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ISS Inc, 1602 Newton Drive, Champaign, IL (2026)

09/08/2026

How do you determine the best excitation wavelength for a two-photon fluorescent probe?

Before a fluorescent molecule can be optimized for two-photon microscopy, researchers need to understand how efficiently it absorbs light across the relevant excitation range.

Developing new fluorescent probes? Characterizing two-photon properties? Building a new spectroscopy workflow? Talk with ISS about configuring a PC1 for your research here: https://iss.com/contact?product=pc1

In a published Bio-protocol study, researchers from Montana State University used an ISS PC1 photon-counting spectrofluorimeter coupled to a tunable femtosecond laser to characterize the two-photon absorption properties of fluorescent molecules across the 680–1300 nm spectral range.

Using a relative fluorescence approach with established reference standards, the researchers measured two-photon excitation spectral shapes and absolute two-photon absorption cross sections. Information that can help researchers identify optimal excitation wavelengths, improve probe selection, and reduce the laser power needed for two-photon imaging.

The study is a strong example of how the PC1 can be integrated into advanced optical measurement systems to provide sensitive, quantitative fluorescence measurements. With photon-counting detection, flexible excitation options, automated control through Vinci software, and detector configurations extending into the near-infrared, PC1 can be configured for demanding fluorescence spectroscopy applications.

Read the publication and explore what PC1 can do for your next experiment here: https://bio-protocol.org/en/bpdetail?id=3498&type=0

09/04/2026

Quantifying Life Under Pressure — At Single-Cell Resolution

Understanding how microbes respond to extreme pressure matters for two very different reasons: it's central to understanding life in the deep biosphere, and it's a direct challenge for high-pressure processing (HPP) - a multibillion-dollar, fast-growing food and beverage sterilization method that preserves taste and texture better than heat, but only works if you understand how pressure-resistant microbes survive it.

If your work touches pressure biology, extremophile adaptation, or HPP-relevant microbiology, our application scientists can talk through how the High-Pressure Cell and Alba v5 would fit your experimental design. Contact us here for more information about the HP Cell and/or Alba v5: https://iss.com/contact

A study published in Frontiers in Microbiology (2024) by Coffin, Fisher, Crippen, Demers, Bartlett, and Royer (Rensselaer Polytechnic Institute and Scripps Institution of Oceanography) set out to quantify E. coli's pressure-induced heat shock response at a resolution no one had achieved before: single cells.

Full publication here: https://www.frontiersin.org/journals/microbiology/articles/10.3389/fmicb.2024.1470617/full

The team used an ISS High-Pressure Cell system to deliver precisely controlled pressure shocks to both standard E. coli and a lab-evolved, pressure-tolerant strain (AN62). Cells were then imaged on an ISS Alba v5 fluctuation microscope using two-photon scanning number and brightness (sN&B) microscopy. A technique that yields absolute, single-cell-resolved molecule counts, not just relative fluorescence intensity.

What they found: all four key heat-shock genes were upregulated after pressure shock in both strains, but the pressure response was genuinely distinct from the classic heat response, and distinct between strains. The pressure-adapted strain favored a different chaperone (GroEL over DnaK) than the standard strain, and one gene's response was so unpredictable cell-to-cell that the authors propose its regulatory protein, RpoE, may function as a built-in pressure sensor.

Why this combination matters for your own research:

→ The HP Cell delivers a precisely defined, reproducible stressor (controlled increments, held pressure, calibrated timing) exactly what dose-response and mechanistic studies require.

→ sN&B on the Alba v5 gives you absolute molecule counts at true single-cell resolution, distinguishing a real increase in expression per cell from simply more cells in the field of view. A distinction ordinary fluorescence imaging can't make.

→ This isn't a one-off pairing. This same Royer lab methodology builds on earlier published work using the identical High-Pressure Cell + Alba combination for live microbial imaging under pressure. A validated, reproducible workflow, not a novel one-time setup.

