bioCafe

Wasting Antibodies Doesn’t Float Your Boat? Try Floating Your Blot Instead!

2012-05-09T20:21:00.000+06:00

Western blots may be great for visualizing protein expression, but they can be a perfect way to waste your precious antibody stocks if you follow the normal protocol. Thankfully, you don’t have to follow the normal protocol any more; here’s how to get great blots with a fraction of the antibody usage.

I have tried several different techniques to minimize the amount of primary antibody that I use. In some labs, I have used heat-sealed bags to create a bag that is just slightly bigger than the blot. This can significantly reduce the amount of liquid required to cover the blot.

More recently, without access to a heat-sealer I turned to diluting my antibody in the smallest volume of dilution buffer possible to just cover a blot laying in a Tupperware container that is slightly larger than the blot (usually 7-10mls for a 9×5.5 cm membrane). Call me frugal, but even this approach still makes me cringe for antibodies that are diluted only 1:500-1:1000.

Floating your blot

But my newest (and now favorite approach) is one I call “floating your blot”. It requires a Tupperware container with a sealable lid and a flat bottom, parafilm, kimwipes, forceps, antibody dilution buffer and primary antibody. A 9×5.5cm membrane requires only 1mL of antibody diluted into buffer. To float your blot, follow these easy steps:
1) Cut a piece of parafilm that is slightly larger than the membrane.
2) Pipet some antibody dilution buffer without antibody (I usually use 1% low-fat dry milk, 0.1% Tween, PBS) onto the bottom of the Tupperware container and spread around using a kimwipe.
3) Lay the parafilm onto the wetted area without creating bubbles between the parafilm and the container. This sticks the parafilm to the bottom of the container.
4) Wipe off excess dilution buffer
5) Dilute antibody in antibody dilution buffer. I use 1mL for a full membrane (9×5.5 cm), and 0.5mL for half a membrane.
6) Pipette diluted antibody onto the parafilm near one end.
7) Using forceps, pick up membrane that has been incubated in blocking buffer and lay protein side down onto the diluted antibody. I lay one edge of the membrane against the liquid and allow the membrane to wick across. Keep the membrane on the parfilm and be careful to prevent any bubbles from forming between the liquid and the membrane.
8) Seal container with lid. This must be an air-tight seal or the diluted antibody will evaporate.
9) Incubate with primary antibody using conditions optimized for the antibody.
10) Remove blot into new container for washes.
11) Technique can be repeated for incubation with secondary antibody if desired. I wish I could take the credit for thinking of this on my own, but I didn’t. A colleague showed me this trick and it really helps me save my antibodies.

Author:

Rebecca Tirabassi, BitesizeBio

Protest SOPA: Black Out Your Website the Google-Friendly Way | Webmonkey | Wired.com

2012-01-19T14:59:00.000+06:00

Protest SOPA: Black Out Your Website the Google-Friendly Way | Webmonkey | Wired.com:

'via Blog this'

How To Read Manuscripts (and anything else) Twice As Fast

2011-06-13T18:49:00.003+06:00

I always thought that doing a speed-reading course would be a good thing to do as a scientist. With the amount of literature we need to consume, speed-reading (the art of reading faster without reducing comprehension) would save a lot of time.

But it turns out that you don’t really need to spend any cash on a course to teach you to read more quickly. There are some pretty simple steps that you can use to dramatically improve your reading speed that won’t cost you a penny.

The basic principles are:

1. Use a tracer, like a pen, or your finger, to trace under each line as you read it, as if you were underlining. You do not read text in a continuous line, but in a sequence of jumps, each of which ends with a temporary snapshot of the text within you focus area. Subconsciously, you will spend a lot of time re-reading and skipping back to previous snapshots. Using a tracer helps your eye focus and prevent this from happening.

2. Train yourself to use your peripheral vision as you read. When we read, we tend to focus just on the words that are in our central focus in each snapshot. But you can train your eye to use your peripheral vision too and so multiply your reading power.

10 minute speed-reading training
The following 10 minute training routine is based on these principles. I’ve tried it a few times recently and have seen a notable improvement in my reading speed:

1. For 2 minutes: Practice reading as fast as possible, using a tracer to guide you. Don’t worry about comprehension to begin with – that will come.

2. For 3 minutes: Train your eye to use your peripheral vision by focussing on the THIRD word and the the THIRD FROM LAST word in each line.

e.g. if the line was this, you would focus on the underlined words:

“We wish to suggest a structure for the salt of deoxyribose nucleic acid (D.N.A.).”

