What are the opening hours?

Monday 9am - 5pm Tuesday 9am - 5pm Wednesday 9am - 5pm Thursday 9am - 5pm Friday 9am - 5pm

https://www.sinobiological.com/category/signaling

SignalChem, Richmond, BC (2026)

10/07/2025

At SignalChem Biotech, our work with ubiquitin enzymes is about more than proteins. It’s about engineering clarity into a complex system.

The ubiquitin cascade works like a relay race: E1 activates ubiquitin, E2 carries it, and E3 attaches it to a target protein. Each step is essential, but how do you know if each handoff works?

That’s where assay design comes in. By tagging each step of the cascade, our scientists can:
- Validate enzyme function independently
- Pinpoint where a reaction stalls
- Tailor assays for E1s, E2s, or E3s based on research goals

Accelerate screening for inhibitors or activators at specific stages
This modular approach transforms a hidden molecular process into something measurable and engineerable, making the “invisible” visible for researchers worldwide.

Tune in tomorrow to hear more tips from Eric and our SCB assay specialist team

10/06/2025

Why our SCB scientists think using insect cells (sf9) to express Ubiquitin is a good idea.

Behind every functional ubiquitin enzyme lies a careful choice: how and where it’s expressed.
Our scientists know that expression systems matter:

E. coli offers speed, but many ubiquitin enzymes misfold, aggregate, or form inclusion bodies.
Insect cells (like Sf9) provide a eukaryotic environment, enabling proper folding, post-translational modifications, and stability.

Equally important is the choice of purification tag (His, GST, or others) because ubiquitin-like proteins are small and easily misfolded if not handled properly.

By refining these details, SCB ensures that every enzyme we deliver is active, validated, and research-ready. It’s a subtle but critical part of our craft, turning complexity into reliability for scientists pushing the boundaries of ubiquitin research.

Tune in tomorrow to hear more tips from Eric, our SCB ubiquitin specialist.

09/10/2025

What if a single chemical tweak decided whether your immune system stayed calm or went to war? That’s exactly the balancing act ADARs perform every day.

When double-stranded RNA (dsRNA) accumulates in cells, sensors like MDA5 can mistake it for viral RNA, triggering an interferon storm. That’s where ADAR1 comes in. By editing adenosines within endogenous dsRNA, ADAR1 essentially “marks” self-RNA as harmless. Without this safeguard, the immune system goes on high alert, even in the absence of infection.

The consequences are profound:

- Autoimmunity: Loss of ADAR1 activity is linked to interferonopathies such as Aicardi-Goutières syndrome.

- Cancer biology: Many tumors downregulate ADAR activity, tipping the balance between immune evasion and recognition.

- Drug development: Understanding ADAR1’s role opens doors for tuning immune responses in antiviral therapy, immuno-oncology, and beyond.

So while A-to-I editing may look like a small molecular trick, in practice it’s a critical checkpoint for immune homeostasis. ADARs don’t just edit RNA, they decide when the immune system should stay quiet, and when it should act.

Read more here: https://www.sinobiological.com/category/ads/adar-enzymes

09/09/2025

When we hear “mutation,” we think of changes to the DNA sequence. But cells have another way of rewriting instructions: editing RNA bases.

Enter the ADAR family of enzymes (Adenosine Deaminases Acting on RNA). These proteins make a subtle but powerful switch: converting adenosine (A) into inosine (I) within double-stranded regions of RNA. Because the translation machinery reads inosine as if it were guanosine (G), this tiny edit can change a codon, alter splicing, or remodel RNA structure.
Here’s why it matters:

- Reversible: RNA editing can be dialed up or down as conditions change, unlike permanent mutations.

- Dynamic: Different tissues, especially the brain and immune system, use ADAR editing to fine-tune signaling.

- Protective: By marking double-stranded RNA as “self,” ADARs help prevent false immune activation.
In short, ADARs are not genome editors, they are epitranscriptome editors, providing a fast, flexible layer of control over gene expression.

As research grows, so does the need for high-quality ADAR enzymes and substrates to explore their roles in disease, immunity, and neuroscience. Understanding the difference between mutation and editing isn’t just semantics. It's the key to unlocking a whole new level of biology.

Read more in the description below

09/05/2025

Why our tau proteins aren’t tagged and 3 other things our experts at SCB learned at their time working here

1. Tags aren’t always helpful.

Most recombinant proteins are expressed with tags to simplify purification. With tau, it’s different: even 6 extra residues can change folding and impact downstream aggregation assays. That’s why researchers often prefer tag-free tau. We’ve managed to find a way to get it to very high purity even without the tags.