09/03/2026

When a Biosensor's Readout Isn't as Simple as It Looks: Pressure Effects on GFP Fluorescence Anisotropy

Green Fluorescent Protein isn't just a marker...its fluorescence anisotropy is routinely used as a readout for molecular packing and rotational dynamics, from measuring how tightly nucleoporins pack within the nuclear pore complex to functioning as an intracellular temperature sensor. But nearly all of that work assumes temperature is the only variable moving the needle. What about pressure?

If your research involves protein or biosensor behavior under pressure (extremophile biology, bioprocessing, or fundamental protein biophysics) our application scientists can talk through how the High-Pressure Cell fits your experimental design. Reach out here: https://iss.com/sample-compartments/high-pressure-cell

A study published in RSC Advances (2022) by Kaur, Nguyen, and Kumar (University of Arkansas) tested that assumption directly, measuring GFP's steady-state fluorescence anisotropy across a combined pressure–temperature grid using a high-pressure cell integrated with temperature-regulated fluorescence measurements.

Fulll publication here: https://pubs.rsc.org/ra/article/12/14/8647/745215/Pressure-and-temperature-dependence-of

The results complicate the simple picture. At constant temperature, anisotropy decreased with increasing pressure. But at atmospheric pressure, anisotropy simply decreased with rising temperature. While above roughly 20 MPa, that relationship changed entirely: anisotropy instead showed a maximum with temperature, and the temperature of that maximum shifted higher as pressure increased. The team also ruled out the most obvious explanation increased solvent viscosity under pressure as the primary driver, pointing instead toward pressure-induced changes in hydrogen bonding around the chromophore itself. All of this remained fully reversible up to 200 MPa.

Why this matters beyond GFP itself:

→ If you're using fluorescence anisotropy as a biosensor readout in any pressure-variable system. Piezophiles, deep-sea organisms, high-pressure bioprocessing, or even cellular compartments under mechanical stress. This work is a reminder that pressure and temperature can interact in genuinely non-intuitive ways, not just add up.

→ Precise, independent control of both pressure and temperature is what made this distinction possible. Without decoupling the two variables experimentally, the non-monotonic pressure effect would be invisible.

→ The ISS High-Pressure Cell is built for exactly this kind of P-T dissection. Pressures up to 400 MPa (well beyond the ~200 MPa range this study explored) with integrated temperature control from -40°C to 80°C, mounting directly into ISS spectrofluorometers for real-time anisotropy, intensity, or lifetime readout as conditions change.

09/01/2026

How Extreme Pressure Is Revealing a New Kind of Cell Membrane Homeostasis

Cells are well known to keep their membranes fluid in response to temperature. A process called homeoviscous adaptation. But do cells also actively regulate the shape of their membrane lipids? A study published in Cell Reports Physical Science (2026) set out to answer that question using an unconventional experimental lever: extreme hydrostatic pressure, similar to what's found in the deep ocean.

If pressure-dependent membrane or protein biophysics is part of your next proposal, our application scientists can talk through how the High-Pressure Cell would fit your experimental design. Find out more about our High Pressure Cell System and contact us here: https://iss.com/sample-compartments/high-pressure-cell

Milshteyn, Winnikoff, Budin, and colleagues (UC San Diego and Harvard) used high pressure to directly compress the molecular curvature of phospholipids in living yeast and human cancer cells. A way to isolate curvature effects from the temperature-driven fluidity effects that have confounded this question in the past. To characterize how membrane packing and phase behavior shifted across pressure, the team ran high-pressure fluorescence spectroscopy using the ISS High-Pressure Cell, measuring C-Laurdan dye polarization across a full pressure–temperature grid (roughly 1–1,000 bar, 5–80°C) to track membrane fluidity independently of curvature.

What they found: both yeast and human cells actively compensated. Yeast ramped up synthesis of phosphatidylinositol, a lipid whose negative curvature hadn't been well characterized before; human cells instead increased ether-linked phospholipids. In both cases, cells pushed their membrane composition toward higher curvature even at a real cost to fluidity. Evidence of a distinct, previously unrecognized homeostatic mechanism the authors call "homeocurvature."