As you practice this and it becomes easier, you can start to move your focus into the fourth and fourth from last words and so on.

3. For 2 minutes: Practice reading each line in only two snapshots using your focus on the third and third from last words as an anchor.

4. For 3 minutes: Read too fast. Using techniques 1-3, practice reading too fast for comprehension for a couple of pages and then (still using the techniques) slow down to a pace that you can comprehend the text. This will help accustom your brain to reading more quickly — a bit like when driving a city speeds seems very slow when you have just come off the motorway.

Obviously the more you repeat the cycle, the faster you will get. If you have a go, please drop me a comment – I’d be interested to hear how it went for you.

ps: If you want to monitor your progress, measure your reading speed (words per minute) before and after. You can calculate the average number of words on a page by calculating the average number of words in 10 lines, then using this to calculate the average number of words per page and so on (but you don’t need me to tell you that!

by Nick Oswald in Organisation & Productivity
From BiteSizeBio

Celebration of Independence Day of Philippine at IRRI, 2011

2011-06-12T12:37:00.001+06:00

How a Jellyfish Changed Biology: the discovery and development of GFP

2011-05-19T18:29:00.001+06:00

Fluorescent tags are widely used for microscopy and expression studies – but it wasn’t so long ago that this everyday tool was unheard of. In this article we’ll talk about how GFP came to be, and what it means for you.

Green fluoresecent protein, or GFP, was first identified in a fluorescent jellyfish, Aequorea victoria. Osamu Shimomura purified GFP and described the biophysics of how it fluoresces. A few years later, Martin Chalfie reported the expression of this protein in E. coli and C. elegans. Roger Tsien is responsible for designing variants on the protein – single amino acid changes that yielded cyan, blue and yellow fluorescent proteins, and the enchanced green protein (EGFP) that is commonly used today. Shimomura, Chalfie and Tsien were awarded the Nobel Prize for Chemistry in 2008 for their work in the discovery and development of this tool. What made GFP such a game changer is the fact that it’s “auto-catalytic” – it doesn’t need any co-factors or enzyme processing to fluoresce – so it can be easily used in a wide variety of organisms.

The major applications for GFP proteins are microscopy based, since its primary value is as a visual marker for protein detection. Here are a few of the most popular ways to use GFP:

1. Translational fusion
One of the most common uses is a fusion marker, where the GFP open reading frame is cloned downstream of your favorite ORF, so that it is translated as one long protein, fusing your favorite protein to GFP. That way, wherever your protein is expressed you will see green fluoresence. This can be used in still images and is striking in images of live cells, as you can track the location and movement of proteins.

2. Transcriptional fusion
GFP can also be used in “transcriptional fusion”, where the expression of a gene and GFP are driven off the same promoter, but with an intervening stop codon. In this case, cells expressing the first gene will fill with soluble GFP – resulting in easy detection of the particular cells expressing your protein.

3. FLIP and FRAP
FRAP (fluorescence recovery after photobleaching) and FLIP (fluorescence loss in photobleaching) rely on the fact that a single GFP molecule emits fluorescent light when it’s excited, but cannot do so indefinitely. Eventually it either bleaches out or stops emitting. So, to study the dynamics of a GFP-labeled protein, you can bleach a small area of a cell and determine how long it takes fluorescently labeled protein to “leak” back into the bleached area (FRAP), or how much fluorescence decreases overall in the rest of the cell as the bleached proteins diffuse (FLIP).

4. FRET
FRET (fluorescence resonance energy transfer) is based on the different excitation and emission spectra of the different variations on GFP. In this case, two proteins are labeled with two different fluorophores, which are carefully selected so the emission spectrum of the first overlaps the excitation spectrum of the second. The cells are then imaged using a laser that excites only the first fluorophore – so the second only lights up if the two proteins are in close enough proximity that the first fluorophore sets off the second.

Check out some of the seminal papers written about GFP:
Green fluorescent protein as a marker for gene expression.
Chalfie M, Tu Y, Euskirchen G, Ward WW, Prasher DC.
Science. 1994 Feb 11;263(5148):802-5.

Wavelength mutations and posttranslational autoxidation of green fluorescent protein.
Heim R, Prasher DC, Tsien RY.
Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12501-4.

A post from bitesizebio.