2. Tau doesn’t look its size.

Theoretical molecular weight? ~60 kDa. But on HPLC, tau often behaves like a ~200 kDa protein. Why? Because it’s intrinsically disordered. Instead of a compact globular structure, tau behaves more like an extended coil, making it difficult to pin down as monomer, dimer, or oligomer. For anyone characterizing tau, size alone can be misleading.

3. Phosphorylation is harder than it sounds.

Phosphorylated tau is central to pathology, but reproducing it in the lab is not straightforward. Many preparations are heterogeneous, phosphorylated at multiple sites without control. Our team is working on site-specific versions, with one product already verified by Western blot (single phosphorylation site). This level of precision is critical for mechanistic studies.
The Tau monomer is the real workhorse.

Tau wants to aggregate. Left unchecked, monomers form oligomers and fibrils with ease. But aggregation studies, drug screening, and mechanistic experiments all start with monomeric tau. We’ve isolated tau in its monomeric form and confirmed it using HPLC.

Takeaway: What looks simple on paper quickly becomes complex in the lab. And that complexity, from purification to post-translational control, is exactly why tau is both a challenge and an opportunity for those tackling neurodegenerative disease.

Find out about our catalogue of over 60 Tau and related proteins in the comments below.
If you’ve worked with tau, what surprised you most in the lab?

09/04/2025

For years, tau was considered “undruggable”.
Now, antibodies are breaking that barrier.

Tau proteins were once thought to be beyond the reach of immunotherapy. They hid inside neurons, formed tangled structures, and spread in ways that seemed impossible to block. But recent advances are proving otherwise.
Antibodies don’t just bind tau, they can intervene at multiple stages of the disease process:
Block spread:

- by binding extracellular tau seeds before they enter neighboring neurons.
- Promote clearance: by tagging aggregates for microglial uptake and lysosomal degradation.
- Enable intracellular degradation: through pathways like TRIM21, which recognize Ab–tau complexes inside cells (pre-clinical studies).

Even more exciting, epitope-specific designs are emerging. For example, antibodies like ADEL-Y01 target tau that’s been acetylated at lysine-280, a modification known to accelerate aggregation and seeding. Precision matters, hitting the right species of tau (oligomers, seeds, or modified forms) is likely to determine which therapies succeed.

Takeaway: Antibodies can now target tau. What was once elusive is becoming tractable and the challenge ahead is not if we can target tau, but which forms of tau we should prioritize.

If you were designing an antibody, would you go after tangles, oligomers, or modified tau first? Read more in the article in the previous posts

09/03/2025

Neurofibrillary tangles made tau infamous.
Yet it’s the invisible oligomers that do the most harm.

Neurofibrillary tangles are one of the most recognizable hallmarks of Alzheimer’s disease. They’re large, visible under a microscope, and easy to stain, which made them the natural suspects for decades. If you could clear the tangles, the thinking went, you could halt the disease.
But visibility doesn’t equal toxicity. The real culprits emerge earlier.

Research now shows that small soluble tau oligomers appear long before tangles ever form. These oligomers are mobile, slipping between neurons and disrupting synapses. Even more concerning, they spread in a prion-like fashion, templating normal tau into misfolded states and propagating pathology across brain circuits.

By the time tangles accumulate, much of the neuronal damage is already done. The tangles may be less the cause and more the grave markers of a process that began years earlier.
So, what does this mean for therapy?

This shift has major implications for drug development. If we continue to chase tangles, we may always be arriving too late. The real therapeutic window lies in stopping tau oligomers and seeds before they wreak havoc.

Antibodies, small molecules, and other strategies need to be designed with this in mind: targeting the toxic species of tau, not just the visible ones.

Takeaway: Clearing tangles ≠ halting disease. To truly alter the course of Alzheimer’s, therapies must confront pathological tau, the early stage drivers of pathology hiding long before tangles appear.

What do you think: are tangles the main target, or do they still have a role in therapy?

Read more in the article in the comments

09/02/2025

Tau stabilizes microtubules… right? Not exactly. New data shows tau’s real role may be in assembly, not just stability.

But our view of tau has shifted in more ways than just this one.

For years, the dogma was simple: tau is an axonal protein whose primary job is to stabilize microtubules. In this view, tau acts like clamps, locking down the cytoskeletal tracks that neurons rely on to transport cargo.