Full publication here: https://www.cell.com/cell-reports-physical-science/fulltext/S2666-3864(26)00183-9

This builds on the same group's 2024 Science paper on pressure adaptation in deep-sea ctenophores...work covered by Quanta Magazine, Scientific American, and Nature News, among others.

Why this matters if membrane biophysics is part of your research:

→ Pressure decouples variables that temperature can't. Using hydrostatic pressure as an experimental lever isolates curvature stress from fluidity effects. A mechanistic dissection other approaches can't cleanly achieve.

→ The ISS High-Pressure Cell reaches well beyond what this study required, up to 400 MPa (4,000 bar) with sapphire windows, with built-in temperature control from -40°C to 80°C, giving real headroom for pressure-dependent membrane, protein, or lipid studies.

→ It mounts directly into ISS spectrofluorometers (PC1, ChronosBH, ChronosDFD) for real-time fluorescence readout during pressure and temperature ramps, rather than requiring separate sample handling at each condition.

08/31/2026

Monitoring Protein Unfolding in Real Time. PC1 and the High-Pressure Cell in Sustainable Protein Research.

Edible insects are increasingly viewed as a scalable, sustainable protein source for a growing global population but turning them into viable food ingredients requires understanding exactly how processing affects their proteins.

If pressure-dependent protein structure is part of your research whether in food science, biophysics, or structural biology our application scientists can talk through how PC1 and the High-Pressure Cell would fit your experiment. Reach out here: https://iss.com/contact

In a study published in Foods (2022), Boukil et al. investigated how high hydrostatic pressure (HHP), a nonthermal food-processing technique, structurally modifies soluble proteins extracted from mealworm (Tenebrio molitor). The team pressurized protein extracts from 70 to 600 MPa and needed a reliable way to both calibrate their pressurization system and directly monitor the resulting protein conformational changes.

Full publication here: https://www.mdpi.com/2304-8158/11/7/956

They used the ISS High-Pressure Cell, directly connected to the ISS PC1 photon-counting spectrofluorometer, to establish accurate pressurization values, and then used the PC1 to run two complementary fluorescence assays: intrinsic tryptophan fluorescence (to track protein unfolding) and ANS-binding surface hydrophobicity measurements (to track exposure of hydrophobic regions as the protein structure opened up).

The results told a clear structural story: fluorescence intensity dropped by as much as 30% at 600 MPa, with a measurable redshift in emission wavelength. A signature of tryptophan residues becoming more solvent-exposed as the proteins unfolded. Combined with electrophoresis, mass spectrometry, and electron microscopy, the team went on to identify, for the first time, the specific mealworm proteins (hexamerin 2, α-amylase, actin, and myosin) driving aggregate formation under pressure.

Why this matters beyond this specific study:

→ Fluorescence spectroscopy gives you a direct, real-time readout of protein unfolding. No need to wait for downstream structural assays to know pressure treatment is having an effect.

→ The HP Cell's direct pump-to-spectrofluorometer connection made precise, calibrated pressurization possible in the first place. Critical for any pressure-dependent structural study.

→ This isn't limited to food science. The same PC1 + HP Cell combination applies anywhere researchers need to study pressure-induced protein folding, unfolding, or aggregation. From alternative proteins to structural biology and biophysics more broadly.

08/26/2026

Two-Species Lifetime Unmixing.
See What Intensity Can’t.

📩 Working with complex samples or need robust lifetime unmixing? Let’s talk. Reach out here: https://iss.com/contact

When multiple fluorescent species overlap, intensity alone can’t tell you who’s contributing what. Fluorescence lifetime (FLIM) can.

The image shown here demonstrates two-species lifetime unmixing from a Convallaria sample using phasor plot analysis on the ISS Alba v5.

In the phasor plot, the data forms a linear distribution. A clear signature that two distinct lifetime species contribute to each pixel. By placing cursors at each end of the line (short and long lifetimes), the system identifies the pure species and calculates their relative contributions.

