reticulum (ER). A putative
Detection of disulfide bonds in bovine brain tubulin and their role in protein folding and microtubule assembly in vitro: a novel disulfide detection approach.
Journal:Biochemistry
PubMed ID:11467944
'Cysteine residues in tubulin are actively involved in regulating ligand interactions and microtubule formation both in vivo and in vitro. These cysteine residues are sensitive reporters in determining the conformation of tubulin. Although some of the cysteines are critical in modulating drug binding and microtubule assembly, it is not clear