Boster offers 9,000+ recombinant proteins and the recombinant protein expression
service. From small scale feasibility studies to industrial production of recombinant proteins, let our
experienced scientists help you with
your expression and purification needs.
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Boster offers a comprehensive selection of recombinant proteins for your research. Over 9,000+ recombinant proteins from human, mouse, rat and a variety of species, these proteins are expressed in E. coli as well as eukaryotic systems.
Boster also provides recombinant protein production service. If you are seeking a vendor for expressing your protein of interest, use our recombinant protein expression expertise for fast and affordable feasibility assessment. If you already have the optimal expression conditions figured out, we can help you scale up to industrial production of the recombinant protein. Send your inquiry to [email protected] for a custom quote.
A brief history of recombinant technology and core concepts.
A recombinant protein is a protein produced artificially by an expression host organism, aka expression system, that is transfected with a recombinant gene (target gene) isolated from another organism. The purpose is to produce the target gene encoded protein in large quantities for medical, research and academic uses.
Early 1950s discovery of DNA plasmids directly led to the field of recombinant DNA (rDNA). Peter Lobban from Stanford University Medical School first proposed the recombinant DNA idea in the early 1970s. The first successful production of recombinant proteins is documented in 1972 and 1973 from Stanford and UCSF. Several people were awarded the Nobel Prize for contribution to the recombinant technology.
The pharmaceutical industry has been utilizing recombinant technology for producing
protein drugs since the early 1980s. One of the most impactful achievements of recombinant
protein technology is the production of recombinant protein insulin. Before recombinant protein
insulin is made, diabetes treatment largely depended on insulin from animal sources. The
recombinant insulin significantly lowered treatment cost and enabled a consistent and sufficient
worldwide supply for diabetes treatment. The discovery of restriction enzymes and ligases
catapulted the field to the ability to insert foreign genetic material and proliferate in a
bacterial system.
Restriction enzymes, more precisely restriction endonucleases, cleave DNA with high specificity in pre-defined cleaving patterns, making them the backbone of recombinant technology. Under the guide of their enzymatic properties, restriction endonucleases are able to cleave plasmids and insert the foreign gene of interest. Further characterization analysis is realized with the enhanced expression.
Individual restriction enzymes recognize specific sequences, referred to as restriction
sequences. Restriction sequences are palindromic sequences, usually 4 to 8 base pairs long.
Palindromic sequences read the same in both the upstream and downstream direction. When restriction
enzymes find these restriction sequences, they cleave the covalent bond of either the pyrimidine (T
and C) or purine (A and G), generating a 5’ phosphate and a 3’ hydroxyl group at the cleavage
point.
This cleavage leaves behind blunt ends with no overlap, therefore they can no longer base pair with other nucleotides. Other types of restriction endonucleases leave sticky ends. These sticky ends are single strand overhangs that extend beyond the cleavage site that may further bond with other nucleotides. Sticky ends come in handy when the same restriction enzyme is used to cleave both the fragment of interest and the vector. This cleavage will leave identical overhangs that a ligase will bind (ligation), resulting in your recombinant product (rDNA, protein, etc.).
There are several common expression systems for producing recombinant proteins, such as E. Coli, Yeast, Insect Cell lines such as Sf21, mammalian cells such as CHO, HEK, and human cell lines. These expression systems act as the factory for recombinant protein production, where the cellular mechanisms involved in protein production use the recombinant gene in the vector as a blueprint to mass produce the target protein.
E. Coli is the first organism, and still often the first choice, to be used as an
expression system. It is easy to use, however cannot produce protein with post-translational
modification (PTM). E. Coli lacks the cellular mechanisms of eukaryotic cells which are necessary
for PTM of proteins. Thus, for producing simple proteins and for applications that do not require
proteins to have PTM, E. Coli is a sufficient and convenient expression system. For more complex
applications, more advanced expression systems are required.
