Increase the sensitivity of your immunoassays with our integrated solutions for polyclonal antibody production. From antigen design to serum purification, our antibody production services were designed for maximum quality and production yield. Generate high-quality polyclonal antibodies using any type of antigen and in any species including rabbit, chicken, mouse, rat, goat, sheep, llama, or alpaca!
Why choose ProteoGenix' polyclonal
antibody production services?
Strong guarantees
All our packages include a high antibody titer guarantee (1/64000 in ELISA). Our anti-protein package even includes WB positive results.
Competitive price
With all-included packages starting from $324, we provide the most competitive price on the market!
Instant online order
Save time and buy polyclonal antibodies directly online thanks to our online form!
Large choice of species
Choose between different species depending on the volume and format of antibodies you require!
One-stop solution
We offer integrated polyclonal antibody production solutions from antigen design to purification and conjugation (if requested).
Express service
Get your polyclonal antibodies in 28 days thanks to our ExpresswayTM protocol.
Our polyclonal antibody production packages
| PACK1 | PACK2 | PACK3 | PACK1XS | PACK2.2 | PACK4 | ||
|---|---|---|---|---|---|---|---|
| Peptide synthesized by ProteoGenix |  | 2 peptides | Modified and non-modified peptides | ||||
| Recombinant Protein produced by ProteoGenix |  | ||||||
| Provided by customer |  |  | |||||
| Immunization of 2 rabbits |  |  |  |  |  |  | |
| Standard (51 days) or Express protocol (28 days)? | Standard | Standard | Standard | ExpresswayTM | Standard | Standard | |
| vs. Protein A or G | |||||||
| vs. Antigen |  |  |  |  | Purification/ depletion | ||
| No purification |  | ||||||
| Guarantee | ELISA titer | ELISA titer | WB + ELISA titer | ELISA titer | ELISA titer | ELISA titer | |
| Timeline | 9-10 weeks | ≈15 weeks | ≈13-15 weeks | 28 days | ≈15 weeks | ≈15 weeks | |
Our polyclonal antibody production process
Antigen design
- Definition of an antigen design strategy for optimized polyclonal antibody production
- Protein design
- Peptide design
1-2 days
Deliverables
Designed sequence for customer’s validation
Antigen production
- Protein production in an expression system of your choice
- Peptide synthesis and conjugation to a carrier (KLH, BSA or OVA) to improve immune response
3-5 weeks for protein
3 weeks for peptide
Deliverables
Antigen sample (protein or peptide)
Animal immunization
- Animal injection with the antigen produced or provided + Freund’s adjuvant
Injection route: subcutaneous, intradermal, intramuscular, intraperitoneal, intravenous
Fast: 28 days
Protein: 51 days
Peptides: 70 days
Deliverables
Pre-immune serum
Antibody testing
- Antibody QC analysis : ELISA, Western Blot or Dot Blot (depending on the guarantees)
1-2 days
Deliverables
Final Immune serum (if no purification)
Serum purification
- Purification against protein A or protein G
- Purification against antigen
- No purification
1 week
Deliverables
-Purified polyclonal antibodies (serum of each animal is purified separately)
-Certificate of analysis (CoA)
What our customers are saying about our polyclonal antibody production service
Prof. XX
Inserm, France
“Lorem ipsum dolor sit amet, consectetur adipiscing elit, sed do eiusmod tempor incididunt ut labore et dolore magna aliqua. Ut enim ad minim veniam, quis nostrud exercitation ullamco laboris nisi ut aliquip ex ea commodo consequat…”
Dr. YY
UP, Portugal
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Our recommendations for polyclonal antibody production
WHAT TO CONSIDER WHEN CHOOSING A HOST FOR POLYCLONAL ANTIBODY PRODUCTION
To select the most suitable species for your polyclonal antibody production, several factors need to be taken into account:
AMOUNT NEEDED
Rabbits are the ideal hosts for polyclonal antibody production – they have a convenient size making them easy to handle. Plus, they produce serum with high titers of target-specific antibodies leading to greater antibody production yields. For larger quantities, goats, sheep, llama, or alpaca should be used.
