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Citations & References (13)
Invitrogen™
PS-Speck™ Microscope Point Source Kit (blue, green, orange & deep-red fluorescent beads)
The PS-Speck™ Microscope Point Source Kit contains four different colors of fluorescence microspheres; each microsphere has a diameter of 0.175Read more
| Catalog Number | Quantity |
|---|---|
| P7220 | 1 kit |
Catalog number P7220
Price (MXN)
7,335.74
Each
Quantity:
1 kit
Price (MXN)
7,335.74
Each
The PS-Speck™ Microscope Point Source Kit contains four different colors of fluorescence microspheres; each microsphere has a diameter of 0.175 +/- 0.005 μm. This exceptionall small diameter coefficient of variation makes the PS-Speck™ microspheres ideal as uniform, subresolution fluorescent point sources for calibrating instrument optics, especially in three-dimensional imaging applications. This kit's four ready-to-use 1 mL suspensions contain bright, monodisperse microspheres with excitation/emission wavelengths of 360/440 nm (blue), 505/515 nm (green), 540/560 nm (orange) and 633/660 nm (deep red). The PS-Speck™ Kit also includes a mounting protocol for the user's convenience and sufficient mounting medium to prepare about 100 slides of each.
See our full collection of microscope calibration reagents ›
See our full collection of microscope calibration reagents ›
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Calibration TypeOptic Calibration, Fluorescence Microscope Calibration
For Use With (Application)Internal or External Fluorescence Microscopy Standards
FormatSuspension Beads
Quantity1 kit
Shipping ConditionRoom Temperature
ColorOrange, Deep Red, Blue, Green
Product LinePS-Speck
TypeMicroscope Point Source Kit
Unit SizeEach
Contents & Storage
Store in refrigerator (2–8°C) and protect from light.
Frequently asked questions (FAQs)
What is the refractive index of the mounting medium in PS-Speck Microscope Point Source Kit (Cat. No. P7220)?
Citations & References (13)
Citations & References
Abstract
Correcting confocal acquisition to optimize imaging of fluorescence resonance energy transfer by sensitized emission.
Journal:Biophys J
PubMed ID:15041688
Imaging of fluorescence resonance energy transfer (FRET) between suitable fluorophores is increasingly being used to study cellular processes with high spatiotemporal resolution. The genetically encoded Cyan (CFP) and Yellow (YFP) variants of Green Fluorescent Protein have become the most popular donor and acceptor pair in cell biology. FRET between these
In vivo mammalian brain imaging using one- and two-photon fluorescence microendoscopy.
Journal:J Neurophysiol
PubMed ID:15128753
'One of the major limitations in the current set of techniques available to neuroscientists is a dearth of methods for imaging individual cells deep within the brains of live animals. To overcome this limitation, we developed two forms of minimally invasive fluorescence microendoscopy and tested their abilities to image cells
Interaction of Maf transcription factors with Pax-6 results in synergistic activation of the glucagon promoter.
Journal:J Biol Chem
PubMed ID:11457839
'In the endocrine pancreas, alpha-cell-specific expression of the glucagon gene is mediated by DNA-binding proteins that interact with the G1 proximal promoter element. Among these proteins, the paired domain transcription factor Pax-6 has been shown to bind to G1 and to transactivate glucagon gene expression. Close to the Pax-6-binding site,
Quality assessment of confocal microscopy slide based systems: performance.
Journal:Cytometry A
PubMed ID:16807897
'BACKGROUND: All fluorescence slide-based cytometry detections systems basically include the following components: (1) an excitation light source, (2) intermediate optics, and (3) a detection device consisting of a CCD camera or a PMT. The optical principles employed is slide-based systems are similar to those of confocal microscopes (CLSM). METHODS: The
Spatial organization of bacteriorhodopsin in model membranes. Light-induced mobility changes.
Journal:J Biol Chem
PubMed ID:12167614
'Bacteriorhodopsin is a proton-transporting membrane protein in Halophilic archaea, and it is considered a prototype of membrane transporters and a model for G-protein-coupled receptors. Oligomerization of the protein has been reported, but it is unknown whether this feature is correlated with, for instance, light activation. Here, we have addressed this