A vector is a tool for manipulating DNA. It is the transport vehicle for the gene of the protein of interest. There are many types of vectors; some common vectors are plasmids and reverse transcription viruses. The DNA that encodes the protein is first synthesized in vitro, or cloned from native host DNA templates, then inserted into the vector DNA. The host organism is processed to take up vectors. Expression vectors, once inside the corresponding host cells, will be both transcribed and translated into proteins. They are engineered specifically to enhance the expression of target proteins.
Vectors are known for producing high numbers of copies, as it is exceedingly efficient in self-replication. It is utilized as a carrier of foreign passenger DNA, to be introduced at the restriction enzyme’s cleavage site. Engineered vectors may have many recognition sites; >20 recognition sites are referred to collectively as Multiple Cloning Sites (MCS). There are many commercially available vector types for cloning and expression studies. Vectors are chosen for their ability to overexpress and produce high numbers of the proteins of interest from the carrier plasmid.
Just like the decision of which vector to use, the importance of the choice of
appropriate biological system, often bacterial, cannot be understated. These systems are referred to
as “protein factories”, as the necessity of a robust system is mandatory for overexpression and
protein production.
Once cloning of the recombinant protein of interest is completed, the protein must be purified. Structural and functional studies, along with high-throughput and large-scale production, require proteins to be >95% pure.
Ion-exchange, affinity chromatography, and gel filtration are the most common purification techniques used to elicit the different inherent properties of proteins. Proteins are studied for structural analysis, and biochemical, immunological and functional testing. The goal of protein purification is to separate the target protein from the components necessary for replication, without influencing the activity and integrity of the protein. While purification techniques and rigor may vary depending on model organism and specific analysis goals, the principles remain the same. Choosing the appropriate purification technique for your system is based upon properties such as the average pKa of ionizable protein side chains, the isoelectric point, pI, and the extinction coefficient, Ɛ.
separates polar molecules based on their affinity to the charge on the column substrate (ion exchanger). Proteins are made up of zwitterionic amino acids. Zwitterions contain both positively and negatively charged moieties that may be targeted by ion-exchange chromatography.
is a type of purification based on the binding interaction, or affinity, of an immobilized ligand or biological agent to its binding partner, often utilized with affinity tagged fusion proteins. In other words, a ligand that binds to the target protein is covalently bond to the stationary phase.
Affinity chromatography is favored for many protein purifications due to its high specificity. Affinity tagging, as discussed below, can further take complicated, insoluble proteins down to a one-step purification with high purity.
is a type of size-exclusion chromatography in which the stationary phase is a porous gel. Target compounds are separated based on size, or even molecular weight. Gel filtration is beneficial for separating out large and small biological samples to determine molecular weight or perform a molecular weight distribution analysis.
Insoluble or otherwise difficult to purify recombinant proteins are often labelled with ‘tags’, or joined with other proteins as ‘fusion proteins’. These fused products facilitate the purification and recovery thereof via affinity purification with a stationary phase that has an affinity for the tag or fused protein. Tags may be added to either the N- or C-terminus of the expression protein. Tagged systems may be used to avoid many of the difficulties encountered during protein purification.
Examples of highly popular pairs are the His-tag (poly histidine tag), the MBP-tag
(maltose binding protein), and the GST-tag (glutathione-S-transferase). These tags are typically
utilized to render a soluble protein product that is normally expressed in an insoluble form, and
other desirable purification enhancers. Affinity purification such as nickel-chelate chromatography
is commonly used with His-tag proteins, as they have high affinity and specificity for the ions of
nickel and other metals. Finally, the tag must be easily removed after purification to ensure no
effect on the protein’s function or activity upon analysis.
Library creation
Molecular weight, structure, etc.