2011-05-11T15:42:00.005+06:00

Antibiotic selection is always a tool of great importance in molecular biology. But Ampicillin as an antibiotic, everyone faces a problem to some extent. The following artical is from BitesizeBio gives some helpful tips to overcome this problem.

Ampicillin is commonly used as a selection marker for plasmids in gene cloning and protein expression in E.coli and other bacteria. While it serves it’s purpose, there can be problems using this selection marker if the user is unaware of it’s limitations. This article provides a quick overview of what these limitations are and how to avoid them.

The basis of ampicillin selection is the hydrolysis and inactivation of the antibiotic by beta-lactamase expressed from the plasmid-borne bla gene. Here’s the problem: beta-lactamase is secreted by the bacteria. The resulting build-up of extracellular beta-lactamase can inactivate the ampicillin in the culture medium, removing the selective pressure, if the culture is not handled properly.

In liquid cultures, this means that a portion (possibly a very large portion) of the cells no longer have the plasmid, giving poor yielding plasmid preps, protein expression etc. On agar plates, ampicillin degradation can lead to the formation of satellite colonies on transformation plates. Satellite colonies are very small colonies of cells that have not taken up the plasmid that form around a large colony that has taken up the bla-containing plasmid. The satellites form because the beta-lactamase released by the bla-expressing colony degrades the ampicillin in the vicinity of the colony. The satellites are not necessarily a problem as they will not grow when transferred to a medium containing fresh ampicillin.

So how do you avoid plasmid loss when using ampicillin as a selection marker? Here’s how:

## Don’t allow liquid cultures to saturate for too long. I would recommend never growing cultures higher than OD600=3 (in LB)
## If you are using a starter culture, always pellet and re-suspend the starter culture in fresh, antibiotic-free medium before innoculating the main culture. This is to remove the secreted beta-lactamase from the medium.
## Use a higher ampicillin concentration if you are experiencing problems. I would recommend using 200 micrograms per mL or higher. This makes it harder for the beta-lactamase to inactivate all of the ampicillin and is especially useful for avoiding satellite formation.
## For the same reason, never use old ampicillin stocks or plates as the ampicillin will have broken down somewhat, giving a reduced effective ampicillin concentration.
If all else fails, switch to carbenicillin selection. This antibiotic is also inactivated by beta-lactamase but more slowly than ampicillin is. For this reason carbenicillin selection is far more effective than ampicillin. Unfortunately it is much more expensive!

কৃত্রিম মস্তিষ্ক তৈরির পথে অগ্রগতি! - প্রথম আলো

2011-04-27T11:44:00.000+06:00

কৃত্রিম মস্তিষ্ক তৈরির পথে অগ্রগতি! - প্রথম আলো

The Young Parliament-andalib

2011-03-28T17:47:00.000+06:00

This Is The Young Parliament-andalib

Live Online Radio : Find the best free Internet Radio, AM and FM stations, and Live web Radio

2011-02-16T18:58:00.000+06:00

Live Online Radio : Find the best free Internet Radio, AM and FM stations, and Live web Radio

Coca Cola Original recipe

2011-02-16T07:15:00.005+06:00

Coca Cola is popular drink for so many years ... but its recipe was kept secret. The only written known is stored in a volt at atlanta. But recently a very old photograph is published which shows the secret recipe of Coca Cola.

Want to try at home?

NASA Probe Has a Valentine's Date With a Comet

2011-02-15T16:01:00.000+06:00

NASA Probe Has a Valentine's Date With a Comet

Eat Bread !!!!!!!!!

2011-02-11T18:33:00.003+06:00

Kittiwat Unarrom, a talented artist from Thailand, uses his skills to create unique loafs of bread shaped like various human body parts.

Kittiwat has experimented with many art forms, from painting to sculpting, but it wasn't until he had to return home and take over the family bakery that he discovered his true passion - making grotesque-looking bread. Since he first started out, in 2006, he has made a name for himself, and his Body Bakery has become a popular tourist attraction.

The gruesome bread Kittiwat Unarrom makes is incredibly realistic looking, but to achieve this level the artist spent many hours studying human anatomy and visiting forensic museums. At the same time, he found it important to make his bread delicious as well, because he didn't want his art to be just an object of art, he wanted audiences to feel involved. His first batch was pretty good, but it wasn't delicious, so he kept improving the recipe until he got the taste just right.

