Alexa Fluor™ 430 Protein Labeling Kit - Citations

Alexa Fluor™ 430 Protein Labeling Kit - Citations

View additional product information for Alexa Fluor™ 430 Protein Labeling Kit - Citations (A10171)

Showing 7 product Citations

Citations & References
Abstract
Alexa dyes, a series of new fluorescent dyes that yield exceptionally bright, photostable conjugates.
AuthorsPanchuk-Voloshina N, Haugland RP, Bishop-Stewart J, Bhalgat MK, Millard PJ, Mao F, Leung WY, Haugland RP
JournalJ Histochem Cytochem
PubMed ID10449539
'Alexa 350, Alexa 430, Alexa 488, Alexa 532, Alexa 546, Alexa 568, and Alexa 594 dyes are a new series of fluorescent dyes with emission/excitation spectra similar to those of AMCA, Lucifer Yellow, fluorescein, rhodamine 6G, tetramethylrhodamine or Cy3, lissamine rhodamine B, and Texas Red, respectively (the numbers in the ... More
Small heat shock protein Hsp16.3 modulates its chaperone activity by adjusting the rate of oligomeric dissociation.
AuthorsFu X, Liu C, Liu Y, Feng X, Gu L, Chen X, Chang Z
JournalBiochem Biophys Res Commun
PubMed ID14521926
'Small heat shock proteins usually exist as oligomers and appear to undergo dynamic dissociation/reassociation, with oligomeric dissociation being a prerequisite for their chaperone activities. However, contradictory cases were also reported that chaperone activities could be enhanced with no change or even increase in oligomeric sizes. Using Hsp16.3 as a model ... More
Detection and quantification of biotinylated proteins using the Storm 840 Optical Scanner.
AuthorsLewis B, Rathman S, McMahon RJ
JournalJ Nutr Biochem
PubMed ID12770643
'The use of the avidin-biotin interaction is becoming an increasingly common method for the detection of proteins. The use of fluorescence detection with avidin-biotin systems has the potential to greatly increase both the sensitivity and linearity of this type of analysis. In this report, three fluorescent systems were tested for ... More
Fluorescent histochemical techniques for analysis of intracellular signaling.
AuthorsOksvold MP, Skarpen E, Widerberg J, Huitfeldt HS
JournalJ Histochem Cytochem
PubMed ID11850432
Intracellular signaling relies on the orchestrated cooperation of signaling proteins and modules, their intracellular localization, and membrane trafficking. Recently, a repertoire of fluorescence-based techniques, which significantly increases our potential for detailed studies of the involved mechanisms, has been introduced. Microscopic techniques with increased resolution have been combined with improved techniques ... More
Efficiencies of fluorescence resonance energy transfer and contact-mediated quenching in oligonucleotide probes.
AuthorsMarras SA, Kramer FR, Tyagi S
JournalNucleic Acids Res
PubMed ID12409481
An important consideration in the design of oligonucleotide probes for homogeneous hybridization assays is the efficiency of energy transfer between the fluorophore and quencher used to label the probes. We have determined the efficiency of energy transfer for a large number of combinations of commonly used fluorophores and quenchers. We ... More
Structural and functional changes in the alpha A-crystallin R116C mutant in hereditary cataracts.
AuthorsCobb BA, Petrash JM
JournalBiochemistry
PubMed ID11123904
alpha-Crystallin, the major protein component of vertebrate lenses, forms a large complex comprised of two homologous subunits, alphaA- and alphaB-crystallin. It has the ability to suppress stress-induced protein aggregation in vitro, bind saturably to lens plasma membranes, and aid in light refraction through short-range ordering. Recently, a missense mutation in ... More
Acquisition of arylsulfatase A onto the mouse sperm surface during epididymal transit.
AuthorsWeerachatyanukul W, Xu H, Anupriwan A, Carmona E, Wade M, Hermo L, da Silva SM, Rippstein P, Sobhon P, Sretarugsa P, Tanphaichitr N
JournalBiol Reprod
PubMed ID12773421
Arylsulfatase A (AS-A) is localized to the sperm surface and participates in sperm-zona pellucida binding. We investigated how AS-A, usually known as an acrosomal enzyme, trafficked to the sperm surface. Immunocytochemistry of the mouse testis confirmed the existence of AS-A in the acrosomal region of round and elongating spermatids. However, ... More