PHYLOGENETIC DISTANCE
The greater the phylogenetic distance between the source of the antigen and the host species, the stronger the immune response. For instance, when generating polyclonal antibodies against a highly conserved mammalian antigen, chickens could be a good host species.
FINAL APPLICATION
When using polyclonal antibodies in tandem with their monoclonal counterparts, the host species for antibody generation should be phylogenetically distant from each other. For instance, when primary rabbit antibodies are used, secondary/polyclonal antibodies should be generated in species like llama, alpaca, chicken, goat, among others.
BEST REASONS TO CHOOSE A HOST SPECIES FOR POLYCLONAL ANTIBODY GENERATION
Rabbits
Sheep and Goats
Chicken
Llama and Alpaca
Host selection is an important step of every polyclonal antibody production process. Although rabbit hosts are the most conventional choice, there is a growing interest in producing chicken and camelid antibodies.
Polyclonal antibody production in chicken can be quite advantageous when the process needs to be scaled-up because IgY antibodies are extracted from egg yolk instead of serum. It is known that egg yolk is more challenging to purify than serum; however, it can be produced in higher quantities in comparison to mammalian polyclonal production.
In contrast, camelids are increasingly appreciated as polyclonal antibody production hosts. In addition to conventional IgG antibodies, they can produce immunoglobulins devoid of light chains – heavy chain antibodies (HAbs). These molecules have unique properties including:
- Increased stability at extreme pH or temperature
- A low steric hindrance allowing easier access to buried antigens that would not be accessible to conventional antibodies.
- A higher capacity of tissue penetration is a precious asset for immunohistochemistry experiments or even for therapeutic applications.
How to optimize the polyclonal antibody production process
ANTIGEN DESIGN AND PRODUCTION
Achieving high titers of target-specific antibodies depends on the antigen’s capacity for eliciting a strong immune response. For this reason, choosing a suitable antigen for immunization remains one of the most important steps of the polyclonal antibody production process
Several antigens may be used for polyclonal antibody generation including:
- Proteins – proteins are the most conventional antigens for antibody generation. They ensure polyclonal antibodies recognize different relevant epitopes naturally exposed in the native conformation of the protein.
- Peptides – using peptides for immunization is useful when developing antibodies for linear epitopes (important in Western Blot applications) or when developing antibodies against a specific epitope (increases assay specificity). Since most peptides aren’t immunogenic, adjuvants are typically used to enhance the immune response.
- DNA – genetic immunization is reserved for special cases. For instance, when the target protein is hard to produce, unstable or contains complex transmembrane domains, genetic immunization may be a suitable alternative.
Other antigens may be used for immunization such as small molecules or even whole cells (native or recombinant); however, these projects require the development and testing of custom immunization solutions.
ANIMAL IMMUNIZATION
Our standard immunization protocol starts at:
- 51 days for anti-protein polyclonal antibody production
- 70 days for anti-peptide polyclonal antibody production
Both protocols can be extended if guaranteed antibody titers are not reached. Typically, it is better to immunize animals with a lower quantity of antigen and for longer periods, rather than using higher quantities of antigen and shorter immunization times.
Pressed for time in your polyclonal antibody production project?
Our exclusive protocol – ExpresswayTM – was designed to generate high-quality polyclonal antibodies in only 28 days.
This is made possible thanks to our special adjuvant aimed at enhancing the immune response.
POLYCLONAL ANTIBODY PURIFICATION
Polyclonal antibodies are typically harvested by bleeding the hosts after desired antibody titers are reached. The cellular fraction and the antibody-enriched serum can be separated by centrifugation resulting in a crude polyclonal antibody solution.
