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Posted by Chris on February 21st, 2018  ⟩  0 comments

What is it about a name that gives us that sense of solidity, structure and instant recognition that, as humans, we seem driven to possess? From the dawn of mankind, we have endeavored in the naming of the world around us. And for the last few centuries, modern scientists have wrestled as the current arbitrators of the naming of things, whether that be creatures or organisms, chemicals or byproducts, everything from planets, stars and galaxies to organs, cells, organelles, atoms or quarks. Scientists seem even more driven to derive the most absolute, unquestionably succinct name for each new discovery (caveat: I am fully aware that there are some notable exceptions to this statement). But it’s as if, in naming the unknown as precisely as possible, we can inherently shine a spotlight on our discoveries for all future generations. And maybe that’s the key. So much of what we work on in science is just beyond the range of what we can physically see. Nobel awards have been given to scientists for the discernment of the actual structure of the important parts of our world, such as Watson and Crick did in their discovery of the structure of DNA.

But in the darkness before discovery, figuring out what to call something is similar to the SyFy Channel‘s game show “Total Blackout” in which contestants must work while completely blind to identify things with by feel, smell, taste or sound. The results are usually humorous to those of us who can watch with special cameras. In science, the answers are often teased apart, strand by strand, sometimes even with significant setbacks, until the full understanding can be revealed. Names for these blind discoveries are given all the while, revised, debated, discarded and then eventually accepted as the norm. The history and naming of DNase is one of these kinds of discoveries.

Deoxyribonuclease, as a tool, was likely discovered via ground up bovine organs (like the pancreas, liver, or spleen) in the mid to late 1800s. Though its use was known, the specifics of what was causing the observable enzymatic reactions remained a mystery. In 1903, the enzyme was being characterized by its activity on nucleins (Araki, 1903). Later, researchers would rename it based on what they were seeing the enzyme break down; Phoebus Levene and Florentin Medigreceanu attempted to characterize it as a “thymus” nucleinase in 1911, Robert Feulgen defined it as a “nucleogelase” in 1923 and 1935, Jesse Greenstein labeled it a Thymonucleodepolymerase in 1943. Then, in 1946, Michael Laskowski stated that the name should be officially amended to either Deoxyribonucleinase or Deoxyribonuclease depending on where the hydrolysis was occurring.

The issue here is that not only were these esteemed biochemists working in the dark about the enzyme, they also suffered from a limited understanding of the particulars of the cell itself. If asked to characterize something by touching alone, how can you do so if you don’t understand the difference between round and square? It took a few more years of characterizing the nucleus of the cells, of DNA in particular, and finally the crystallization of DNase by Moses Kunitz in 1950 to firmly settle the matter of the name (Fun Fact: Kunitz was nominated 3 times for a Nobel Prize for his work in this field, but never received the award).

With the establishment of an accurate name, science can more precisely utilize a biological tool like DNase. Since Kunitz’s final characterization of the enzyme, DNase has been cited over 100,000 times in pubmed. It has been cloned and expressed in E. coli, and is even still being characterized by scientists for characteristics such as its specificity (Heddi, 2010) and binding activity. More recently, GoldBio’s DNase was utilized in the understanding of the expression patterns of Fragile X syndrome (FXS), a common inheritable genetic mutation causing autism spectrum disorder (ASD) (Wallingford, 2017).

Research such as theirs is instrumental in the continued understanding of our world and ourselves. And as we increase in our understanding of how things work, we can begin to more precisely intervene and continue the fight against the nameless (and sometimes named) monsters that still frighten us in the dark.


Araki, T. (1903). Über enzymatische Zersetzung der Nucleinsäure. Hoppe-Seyler’s Zeitschrift für physiologische Chemie, 38(1-2), 84-97.

Levene, P. A., and F. Medigreceanu. "ON NUCLEASES Second Paper." Journal of Biological Chemistry 9, no. 5 (1911): 389-402.

Feulgen, R. (1935). Über a-und b-Thymonucleinsäure und das die a-Form in die b-Form überfahrende Ferment (Nucleogelase). Hoppe-Seyler’s Zeitschrift für physiologische Chemie, 237(5-6), 261-267.

Greenstein, J. P. (1943). Tumor enzymology. Journal of the National Cancer Institute, 3(4), 419-447.