When he first started working at his family's bakery, he was convinced he wasn't going to get to practice his art anymore, but as soon as he discovered dough, he realized the possibilities are endless. Every day he works with the dough he gets new ideas about new edible art projects, and he believes art shouldn't be limited to art galleries and museums.

His body-part bread looks just like the real thing, but he admits it's pretty strange eating someone's head, piece by piece, and looking in their eyes at the same time. In case you were thinking of going to Thailand for a piece of human-looking bread, forget about it, Kittiwat's bakery is only selling normal bread, at least for the moment.

From: Fropki.

My wedding : second session

2011-02-11T11:08:00.002+06:00

My actual wedding took place on January 7 2011. After that staying a week there I came to LosBanos to my work place. I was invited for a simple dinner to some of my friends here. To my surprise they arranged a crazy program. That was something I will remember throughout my life. Thank you guys for the nice evening.

Here are the videos of that event.

Part 1

Part 2

Thanks Andy, Aryo, CJ, Park, Manish, Diago and also Jasmin :)

2011-02-10T00:28:00.001+06:00

ভাষার সুপারপাওয়ার পাপুয়া নিউগিনি

2011-02-04T06:30:00.001+06:00

ভাষার সুপারপাওয়ার পাপুয়া নিউগিনি

Six New Planets: Mini-Neptunes Found Around Sunlike Star

2011-02-03T16:22:00.000+06:00

Six New Planets: Mini-Neptunes Found Around Sunlike Star

Ultimate Adventure Bucket List -- National Geographic Adventure

2011-01-21T13:38:00.000+06:00

Ultimate Adventure Bucket List -- National Geographic Adventure

Science communication in the 70’s – a unique take on protein synthesis!

2010-12-07T20:09:00.000+06:00

প্রথম আলো - সবচেয়ে ছোট হোটেলে মধুচন্দ্রিমা

2010-12-06T12:09:00.000+06:00

প্রথম আলো - সবচেয়ে ছোট হোটেলে মধুচন্দ্রিমা

এটি ২৮২ বছরের পুরোনো একটি হোটেল। নবদম্পতিদের মধুচন্দ্রিমার জন্য সম্প্রতি একটি প্যাকেজ ঘোষণা করেছে হোটেল কর্তৃপক্ষ। এই হোটেলের বিশেষত্ব হচ্ছে, এটি এত ছোট যে, সেখানে একসঙ্গে দুজনের বেশি থাকা যায় না। বিশ্বের সবচেয়ে ‘ছোট’ বলে খ্যাত এই হোটেলে এক রাত কাটাতে খরচ হবে মাত্র ২৪০ ইউরো।
হোটেলটির নাম এহয়জেল (বিয়ের ঘর)। জার্মানির বেভারিয়ান শহরে এটি অবস্থিত। ১৭২৮ সালে নির্মিত এ হোটেলটি মাত্র আড়াই মিটার চওড়া। বেভারিয়ানের তখনকার স্থানীয় শাসক ঘোষণা দিয়েছিলেন সম্পত্তি (ঘরবাড়ি) ছাড়া কোনো দম্পতি বিয়ে করতে পারবে না। এরপর দরিদ্র দম্পতিদের সুবিধার জন্য এ হোটেলটি নির্মাণ করা হয়। এটি এতই ছোট যে, মাত্র এক দম্পতির জায়গা হবে এতে।
হোটেলের মালিকেরা দাবি করেছেন, এটিই বিশ্বের সবচেয়ে ছোট হোটেল। তাঁরা বলেন, হোটেলটি খুবই সাদামাটাভাবে তৈরি করা হয়েছিল। তখনকার রীতি অনুযায়ী নবদম্পতিরা এটি স্বল্প সময়ের জন্য কিনে নিতেন। সেখানে কিছুদিন কাটানোর পর এটি আবার আরেক নবদম্পতির কাছে বিক্রি করে দেওয়া হতো।
দীর্ঘদিন বন্ধ থাকার পর সম্প্রতি হোটেলটি ফের চালু করা হয়েছে। যুগের দাবি মেনে এটি আধুনিকও করা হয়েছে। ওপরে বাড়িয়ে সাততলা করা হয়েছে। পাঁচ তারকা হোটেলের সব সুযোগ-সুবিধা নিশ্চিত করা হয়েছে এতে। ফায়ারপ্লেস ও বিলাসবহুল স্নানাগারও রয়েছে সেখানে।
সম্প্রতি বারবারা ও হাইঞ্জ ভিলহেম নামের সত্তরোর্ধ্ব এক দম্পতি এই হোটেলে রাত কাটিয়েছেন। এই দম্পতি বলেন, ‘পৃথিবীর অনেক হোটেলে আমরা থেকেছি। সেসব হোটেলে আমাদের পাশাপাশি আরও অনেক অতিথি ছিলেন। কিন্তু এই হোটেলে আমরাই কেবল অতিথি।’
হোটেলটির আধুনিক সাজসজ্জার নকশা করেছেন মারিয়ান্না লস। তিনি বলেন, ‘হোটেলটিকে নতুন রূপে সাজানোর ক্ষেত্রে অনেক বাধা পেরোতে হয়েছে। নবদম্পতিদের মধুচন্দ্রিমার ক্ষেত্রে হোটেলে কিছুটা ছাড় দেওয়া হয়েছে।

