Recombinant Proteins

Boster Bio Recombinant Protein

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.

Browse all recombinant proteins

Browse all recombinant proteins

Product
Figures
Species
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Price

1 images

$617
Cat # PROTP00750
20 ug

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$1078
Cat # PROTQ96DG6
20 ug

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$1078
Cat # PROTQ16790
50 ug

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$1078
Cat # PROTQ68D85
50 ug

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$1078
Cat # PROTP20823
20 ug

1 images

$1078
Cat # PROTP43351
20 ug

1 images

$1078
Cat # PROTQ7Z333
20 ug

1 images

$1078
Cat # PROTQ9HC57
20 ug

1 images

$1078
Cat # PROTO75473
20 ug

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Recombinant proteins for your research

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.

What Is A Recombinant Protein?

A brief history of recombinant technology and core concepts.

Recombinant technology Concept overview

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.

History of recombinant protein technology

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.

What does a restriction enzyme do?

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.).

Expression systems

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.

Expression Vectors

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 to Recombinant 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.

Purification of Recombinant Proteins

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.

Ion-exchange chromatography

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.

Affinity 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.

Gel filtration

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.

Affinity Tags and Fusion Proteins

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.

Application of Recombinant Proteins

Genomic
studies

Library creation

Structural and
Functional

Molecular weight, structure etc.

Agricultural
modifications

pest or drought resistance

Viral
identification

HIV, hepatitis

Genetic
disorders

e.g. cystic fibrosis

Protein-based
Therapeutics

Vaccines, Medications such as Insulin

Boster Popular recombinant proteins list

These are the top 160 most popular recombinant proteins. Check out the full list here: browse all recombinant proteins

A2M (PROTP01023) DCN (PROTP07585-1) HPRT1 (PROTP00492-1) POMC (PROTP01189-1)
ABO (PROTP16442) DDT (PROTP30046) HSPA5 (PROTP11021) PON1 (PROTP27169)
ackA (PROTP0A6A3) DEFB103ADEFB103B (PROTP81534) IFNA2 (PROTP01563-2) PPP2R1A (PROTP30153)
ADA (PROTP00813) DERP1 (PROTP08176) IFNB1 (PROTP01574-1) PROK (PROTP06873)
AFP (PROTP02771) DNASE1 (PROTP24855) IFNG (PROTP01579-1) PRTN3 (PROTP24158)
AGT (PROTP01019) DPP4 (PROTP27487-1) IGF1 (PROTP01343-1) PSMA3 (PROTP25788)
ALB (PROTP02769) dps (PROTP43313) IGFBP6 (PROTP24592-1) PTMA (PROTP06454)
ALBGIG20 (PROTP02768-1) EEF1A1 (PROTP68104) IL12RB1 (PROTP42701) PTX3 (PROTP26022-1)
Aldoc (PROTP05063) EEF2 (PROTP13639) IL1A (PROTP01583) RBM3 (PROTP98179)
AMH (PROTP03971) EFNB2 (PROTP52799) Il1b (PROTP10749-1) S100a10 (PROTP08207)
ampC (PROTP00811) EGF (PROTP01133) Il2 (PROTP04351) S100a8 (PROTP27005)
ANXA5 (PROTP08758) EGFR (PROTP00533-2) IL3 (PROTP22629) SELP (PROTP16109)
APOC1 (PROTP02654) ENO1 (PROTP06733) IL6 (PROTP05231-1) SERPINE1 (PROTP05121-1)
APOE (PROTP02649) EPO (PROTP01588-1) INS (PROTP01308) SHBG (PROTP04278)
APP (PROTP05067) EPOR (PROTP19235) KRAS (PROTP01116-1) SLPI (PROTP03973)
ASGR2 (PROTP07307) ERBB2 (PROTP04626-2) LDHA (PROTP00338) SNCA (PROTP37840-8)
ASS1 (PROTP00966) F8 (PROTP00451) LHB (PROTP01232) SOD1 (PROTP00441)
AVD (PROTP02701) FCER1A (PROTP12319-1) LIF (PROTP15018-2) spa (PROTP38507-2)
B2M (PROTP61769-3) FGF1 (PROTP05230) LMNA (PROTP02545) SPINK1 (PROTP00995)
BDNF (PROTP23560-2) FGF2 (PROTP09038-1) LOX (PROTP28300) SPR (PROTP35270)
BMP2 (PROTP12643-1) Fkbp1a (PROTP26883) LPL (PROTP06858) SPRR1B (PROTP22528)
BMP7 (PROTP18075) FSHB (PROTP01228) LRG1 (PROTP02750) SSB (PROTP05455)
BRAF (PROTP15056) FST (PROTP19883-2) lss (PROTP10547) ST6GAL1 (PROTP15907)
C5 (PROTP01031) FTH1 (PROTP02794) malE (PROTP0AEX9-1) TCF4 (PROTP15884-1)
C9 (PROTP02748) FURIN (PROTP09958) MAOA (PROTP21397) TF (PROTP02787)
CCL18 (PROTP55774-1) GALT (PROTP07902) MB (PROTP02144-2) TFRC (PROTP02786)
CCL5 (PROTP13501) GBA (PROTP04062) MBL2 (PROTP11226) Tgfb1 (PROTP04202)
CD38 (PROTP28907) GCG (PROTP01275-2) MBP (PROTP02686) TGFB3 (PROTP10600-5)
CDA (PROTP32320) Gdf7 (PROTP43029) MIF (PROTP14174-3) TMPRSS15 (PROTP98073)
Cdh5 (PROTP55284) GFP (PROTP42212) MMP9 (PROTP14780) TNF (PROTP01375-3)
CEACAM5 (PROTP06731) GH1 (PROTP46407) MPO (PROTP05164) TOP1 (PROTP11387)
CFB (PROTP00751) GHR (PROTP10912-1) MX1 (PROTP20591) TYRP1 (PROTP17643)
CFD (PROTP00746) GNAI1 (PROTP63096) NCL (PROTP19338) USF1 (PROTP22629-1)
CKM (PROTP06732) GNRH1 (PROTP01148-1) NGF (PROTP01138-2) VAMP2 (PROTP63027-1)
CLU (PROTP10909-1) GPC3 (PROTP51654) PDGFB (PROTP01127-3) VCAM1 (PROTP19320)
COL3A1 (PROTP02461) GRN (PROTP28799) PDIA3 (PROTP30101) VEGFA (PROTP15692-6)
CRHBP (PROTP24387) H3F3AH3F3B (PROTP84243) PGF (PROTP49763) WNT3A (PROTP56704)
CRP (PROTP02741-2) HAPLN1 (PROTP10915) phrB (PROTP00914) YBX1 (PROTP67809)
CXCL8 (PROTP10145) HLA-DRA (PROTP01903) PKM (PROTP14618)
CYP2D6 (PROTP10635) HMGB1 (PROTP09429-1) PLAT (PROTP00750)
CYP2E1 (PROTP05181) HMGB2 (PROTP26624-1) PNMT (PROTP11086)

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Boster antibodies and ELISA kits are cited over 23,000+ 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.

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Primary Antibodies

Primary and Secondary Antibodies

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!

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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.

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Recombinant Proteins

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.

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Reagents

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.