Laskowski, M. (1946). Crystalline protein with thymonucleodepolymerase activity isolated from beef pancreas. Journal of Biological Chemistry, 166(2), 555-563.

Kunitz, M. L. (1950). Crystalline desoxyribonuclease: I. Isolation and general properties spectrophotometric method for the measurement of desoxyribonuclease activity. The Journal of general physiology, 33(4), 349-362.

Heddi, B., Abi-Ghanem, J., Lavigne, M., & Hartmann, B. (2010). Sequence-dependent DNA flexibility mediates DNase I cleavage. Journal of molecular biology, 395(1), 123-133.

Wallingford, J., Scott, A. L., Rodrigues, K., & Doering, L. C. (2017). Altered Developmental Expression of the Astrocyte-Secreted Factors Hevin and SPARC in the Fragile X Mouse Model. Frontiers in molecular neuroscience, 10, 268.

Category Code: 79101

Posted by Karen on February 12th, 2018  ⟩  0 comments

With a long history of myth and tradition, the Chinese New Year (Lunar New Year or Spring Festival) still remains the most important holiday in China. It is a time for reunion, feasting, honoring ancestors and making way for a good luck. And the celebration is not limited to China. In the United States, several cities put on extravagant parades to ring in the New Year.

San Francisco

San Francisco not only claims the biggest celebration in the country, it is also the oldest. The first celebration in San Francisco happened in 1858 where Chinese traditions were incorporated into a parade with flags, drums and lanterns. Since the Gold Rush, the parade has become a mesmerizing show filled with firecrackers, dragons, lions, giants, dancers, acrobats and more.

This year’s parade starts on Market, Saturday, February 24, 2018 at 5:30 pm.

To find more information about the famous parade and surrounding events, click here.


Events in Chicago begin February 16th and run all the way through the first week of March. With one of the largest Chinatowns in North America, you can be sure to find a wealth of festivities including parades, foods and this year – puppies! You can find an events calendar here.

Chicago’s popular Navy Pier will host performances food and art. On Sunday, February 25th in Chigago’s Chinatown, you can see the annual Lunar New Year parade celebrating the year of the dog. And of course, dogs are invited to participate. If you want your pup to be in the spectacle, fill out the entry form here.

New York City

New York City has one of the highest Chinese populations outside of Asia. Therefore, it’s no surprise that this culturally diverse city would have many significant events during the Lunar New Year.

On February 16th, you can find a show featuring 600,000 firecrackers, food, crafts, lion dancers and more at Sara D. Roosevelt Park.

Also on Friday is the Lunar New Year parade in Chinatown. With it being the year of the dog, canines will have their place in the procession. To learn more about Lunar New Year events in New York City, click here.

Other cities hosting remarkable festivals include Boston, Seattle, Philadelphia and more. For an in-depth look at events in those cities, click here.

              Karen Martin
GoldBio Marketing Director

"To understand the universe is to understand math." My 8th grade
math teacher's quote meant nothing to me at the time. Then came
college, and the revelation that the adults in my past were right all
along. But since math feels less tangible, I fell for biology and have
found pure happiness behind my desk at GoldBio, learning, writing
and loving everything science. 

Posted by Karen on February 9th, 2018  ⟩  0 comments

Insects have an established history within folklore and mythology. Butterflies, bees, scarabs and other bugs have become symbolic markers of rebirth, purity, life and death. The firefly, with its enchanting light is no exception. In ancient Amazonian mythology, firefly light came from the gods and provided hope and guidance (Kritsky & Cherry, 2000). And in Japanese legend, two species of firefly, the Genji-hotaru and the Heike-hotaru, are associated with the ghosts of the Minamoto warriors and the Taira warriors. Each year in Japan several viewing festivals start up during the month of June to see the "battle of the fireflies." Fireflies, in ancient times, were also believed to offer universal remedies, counteracting poison and driving away evil (Davis, 2008).

Firefly ancient folklore and modern innovation

It’s no surprise that in modern times, we still draw from the inspiration and curiosity of the firefly’s flickering radiance. As a result, fireflies continue to fulfill their legendary roles, not quite literally, but they presently hold an important position within guidance in healing. Popularly, luciferin, the magic behind the firefly’s glow, has been used in cancer research. Scientists use the methodology behind the luciferin-luciferase relationship to study cancer metastasis and tumor growth.