Top Ten Discoveries of 2010: Nat Geo News's Most Popular

2010-12-03T06:50:00.000+06:00

Top Ten Discoveries of 2010: Nat Geo News's Most Popular

A team of evangelical Christian explorers claimed they'd found the remains of Noah's ark beneath snow and volcanic debris on Turkey's Mount Ararat (pictured) in April.

But some archaeologists and historians took the latest claim that Noah's ark had been found about as seriously as they had past ones—not very.

Nat Geo

Pictures: Medieval Cave Tunnels Revealed as Never Before

2010-12-02T08:45:00.000+06:00

Pictures: Medieval Cave Tunnels Revealed as Never Before

এক্সক্লুসিভদরিদ্রদের 'ইউনূসফাঁদ' | bdnews24.com

2010-12-01T16:26:00.001+06:00

এক্সক্লুসিভদরিদ্রদের 'ইউনূসফাঁদ' | bdnews24.com

How to Shine in a Small Biotech Company

2010-11-29T19:39:00.000+06:00

So you finally got your PhD (or your masters or batchelor’s) and you are making the big switch to a small biotech company.

You will probably have been hired for the specific skill set that you have built during your training, but now you have to learn to apply those skills to solve real world, commercially-driven scientific problems. The future of your new employer, and your job, will depend on it.

Working in a small biotech company is completely different from academia. There is much less of a support structure around you so have to learn to support yourself and others. You need to tap into the experience and knowledge of those around you, contribute to the knowledgebase and take responsibility for your own development.

A small biotech company needs to be a team much more than an academic group does. They need to pull together to reach their goals. And you need to be an integral player.

More than that, to make sure that you and your career prospects shine, you should set out to be the star player. Here are some tips that I think will help you to do this:

1. Keep the company’s goals in mind

The first thing you should strive to understand is the company’s commercial goals and how your work fits into them. Understanding this will help to keep you motivated, but it will also help you to stay focused in your research. Your company wants results that will build a path towards the profits it needs to make it a success. It does not care about the “interesting” detours and neither should you, but to stay on the path you need to know the intended destination.

2. Don’t assume others know what approach is best

In the first biotech company I worked for, I came straight out of my PhD and landed in an excellent group of people who were all trying to solve the same problem. Within two weeks, I had actually pinpointed a crucial flaw in their approach, but I assumed that I was wrong. 6 months later I started talking about what I thought the problem was and stimulated a discussion that ended up with a radically new, and entirely successful approach. Obviously I should have started talking much earlier as it would have saved a lot of time, money and heartache.

My mistake was that I deferred far to easily to those around me, assuming that they knew much more and had it covered. Thinking like this is not good in any organisation, but is especially damaging in a small biotech company because the team tends to be a lot more threadbare.

It could be that the people who are more experienced than you are having to wear a number of different hats so are more likely to miss small details, or it could be – as it was in the case I just described – that the problem fell between the cracks of the different disciplines being applied to the problem.

Whatever the case, in a small biotech company, perhaps more than in any other early career scientist position, your opinion matters and it is your job to voice it.

3. Go cross-disciplinary

Many biotech companies are trying to solve problems that are interdisciplinary, which means that the solution lies in the no-man’s-land between the disciplines, as was the case in (2) above. It is very difficult for employers to find people who are cross-disciplinary so to prosper in a company like this, you should learn about the other disciplines involved in the project and help to plug the gaps. You can do this by reading or just actively learning from your colleagues.

It takes a lot of effort to do this, but it is worth it because it is in that no-man’s-land that you can help establish yourself as an expert in the problems that the company are trying to solve and become a vital member of the team.