Crude preparations are useful for many applications. However, for enhanced sensitivity and reduced off-target binding, these preparations should be purified. Polyclonal antibody purification can be carried out by:
- Protein A or G purification – these proteins are produced by Staphylococcus aureus and Streptococcus spp., respectively, and they can bind the Fc fragment of antibodies with high affinity. Protein A/G purification allows the straightforward separation of immunoglobulins from all other serum components. However, unspecific antibodies with a low affinity towards the target are not eliminated with this type of purification.
- Antigen-specific purification – using affinity chromatography to recover polyclonal antibodies with high affinity towards a specific antigen is a widely used process of polyclonal antibody purification. It ensures only the antibodies with the highest affinity are recovered, reducing off-target binding and, consequently, reducing background noise in immunoassays.
For more answers to the most frequently asked questions about polyclonal antibodies, consult our dedicated page.
Need advice for your custom polyclonal antibody production? Please feel free to contact your dedicated account manager!
Polyclonal antibody production:
featured publications
- Stapane, L. et al. Avian eggshell formation reveals a new paradigm for vertebrate mineralization via vesicular amorphous calcium carbonate. J Biol Chem. 2020 Nov; 295(47):15853-15869. doi: 10.1074/jbc.RA120.014542
- Liebers, M. et al. Nucleo‐plastidic PAP 8/pTAC 6 couples chloroplast formation with photomorphogenesis. EMBO J. 2020 Nov; 39(22):e104941. doi: 10.15252/embj.2020104941
- Jaouannet, M. et al. Atypical Membrane-Anchored Cytokine MIF in a Marine Dinoflagellate. Microorganisms. 2020 Aug; 8(9):1263. doi: 10.3390/microorganisms8091263
- Ślęzak, P. et al. Porphyromonas gingivalis HmuY and Streptococcus gordonii GAPDH-Novel Heme Acquisition Strategy in the Oral Microbiome. Int J Mol Sci. 2020 Jun; 21(11):4150. doi: 10.3390/ijms21114150
- Dziuba, M. V. et al. Single-step transfer of biosynthetic operons endows a non-magnetotactic Magnetospirillum strain from wetland with magnetosome biosynthesis. Environ Microbiol. 2020 Apr; 22(4):1603-1618. doi: 10.1111/1462-2920.14950
- Raman, S. C. et al. The Envelope-Based Fusion Antigen GP120C14K Forming Hexamer-Like Structures Triggers T Cell and Neutralizing Antibody Responses Against HIV-1. Front Immunol. 2019 Dec; 10:2793. doi: 10.3389/fimmu.2019.02793
- Stapane, L. et al. The glycoproteins EDIL3 and MFGE8 regulate vesicle-mediated eggshell calcification in a new model for avian biomineralization. J Biol Chem. 2019 Oct;294(40):14526-14545. doi: 10.1074/jbc.RA119.009799
- Perrier, A. et al. The C-terminal domain of the MERS coronavirus M protein contains a trans-Golgi network localization signal. J Biol Chem. 2019 Sep; 294(39):14406-14421. doi: 10.1074/jbc.RA119.008964
- Cheval, L. et al. ANP-stimulated Na+ secretion in the collecting duct prevents Na+ retention in the renal adaptation to acid load. Am J Physiol Renal Physiol. 2019 Aug;317(2):F435-F443. doi: 10.1152/ajprenal.00059.2019
- Martenot, C. et al. Exploring First Interactions Between Ostreid Herpesvirus 1 (OsHV-1) and Its Host, Crassostrea gigas: Effects of Specific Antiviral Antibodies and Dextran Sulfate. Front Microbiol. 2019 May; 10:1128. doi: 10.3389/fmicb.2019.01128