But the importance of luciferin is not limited to the study of cancer. Engineers at MIT are using the glowing concept to turn plants into natural lamps. Rather than genetically altering a plant, making it capable of luciferase expression, the researchers at the Strano Lab at MIT are using nanoparticles packed with the chemical components necessary to carry out the luciferin-luciferase reaction. And so far, the team has been successful in adapting this technology in several plant types (Trafton, 2017).

While glowing plants have the potential to benefit the world, relieving us of some aspects of energy dependence, it has also allowed researchers to visualize plant reactions to certain stimulation. Back in 2000 plant geneticist Janet Braam used this iconic chemical relationship to study plants’ reactions to human touch (Riley, 2000).

Braam’s early studies showed evidence that regular human touch could negatively stunt the growth of certain plants. To further her research on this topic, she incorporated the glowing mechanism with plant "touch genes." When a plant was touched, it glowed where it was touched. Further, she observed that over time, other areas of the plant glowed causing her to suspect that the “information” traveled through other areas of the plants switching on those "touch genes" (Riley, 2000).

There are countless studies that have used this marvelous mechanism. The mysticism of these glowing creatures, along with many other bioluminescent organisms continues to inspire our curiosity and guide us on a path of unimaginable discovery.


Davis, F. H. (2008). Myths and Legends of Japan. Moskva: "T︠s︡entrpoligraf".

Hooper, R. (2013, April 14). Casting a little light on fireflies. The Japan Times. Retrieved February 6, 2018, from

Inagaki, Y., Fujioka, M., Kanzaki, S., Watanabe, K., Oishi, N., Itakura, G., . . . Ogawa, K. (2016). Sustained Effect of Hyaluronic Acid in Subcutaneous Administration to the Cochlear Spiral Ganglion. Plos One,11(4). doi:10.1371/journal.pone.0153957

Kritsky, G., & Cherry, R. H. (2000). Insect mythology. San Jose: Writers Club Press.

Riley, C. (2000, May 17). Glowing plants reveal touch sensitivity. BBC News. Retrieved February 06, 2018, from

Trafton, A. (2017, December 12). Engineers create plants that glow. Retrieved February 06, 2018, from

              Karen Martin
GoldBio Marketing Director

"To understand the universe is to understand math." My 8th grade
math teacher's quote meant nothing to me at the time. Then came
college, and the revelation that the adults in my past were right all
along. But since math feels less tangible, I fell for biology and have
found pure happiness behind my desk at GoldBio, learning, writing
and loving everything science. 

Category Code: 79101 88241

Posted by Karen on January 25th, 2018  ⟩  0 comments

They come in every GoldBio order. They show up in masses at every vendor show. And they build up into a great green pile in your lab, usually near the water baths. Green, GoldBio floating tube racks – they’re everywhere!

GoldBio Floating Tube racks - waterbath tube racks

Despite their abundance, researchers have repurposed them into other useful tools. Aside from floating microcentrifuge tubes, having so many floating tube racks means there is little fear in cutting them up and refitting them to float conical tubes.

And outside of the lab, people become even more creative. From coasters to pen holders to pin cushions, these floating tube racks have made a cameo in all sorts of unusual places.

It is for that reason, we launched a contest three years ago, discovering other creative ways researchers have used the GoldBio floating tube racks. And we’re doing it again.

Meet Ph.D. candidate Eric Samuels from the lab of Dr. Tom Poulos at the University of California, Irvine, who found a unique way to use the surplus of floating tube racks. For his son’s 

first birthday, Samuels built a busy board equipped with buttons, horns, latches, switches, clickers, spinners and GoldBio’s floating tube racks.

“I know finger dexterity is important in early development and the holes [in the tube rack] are perfect for little fingers. Additionally, the foam helps

 protect him from the corners of the board, which is why I put them there specifically,” Samuels said.

His gift for creativity and problem solving has been extremely important in the lab. Currently, Samuels’s research focuses on cytochrome P450 3A4, an enzyme in our livers that is responsible for metabolizing more than half the drugs on the market. Samuels is studying the enzyme’s mechanism of inhibition as well as designing and developing CYP34A inhibitors. By better controlling this enzyme, the same dose of a single drug would be able to pack a greater punch.