Using the Multi-image Phasor Analysis (MiPA) module in ISS VistaVision software, you can:
✔️ Separate lifetime species without model fitting
✔️ Calculate fractional contributions at every pixel
✔️ Generate unmixed images for each species
✔️ Create a merged false-color map (e.g., green = shorter lifetime, red = longer lifetime)

MiPA also supports:
• Multi-frequency phasor analysis
• Multi-image comparison in a single phasor space
• ROI-based selection with flexible cursor shapes
• Built-in denoising and thresholding tools
• FRET efficiency mapping for interaction studies

And with FastFLIM, phasor plots can be visualized in real time. Giving immediate feedback during acquisition.

Available Across ISS Confocal Platforms. Phasor and MiPA-based FLIM analysis are available across ISS laser scanning confocal systems, including:

Alba v5
Alba STED
VIVIsight PRO
FLIMsight PRO
Q2

🤝 Enhanced by Time-Tagging Innovation

Through its collaboration with Swabian Instruments, ISS integrates advanced Time Tagger technology into select systems.

This enables:
✔️ Ultra-precise photon timing (picosecond resolution)
✔️ Simultaneous multi-channel acquisition
✔️ High-throughput data streaming for real-time FLIM and phasor analysis

The result is faster, more accurate insight into molecular environments and interactions.

💬 Bottom line:
Phasor-based FLIM with MiPA transforms overlapping signals into clear, quantitative maps of distinct species. Pixel by pixel.

08/25/2026

Fluorescence intensity tells you where but fluorescence lifetime (FLIM) tells you what’s happening.

📩 Exploring FLIM for your research or comparing TCSPC vs FastFLIM? Let’s talk. Find out more here: https://iss.com/fluorescence/time-resolved-laser-scanning-confocal-microscopes/alba

The image shown here highlights confocal FLIM of Convallaria with data analyzed using both:

Time-domain (TCSPC) fitting
Digital frequency-domain (FastFLIM) fitting

On the ISS Alba v5, you don’t have to choose one approach. You can leverage both, depending on your experimental needs. Flexible FLIM Acquisition

ISS systems support:

✔️ Digital TCSPC for maximum sensitivity and detailed decay reconstruction
✔️ FastFLIM (frequency-domain) for rapid, real-time lifetime measurements

Both approaches cover an exceptional dynamic range from 100 ms. Enabling analysis of everything from ultrafast photophysics to slow biological processes.

Each FLIM dataset also contains steady-state intensity data, and when optimized, supports advanced analyses like RICS and Number & Brightness (N&B) turning every image into a multi-dimensional dataset.

🤝 Enhanced by Swabian Instruments Time-Tagging Innovation

Through its collaboration with Swabian Instruments, ISS integrates advanced Time Tagger technology into select systems.

This enables:
✔️ Ultra-precise photon timing with picosecond resolution
✔️ Simultaneous multi-channel acquisition
✔️ High-throughput data streaming for advanced FLIM and correlation analyses

💬 Bottom line:
ISS FLIM gives you the flexibility to choose the right method and the tools to extract quantitative, defensible insight from every pixel.

08/24/2026

Unmixing Complexity, One Lifetime at a Time!
Biological samples are rarely simple. Even standard stains can produce overlapping fluorescence signals that make it difficult to confidently distinguish what’s contributing to your image.

Working with complex samples or overlapping fluorophores? Let’s talk. Contact us here: https://iss.com/contact

ISS solves this with quantitative, time-resolved unmixing.
Using two-photon excitation (780 nm) and hybrid PMT photon-counting detection, ISS systems capture high-quality fluorescence data from complex samples. Such as hematoxylin and eosin (H&E)-stained tissue.

With integrated FastFLIM technology, fluorescence decay is recorded at every pixel, enabling:

✔️ Full lifetime-resolved datasets across the image
✔️ High sensitivity for weak or overlapping signals
✔️ Accurate representation of underlying molecular contributions

The real power comes in analysis.
Using the ISS VistaVision phasor plot module, this time-resolved data is:

✔️ Quantitatively unmixed into distinct fluorescent species
✔️ Separated without model assumptions or complex fitting
✔️ Visualized as individual component images

The result?
Three clean, independent images. Each representing a single fluorescent species, combined into a composite where:

🔴 Red = shortest lifetime
🟢 Green = intermediate lifetime
🔵 Blue = longest lifetime

Why it matters:
Instead of guessing based on intensity alone, you gain clear, quantitative separation of signals. Strengthening interpretation, reproducibility, and confidence in your results.