4. Teach others what you know

As well as trying to plug the inter-disciplinary gaps in your own knowledge. It pays to freely share your own knowledge with your colleagues. Think of it as Karma. You help them, they help you and you all benefit, as does the company.

5. Write SOPs

The ultimate way to share your knowledge is through writing standard operating procedures (SOPs) on the procedures you perform. SOPs are vital for ensuring that things are done uniformly across the company, but they are often overlooked because everyone, especially the management, are too busy to think about them.

If you are new to the company, a great thing to do it to start to establish an SOP-culture. It is easy to set up a word template for writing up SOPs, set aside a folder to keep them in, and an Excel file to list them. There are more advanced ways to do it of course, but even this is infinitely better than having no SOPs. Talk about it with your manager and your colleagues to get their buy-in first of course.

6. Ask questions – promote discussion

In any lab meeting or discussion you should aim to actively contribute. Its easy to sit back and listen, but that’s not your job. You should be trying to contribute new ideas or increase the understanding of yourself or others on the subject being discussed.

If you are nervous about this, one great way to get started is to challenge yourself to ask at least one question at each meeting. It does not matter what you ask – just ask something, and you’ll soon get into the habit.

7. Push new technologies and ideas

In a hard-pushed company and without a large community of scientists around it is easy to become isolated from new technologies and ideas. Strive to keep abreast of the new technolgies in your field and if you find something you think is useful, research it carefully to ensure you know what you are talking about and then put it forcefully to the group. Whether or not your idea is taken up you will be doing them a service.

8. Improve your existing skills

I have talked so far about branching out into new areas of knowledge to help become an integral part of your group. But it is also very important to polish your core skills as highly as possible. Whether you were brought in to group because of your specific abilities, or you were given a specific role to learn, your company depends on you to be an expert. You might even be the only one that they have.

9. Keep meticulous records, and make them as accessible as possible

During your PhD your lab book was your own, and if you didn’t keep it well it was only you who suffered. But in your close-knit biotech research team, anyone could need to access your results.Â And more to the point, your results are the property of the company you work for.

Make a point of keeping your records very accurate and easy to navigate and you will not only be doing a great job, you will also gain a reputation for being accurate and reliable. A simple lab notebook admin system might help.

10. Dress for the part when needed

Whenever you receive visitors, go out to a collaborator or attend a conference you are representing your company so jeans and t-shirt might not be the order of the day. You need to dress for the part, which – shock horror – might involve wearing a suit, or even shining your shoes! Check with your boss what the dress code should be for events like this, and stick to it.

11. Don’t let your science get sloppy

Often your work will not be published when you work in biotech, but it will remain part of the internal knowledge of the company. But just because your work is not peer-reviewed does not mean you can afford to let your science get sloppy. In fact in many ways it is more important than ever to be stringent with your work because the tools you make or the conclusions you draw will become part of the framework upon which your colleagues build.

n=1 is not good enough and neither are plasmids checked only with a quick digest. You have to be meticulous and you should be vocal in ensuring that others in the group are doing so too.

12. Don’t talk about your “results” until they are in the bag

I think I have finally got expression from that plasmid. Oh wait, no, it was just a squashed fly on the gel.

I was very guilty of this when I worked in the lab. I got so excited about possible results that I would blab about them before I had confirmed them. This is not a good strategy because if you do it often enough it will damage your reputation. Keep things under your hat until you are certain about them.

13. Never, everÂ make your boss look bad

This is true in any job. And the title says it all.

14. Learn to resolve conflict

In any small team, conflicts will arise. Try to work on being the kind of person who snuffs out conflicts at source, rather than the sort who lets things rumble on and on for months or even years. The reduced stress alone will probably add years to your life!

15. Be cheerful

Life can be tough in a small biotech company. There are a lot of pressures, especially when the science isn’t going well. Strive to be cheerful and inspire those around you to do the same. Cheerfulness, even in adversity, is a great attribute to have as a team member, but also marks you out as a great leader for the future.

Those are my tips for prospering in a small biotech company. Do you agree with them, or do you have some of your own? Let us know in the comments.

Nick; BitesizeBio

Explosion in Korea

2010-11-28T18:38:00.000+06:00

Explosion in Korea The risk in modern hi tech society.

Making a difference in the developing world – Katarlah Taylor from CGIAR

2010-11-17T15:17:00.000+06:00

Making a difference in the developing world – Katarlah Taylor from CGIAR