If you’ve got a knack for creativity or are just curious about the contest, visit our Facebook page. You can also find an album on our Facebook page showing archived images of previous entries. And you can enter your own creations here. Be silly, be crafty, be clever – spin however you like, share your project, get votes and win.

The first place winner of this year’s contest will receive a gift card, plaque and GoldBio Goodies.

              Karen Martin
GoldBio Marketing Coordinator

"To understand the universe is to understand math." My 8th grade
math teacher's quote meant nothing to me at the time. Then came
college, and the revelation that the adults in my past were right all
along. But since math feels less tangible, I fell for biology and have
found pure happiness behind my desk at GoldBio, learning, writing
and loving everything science. 

Category Code: 79106 79105  79101 88261

Posted by Megan on January 2nd, 2018  ⟩  0 comments

When it comes to immunological analysis, you can’t forget enzyme-linked immunosorbent assays, commonly referred to as ELISAs. This process was developed to determine the presence of antibodies in a biological sample. Samples processed may be protein mixtures from a cellular lysis or sourced from an organism being studied for infection. Data can be quantified for antigen concentration; alternatively, results are qualified for a positive or negative diagnosis.

The method isn’t as simple as tossing a solution into the assay and getting a “yes” or “no.” Immunodiagnostics are a bit more complicated than that, and some assessments can’t be accomplished with the simplest ELISA format. To compensate for these circumstances, multiple ELISA procedures have been developed. Here, we’ll differentiate the four primary categories by process, advantages and disadvantages. We’ll ascend through the list based on the process’s simplicity. 

Direct ELISA

The most straightforward version of these assays is the direct ELISA, a test capable of identifying antigens in a sample by optimizing the formation of antigen-antibody complexes.


  1. A prepared, usually diluted sample containing the antigen is incubated, promoting antigen molecules to attach against the walls of a solid-phase well plate; excess solution is rinsed away
  2. Protein additive (usually BSA) is applied to the plate to block other binding sites the antigen hasn’t covered, and the plate is washed again
  3. Antigen-specific antibody is applied and interacts with the antigens, surplus antibodies are removed by a third wash that leaves only active antigen-antibody complexes in the well
  4. The antibodies carry enzymes for identification, so enzyme substrate is added to activate with the conjugated enzymes, and the plate undergoes a final wash
  5. The enzyme reaction is measured and demonstrates antigen presence with either a colored or fluorescent signal; higher concentrations of antibody in the solution produce stronger signals
  6. The signal is quantified by a spectrometer


Direct assays are the simplest ELISA and offer the fastest performance. It is capable of providing data on antibody-to-antigen reactions by detecting the specific antigens in a sample. Even if there are few bound antibodies, the enzymes attached to these complexes will produce multiple signal molecules and trigger detection. This technique eliminates the potential for cross-reactivity because only one antibody is used.


The direct analysis produces lower sensitivity results. And there is potential for a higher background than other ELISA methods. Therefore, it’s necessary to purify your sample. In addition, enzyme-conjugated primary antibodies are uncommon and labeling them yourself is a time-consuming and expensive process.

Indirect ELISA

The indirect method is similar to direct in that sample antigen and blocking protein solutions are attached to the solid phase wells, requiring the same wash cycles and detection mechanism. The main difference exists in the antibodies: indirect ELISA primary antibody is not labeled by an enzyme when it forms its complex. Following the first three steps of the direct ELISA method, we then add the following stages.


  1. An enzyme-conjugated secondary antibody is applied to react with the attached primary antibody forming complexes with the sample antigens
  2. The secondary antibody’s enzyme substrate is then added to detect the secondary antibody and thus the antigen two molecular layers away


Indirect methods raise sensitivity because multiple antibodies attach to each antigen and their concentration is measured. Specific antibodies are detected with fewer labeled antibodies, and primary antibodies are optimally reactive to the sample antigen because they’re unlabeled. Additionally, multiple primary antibodies can be recognized by one species of secondary antibody, and there are a multitude of secondary antibodies available, making this technique versatile.