Here are 3 things that changed:

1. From “stability” to “assembly”

Live-cell imaging reveals that tau doesn’t merely lock microtubules into place, it actively promotes microtubule assembly. Instead of being a static stabilizer, tau appears to be a dynamic builder, guiding the growth and renewal of axonal tracks.
This matters because in tauopathies, loss of tau isn’t just about aggregates becoming toxic. It’s about losing a protein that normally helps neurons construct and maintain their architecture.

2. More than just axons

Another surprise: tau isn’t confined to axons. It’s been detected in dendrites, synapses, neuronal somata, and glial cells. This broader distribution hints at roles in synaptic signaling and cell-to-cell communication and suggests that mislocalization of tau may be a driver of neurodegeneration in its own right.

3. Rethinking pathology

The old tau dogma painted disease as a story of toxic gain-of-function — hyperphosphorylated tau clumping into tangles. The new view adds another layer: loss-of-function. Without tau promoting assembly and supporting multiple compartments of the CNS, neurons are deprived of a vital set of functions.

This duality changes how we think about therapy. Should strategies focus only on clearing aggregates, or also on restoring tau’s normal roles? Should we treat tauopathies as conditions of excess toxicity — or as conditions of absence as well?

Takeaway: Tau stabilizes microtubules… right? Not exactly. Its real role is more dynamic, more widespread, and more fragile than the old dogma ever suggested. And if we want to design effective therapies, we need to confront both sides of the equation — what tau becomes, and what tau stops doing.

What do you think: are tauopathies more about toxicity, loss, or both? Read more in the article in the comments

08/15/2025

Ever wondered what it’s like to work at the frontline of kinase research? Here’s a peek into a day in the life of Ivan, a UBC co-op student at SCB.

Q: Why did you choose this co-op?
SCB is the top manufacturer of kinases. It’s the perfect place to experience peak kinase research.
But the secret, more personal answer? I wanted to try industry work. I’m returning to UBC to do my honours anyways, so I want to use co-op to get industry experience.

Q: What do you do at SCB?
I run kinase assays – from plating/welling to assaying activity.
One of my key projects is determining the Km value for human kinases (Michaelis constant). I focus on helping to build a comprehensive database for customers for 300 of these commonly used human kinases.
I also:
- Optimize conditions (e.g., SB10 where signal/background ratio = 10)
- Perform IC50 screenings against inhibitors
- Troubleshoot assays (sometimes it’s just kinase-dependent)

Q: What’s a typical day like?
Half the day is spent preparing assays, the other half running them (3–4 hours), plus time reading papers and learning more about kinase science.

Q: What’s been your peak experience so far?
The discussions. Talking through experiments and ideas has been the most fun and rewarding part. The researchers & advisors here are pretty chill. (That, or they don’t know how to say no when I walk up to bother them)

Q: Things you’ve learned?
- Electronic pipettes aren’t always your friend. I wasted a whole 96 well plate because of them
- How kinase activity is actually measured. The people here actually know their stuff.
-How to prioritize reagent use when supplies are limited. Some stuff, like buffers, you can actually dilute as long as you can put it in there

Q: Things that I could improve?
- Better experiment documentation
- More efficient cleanups
- Improved box organization and labeling (30 minutes to find a specific enzyme makes me wish I shouldn’t have even started the assay)

Passionate about science and looking to make an impact? Join us at SCB and help push the boundaries of kinase research.

08/15/2025

What else is your drug hitting?
A kinase panel could expose off-target risks before your patients do.

You're screening a small library of ATP-competitive kinase inhibitors originally designed for JAK1, an important cancer drug target.

One lead candidate works at the nanomolar scale.

Sounds exciting, right?

But your investor wants confidence in selectivity. They’re concerned about off-target effects that could derail safety down the line.

Instead of individually sourcing kinases or guessing based on sequence homology, you run the compound through a SignalChem Tyrosine Kinase Panel which includes JAK1, CSK, LCK, EPHA6, FLT1, ABL1, and more.

The result? You discover moderate inhibition of ABL1 and TNK1 at therapeutic concentrations. That single finding shifts your entire risk assessment.

Now, you can:

- Flag potential safety concerns early
- Refine your structure to improve selectivity
- Consider repositioning the lead toward dual-activity indications (e.g. JAK–ABL cancers)

So, what else is in our TK panel that is useful to you?