08/24/2026

Can fluorescence lifetime imaging unlock the full potential of near-infrared probes?

A groundbreaking study, utilizing the Alba v5, published in Chemical Science introduced a new class of highly luminescent, biocompatible ytterbium (Yb³⁺) complexes designed for near-infrared (NIR) fluorescence imaging in living cells. These innovative probes combine high brightness, excellent stability, and remarkably long fluorescence lifetimes, opening new possibilities for biological imaging.

👉 Learn more about the Alba v5: https://iss.com/fluorescence/time-resolved-laser-scanning-confocal-microscopes/alba

Why is this important?

Near-infrared fluorophores offer significant advantages for biological imaging, including reduced background interference and deeper optical pe*******on. When paired with Fluorescence Lifetime Imaging Microscopy (FLIM), researchers can distinguish probe signals from cellular autofluorescence with exceptional clarity. Revealing information that conventional intensity-based imaging may miss.

To investigate these advanced NIR probes, the researchers utilized the ISS Alba v5 Time-Resolved Laser Scanning Confocal Microscope, demonstrating how quantitative fluorescence lifetime imaging can capture intracellular lifetime distributions while delivering high signal-to-noise measurements in living cells.

This work highlights the growing impact of combining innovative fluorophore design with time-resolved fluorescence microscopy to advance applications in molecular imaging, chemical biology, and biomedical research.

📖 Featured Publication:
Highly luminescent, biocompatible ytterbium(III) complexes as near-infrared fluorophores for living cell imaging. Chemical Science (2018). Full publication here: https://pubs.rsc.org/sc/article/9/15/3742/621756/Highly-luminescent-biocompatible-ytterbium-iii

08/21/2026

🧠 Hemoglobin Changes Are Only Part of the Story. What About Brain Metabolism?

Many optical brain imaging studies rely on standard NIRS measurements of oxygenated and deoxygenated hemoglobin. While useful, those signals alone don’t reveal how much oxygen the brain is actually consuming. A critical metric when studying aging, cerebrovascular disease, neurorehabilitation, sleep disorders, or cognitive decline.

📩 If your next study requires CMRO₂ and not just hemoglobin changes, request a MetaOx configuration and budgetary quote tailored to your population and protocol, or schedule a MetaOx application consultation. HERE: https://iss.com/biomedical/metaox

ISS Medical MetaOx was designed to close that gap.
MetaOx uniquely integrates Frequency-Domain Near-Infrared Spectroscopy (FDNIRS), Diffuse Correlation Spectroscopy (DCS), and pulse oximetry in a single system. By combining quantitative oxygenation, cerebral blood flow, and arterial oxygen saturation, the platform enables researchers to derive the cerebral metabolic rate of oxygen (CMRO₂). A direct indicator of brain metabolic activity.

Instead of assembling multiple instruments and synchronizing datasets, MetaOx delivers simultaneous measurements from these complementary technologies, allowing researchers to monitor real-time metabolic shifts in the brain during cognitive, physiological, or clinical experiments.

Why researchers choose MetaOx

✔ Simultaneous FDNIRS + DCS acquisition for integrated physiology measurements
✔ Quantitative measurement of hemoglobin concentration and oxygenation
✔ Optical measurement of microvascular blood flow using DCS
✔ Derivation of cerebral CMRO₂ by combining oxygenation, flow, and arterial saturation
✔ Fast acquisition (up to ~50 Hz) for tracking dynamic metabolic changes
✔ Multi-wavelength NIRS system for robust optical tissue characterization

MetaOx is already supporting research applications ranging from neonatal brain physiology and congenital heart disease studies to cerebrovascular reactivity, stroke, traumatic brain injury, and aging research.

Instead of asking “How did hemoglobin change?” researchers can now ask: “How did brain metabolism change?”

ISS Inc

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