As in direct ELISA, small samples of antigen can be missed in detection if nonspecific binding occurs on the wells, so purification is often necessary. Cross-reactivity among secondary antibodies can result in nonspecific signals. The process involves more stages; if you don’t want to add extra steps to the original form, secondary antibodies may be an inconvenience.

Sandwich ELISA

Slightly altered from the first two tests, the sandwich ELISA method measures the quantity of an antigen caught between two different antibody layers. This requires a pair of molecules, one species for “capture” and the other for “detection.” Both need to be optimally reactive with the antigen of interest.


  1. A “capture” antibody is incubated and attached to the solid phase plate that is then washed
  2. Non-specific protein is added to fill open sites
  3. Sample solution with an unknown antigen (displaying at least two epitopes) is applied and captured by well-bound antibody, forming a complex
  4. Antigen-specific “detection” antibody is then added and attaches to another open epitope of the antigen
  5. If the detection antibody has been enzyme-conjugated, its enzyme is triggered by substrate
  6. There’s an additional step if another enzyme-linked secondary antibody is employed to detect the detection antibodies, totaling three antibody species; these are then detected with an enzyme substrate for measurement


Samples in sandwich ELISA don’t need to be purified as with direct and indirect versions because of the specificity involved, so this method is good for complex samples. Heightened sensitivity results from capture activity; sample antigen is detected efficiently at low or unknown concentrations. There is also the option of using either direct or indirect antibody relationships for final signal production.


Sandwich ELISA is overall difficult to optimize. The antigen being studied must display multiple epitopes for the two antibodies to react. The two (or three) antibodies involved can’t disrupt each other’s antigen complexes, so they must be “match-paired” to avoid this. “Match-paired” antibodies must be monoclonal to recognize specific epitopes. It’s difficult to find detection antibodies that are conjugated, leading to the necessity of three antibodies. On top of these complications, you add even more steps to the assay process than were involved in the first two options.

Competitive ELISA

Competitive ELISAs are the most separated in comparison to the alternate assays. This division is due to the competitive binding necessary within the solution being analyzed. Data is also assessed in the opposite way to all previous ELISAs.


  1. An unlabeled primary antibody and sample antigen are incubated together
  2. The resulting complex is applied to a plate with the same antigen coated on the wells
  3. Any primary antibodies without previous complex-binding formed during incubation will attach to the plated antigen while complexes are washed away
  4. Enzyme-conjugated secondary antibody binds to the newly bound primary antibodies, and enzyme substrate is added for signal production; weaker final signals imply a higher concentration of antigen in the original sample
  5. Other kits use labeled antigen which binds to any primary antibody not in a complex with the sample antigen, and this concentration is measured as plate-bound antibodies would be


Competing antibodies or proteins produce highly specific results in this method. Impure samples will maintain selectivity, and specific capture is helpful for detection. As with sandwich ELISA, direct and indirect processes can be used, but there is no need for match-pairing in competitive ELISA. Furthermore, there is the option of primary antibody being monoclonal or polyclonal.


Competitive ELISA operates on a different system than the previous examples, so you have to change your perspective on the operation and interpret results accordingly. The antigen of interest must also display only one epitope detectable by the primary antibody for results to be accurate.

ELISA is a versatile technique with different options to fit various laboratory analyses. Each version of the assay has different stages, benefits and drawbacks associated to it, so the informed researcher should consider these before making a decision. Choose the appropriate ELISA based on the sample you test and results you need; this will produce the most reliable, relevant data. Browse some of GoldBio's antibody labeling and protein purification products to begin your next research project.


Davis, C. P. (n.d.). ELISA Tests. Retrieved August 3, 2017, from

Giri, D. (2015, December 24). ELISA : Principle, Procedure, Types, Applications and Animation. Retrieved August 4, 2017, from

                Megan Hardie
           GoldBio Staff Writer

Megan Hardie is an undergraduate student at The Ohio State
University’s Honors Arts and Sciences program. Her eclectic
interests have led to a rather unwieldly degree title: BS in
Anthropological Sciences and BA English Creative Writing,
Forensics Minor. She aspires to a PhD in Forensic Anthropology
and MA in English. In her career, she endeavors to apply the
qualities of literature to the scientific mode and vice versa,
integrating analysis with artistic expression.

Category Code: 79104, 79107, 79108, 88221