Pest or drought resistance
HIV, hepatitis
e.g. Cystic fibrosis
Vaccines, medications such as insulin
These are the top 100 popular recombinant proteins. Check out the full list here: browse all recombinant proteins
Here are some quick facts about bosterbio.com
Boster antibodies and ELISA kits are cited over 60,000+ times in publications around the world. According to the big data research company CiteAb.com, Bosterbio is globally the fastest growing antibody company in terms of the number of academic publication citations. For Picokine® ELISA kits specifically, an estimate of 6000+ publications are available. You can find specific citations for ELISA kits and antibodies on each product page.
What life scientists are saying about Boster ELISA kits
Maria Teresa Dell'Anno
Postdoc
This Antibody Works Perfectly!
I used it for IHC on frozen sections at a dilution of 1:500. It did not need several trials to optimize the protocol. No bad things overall. I will purchase it again.
Immunohistochemistry , Spinal cord , Confocal microscope
Hanjo Hellmann
Associate Professor
Verification Of Antibody On Recombinant Protein
We tested the antibody against recombinant GST-tagged BnaA07g20720D protein. As controls, we used another GST-tagged protein GST-MYB25, and GST alone. The antibody was well capable of detecting specifically BnaA07g20720D. We loaded ~100 ng of either GST:BnaA07g20720D, GST:MYB25, or GST alone, and the antibody was very specifically detecting BnaA07g20720D. It did not cross-react at all with the other two proteins. Highly specific. I would highly recommend the antibody for basic western-blot analysis of purified proteins. Probably one can significantly reduce the dilution to 1:10000 to still get a good result. Unfortunately, we did not have the opportunity with good controls to verify how the antibody works on whole plant extracts or for IP experiments.
Western Blot , Recombinant protein expressed in and purified from E. coli , Chemiluminescence
Ramaz Geguchadze
Research Scientist
A Good PKC Alpha Antibody For IP And WB
We used Anti-PKC Alpha Picoband™ Antibody for immunoprecipitation experiment from neuronal cells in order to characterize PKC Alpha expression in different conditions. Strong positive band with right mass. Works great without optimization! Good quality and ready for publish Ab
Western Blot , Dorsal root ganglia (neuronal cells) , CyDye
Dinesh Joshi
Research Scientist
Best Calbindin Antibody For IHC In Mouse Cerebellum
I tried this antibody for Purkinje cell labeling in mice cerebellum using IHC-P. Antigen retrieval - 20min boiling in EDTA based buffer. Permeabilization - 0.3% triton for 15min. Blocking - 10% goat serum for 1hr. Primary antibody - 1:250 overnight at 4 Degree C. Secondary antibody - Fluorescence conjugated secondary antibody at 1:250 for 2hr at RT. I was amazed to see the beautiful dendrites, soma and axons. In my hand, this is the best labeling of Purkinje cells I have ever seen using IHC-P. Beautiful labeling of Purkinje cell soma, dendrites and axons. Best antibody I have used till now. Highly recommended for IHC-P.
Immunohistochemistry , Mice Cerebellum , Fluorescence
Jakub Famulski
Principal Investigator
Good Zebrafish Antibody For Nlz2
Zebrafish-specific antibody. Used in whole mount IF on 24hpf zebrafish embryos. The signal is not precisely clean, but we do observe nlz2 expression in the ventral region of the retina as expected from in situ hybridization results. This antibody shows some promising results in whole mount applications using 24hpf embryos. Applications with cryosections may be more precise.
Immunohistochemistry , Zebrafish embryos 24hpf , Confocal Microscopy
P DPN
Postdoctoral Researcher
Awesome Kip2 Antibody From Boster Bio
We've been using this Ab for several months, and it's been working great. We have already ordered several vials of this Ab for detecting podocytes in mice kidney. We used an autostainer machine for the process. With this Ab dilution, and using EDTA for Ag retrieval, we had the least background. Easy to use, works every time. Worth it.
Immunohistochemistry , Mice kidney , DAB chromogen
Sanjay Arora
Graduate Student
Quantification Of BDNF Post-Transfection In Primary Neuronal Cells
The kit was used to quantify amount of BDNF produced after transfection with plasmid DNA encoding human BDNF using non viral vector, liposomes. Provided good reliable quantification of BDNF produced. No interference. Good reproducibility. Reliable estimation, good sensitivity. Reasonable price as well. Would purchase again." (Customer’s Tip: "Don't dilute sample, assay directly.