Besides JAK1, our panel includes a hand-picked mix of both receptor and non-receptor tyrosine kinases, covering key nodes across oncology, immunology, and angiogenesis.

- ABL1: a critical player in leukemias (e.g. BCR-ABL in CML)
- LCK & CSK: essential regulators of T cell activation
- FLT1 (VEGFR1): involved in angiogenesis and tumor vascularization
- DDR2: linked to fibrosis and certain solid tumors
- EPHA6 & TEC: emerging targets in neural development and immune signaling
- TNK1: a lesser-known kinase with tumor suppressor roles

Each kinase in the panel is active, quality-verified, and available in scalable quantities. This makes it ideal for selectivity profiling, repurposing screens, or mechanism-of-action studies.

Whether you’re validating a hit, de-risking a lead, or mapping off-targets, this panel gives you a strategic snapshot of how your compound behaves across the TK family.

We don’t just offer the TK panel, of course.
There are 8 other panels available, like the AGC panel shown below. Right now, you can mix and match them and get up to 20% off!
Visit: https://ow.ly/1yvH50WE9xi

08/13/2025

Are you using the right kinase isoform? Here’s another subtle, yet crucial, point that most people overlook.

When a kinase behaves unexpectedly in your assay, the first instinct is to question the buffer, the substrate, or the inhibitor.

But there’s a quieter culprit that you may have missed: You might be using the wrong isoform.

So, what is an isoform?

The same gene for proteins can be spliced in different ways, resulting in many variants across many cell/tissue types. These variants are called isoforms and kinases are no different.

Even with this simple variation, the regulation, and biological role can be vastly different:

One isoform may be active in your tissue model, another silent.

Some bind cofactors; others don’t.

Even minor sequence differences can alter inhibitor binding.

It’s entirely possible to screen hundreds of compounds against a clean, pure, yet inactive isoform. It’s a huge waste of time and resources.

So here’s a quick sanity checklist for you:

- Is this the isoform expressed in my system?
- Does it have the correct domains for activity?
- Am I optimizing against the therapeutically relevant variant?

Purity is great. Activity is better. But biological relevance is what drives results.

Sometimes, switching isoforms is all it takes to unlock real insight.

08/12/2025

Kinase purity ≠ kinase activity. This subtle, yet crucial point can derail entire drug development programs. Let’s unpack it.

Just because a kinase prep looks pure by SDS-PAGE, Mass-spec or HPLC doesn’t mean it’s functional.This matters especially in high-throughput screening.

But why?

Purity will certainly tell you what’s there, but activity tells you what works.

Those two can be mutually exclusive because any kinases require:
• Proper phosphorylation state
• Correct folding & domain alignment
• Specific cofactors or substrates
• Minimal aggregation or truncation

Without these proper conditions, you can have a scenario with 98% purity and 0% function.

In high-throughput screening, If your kinase is inactive, even the best inhibitors won’t show up as hits. Worse, you may flag false positives: molecules that bind dead protein, not real active sites.

Let’s say you’re using an assay that doesn’t measure activity directly, but instead looks at:
• Thermal stabilization (e.g. DSF or Tₘ shift assays)
• Ligand binding (e.g. SPR, FRET, BLI)
• Structural readouts (e.g. conformational changes)

These can show binding, even if the protein is inactive.

If your kinase is misfolded, truncated, or has an altered conformation, its active site may still have some pockets that small molecules can bind to. But these are not physiologically relevant interactions.

So what happens?

You think it’s a hit, but it’s actually a false positive. That molecule would have no effect on the active form of the enzyme in real life.

So, that’s why at SignalChem Biotech, we not only prioritize ensuring active kinases, but make sure they’re highly active. We’ve done this for over 2,000 customer publications in high impact journals.

We’ve been doing this for over 20 years, and we’ve learned one thing:

If your kinase “isn’t working,” activity is the first place you should look.

Learn more about our kinases at: https://ow.ly/8OH850WEm6R

SignalChem

10/07/2025

10/06/2025

09/10/2025

09/09/2025

09/05/2025

09/04/2025

09/03/2025

09/02/2025

08/15/2025

08/15/2025

08/13/2025

08/12/2025

Address

Opening Hours

Telephone

Website

Alerts

Contact The Business

Shortcuts

Share

Category

Monday	9am - 5pm
Tuesday	9am - 5pm
Wednesday	9am - 5pm
Thursday	9am - 5pm
Friday	9am - 5pm