ELISA , Cell lysate and culture medium
Sanjay Arora
Graduate Student
Adiponectin Analysis in Mouse Serum and Culture Media
I used this kit to quantify adiponectin adipokine in cell culture supernatant (3T3-L1 cells) and mouse serum (C57BL6 mice on control/ western diet). The goal was to check if western diet treatment reduced serum and tissue adiponectin levels. The results were reasonable and reproducible. Although we had to use two different standard curves for high and low concentration estimations. Performing a standard curve with each sample helped. Reliable estimation, good supplier, reasonable price. Will keep using it." (Customer’s Tip: "Dilute tissue homogenate 1:100, use serum directly.
ELISA , Serum, tissue homogenate
Swati Naphade
Postdoctoral Fellow
Good TIMP-1 Antibody for Western Blotting
We study neurodegeneration in our lab and I was looking for an antibody for human TIMP-1. The antibody detects a band at 28kD, which is the predicted molecular weight of TIMP-1. Good antibody for TIMP-1, cleaner than other antibodies I have tested. In summary, this antibody is good for human samples and I highly recommend it.
Western Blot , Human NSC cell lysates , ECL chemiluminescence
Peter J. Thompson
Postdoctoral Scholar
This Antibody Gives Strong Membrane Staining
CD47 is broadly expressed in many cell types. This antibody gives strong membrane staining throughout many of the beta cells (Insulin-positive) in the immune cell infiltrated islets of NOD mice at age 12 weeks.
IHC-Paraffin, IHC-cryo , NOD/ShiLtJ mouse pancreas sections, formalin-fixed paraffin embedded , Zeiss Apotome widefield fluorescence microscope
Chi Li
Professor
The Signal Was Very Strong And Clean!
Thirty micrograms of whole cell extract of pancreatic tumor cell MIA PaCa-2 were loaded on a 4-12% Bis-Tris gel. The membrane was blotted with 1xPBS + 0.2% Tween-20 + 10% non-fat dry milk. The membrane was incubated with Anti-HMOX1 Antibody (PB9212) at the concentration of 200 ng/ml at room temperature for 3 hours. The membrane was then blotted with HRP-conjugated anti-rabbit secondary antibodies at 4oC overnight. The band was detected using regular ECL with 1 minute exposure. A major band with 32 kD was detected.
Western Blot , Whole cell extract of pancreatic tumor cell MIA PaACa2 , Enhanced chemiluminescence
| ALPL | AQP3 | BDNF | BMP2 |
| BRCA1 | CCR5 | CD68 | COL1A1 |
| CSF3 | CTSB | CTSD | CXCL8 |
| ESM1 | HAVCR1 | IFNG | IGFBP7 |
| IL10 | IL1B | IL6 | LCN2 |
Boster Bio offers over 16,000 antibodies that have been validated for IHC, WB, ELISA, and FC in human, mouse, and rat samples. Rabbit and mouse monoclonal antibodies as well as rabbit polyclonal antibodies are available. Buy a primary antibody and get a secondary antibody for free!
More than 1,000 ELISA kits, both singleplex and multiplex, that have been cited 6,000+ times are available at Boster. We offer our Boster-branded Picokine™ ELISA kits (sandwich ELISA) and EZ-Set™ ELISA kits (DIY antibody pairs) in addition to many multiplex ELISA kits.
Boster provides a wide range of human, mouse, and rat recombinant proteins, which include cytokines, growth factors, chemokines, and many more. Our recombinant proteins have high stability, biological activity, and purity.
Boster offers all the reagents you need for your immunostaining and western blotting experiments. We've got everything from buffers to lysates to kits, including our popular and well-cited BCA, CCK-8, and MTT assay kits.