- Liang, Y. et al. Branched-Chain Amino Acid Catabolism Impacts Triacylglycerol Homeostasis in Chlamydomonas reinhardtii. Plant Physiol. 2019 Apr; 179(4): 1502–1514. doi: 10.1104/pp.18.01584
- Marsolier, J. et al. Secreted parasite Pin1 isomerase stabilizes host PKM2 to reprogram host cell metabolism. Commun. Biol. 2019 Apr; 2:152. doi: 10.1038/s42003-019-0386-6
- Kenno, S. et al. Candida albicans Factor H Binding Molecule Hgt1p – A Low Glucose-Induced Transmembrane Protein Is Trafficked to the Cell Wall and Impairs Phagocytosis and Killing by Human Neutrophils. Front Microbiol. 2019 Jan; 9:3319. doi: 10.3389/fmicb.2018.03319
- Signes, A. et al. APOPT1/COA8 assists COX assembly and is oppositely regulated by UPS and ROS. EMBO Mol Med. 2019 Jan; 11(1): e9582. doi: 10.15252/emmm.201809582
- Werth, E. G. et al. Investigating the effect of target of rapamycin kinase inhibition on the Chlamydomonas reinhardtii phosphoproteome: from known homologs to new targets. New Phytol. 2019 Jan; 221(1):247-260. doi: 10.1111/nph.15339
- Gassias, E. et al. The insect HR38 nuclear receptor, a member of the NR4A subfamily, is a synchronizer of reproductive activity in a moth. FEBS J. 2018 Nov; 285(21):4019-4040. doi: 10.1111/febs.14648
- Grandi, A. et al. Vaccination With a FAT1-Derived B Cell Epitope Combined With Tumor-Specific B and T Cell Epitopes Elicits Additive Protection in Cancer Mouse Models. Front Oncol. 2018 Oct; 8: 481. doi: 10.3389/fonc.2018.00481
- Moscatiello, R. et al. The Hydrophobin HYTLO1 Secreted by the Biocontrol Fungus Trichoderma longibrachiatum Triggers a NAADP-Mediated Calcium Signalling Pathway in Lotus japonicas. Int J Mol Sci. 2018 Sep; 19(9):2596. doi: 10.3390/ijms19092596
- Kong, F. et al. Interorganelle Communication: Peroxisomal MALATE DEHYDROGENASE2 Connects Lipid Catabolism to Photosynthesis through Redox Coupling in Chlamydomonas. Plant Cell. 2018 Aug; 30(8):1824-1847. doi: 10.1105/tpc.18.00361
- Bastet, A. et al. Trans-species synthetic gene design allows resistance pyramiding and broad-spectrum engineering of virus resistance in plants. Plant Biotechnol J. 2018 Mar 5;16(9):1569-1581. doi: 10.1111/pbi.12896
- De Sousa, N. et al. Hippo signaling controls cell cycle and restricts cell plasticity in planarians. PLoS Biol. 2018 Jan; 16(1):e2002399. doi: 10.1371/journal.pbio.2002399
- Tirado-Duarte, D. et al. The Akt-like kinase of Leishmania panamensis: As a new molecular target for drug discovery. Acta Trop. 2018 Jan; 177:171-178. doi: 10.1016/j.actatropica.2017.10.008
- Barca, A. et al. Molecular and expression analysis of the Allograft inflammatory factor 1 (AIF-1) in the coelomocytes of the common sea urchin Paracentrotus lividus. Fish Shellfish Immunol. 2017 Dec; 71:136-143. doi: 10.1016/j.fsi.2017.09.078
- Paiola, M. et al. Oestrogen receptor distribution related to functional thymus anatomy of the European sea bass, Dicentrarchus labrax. Dev Comp Immunol. 2017 Dec; 77:106-120. doi: 10.1016/j.dci.2017.07.023
- Langer, N. et al. Determination of cross-reactivity of poly- and monoclonal antibodies for synthetic cannabinoids by direct SPR and ELISA. Forensic Sci Int. 2017 Nov; 280:25-34. doi: 10.1016/j.forsciint.2017.09.011
- Pulze, L. et al. A new cellular type in invertebrates: first evidence of telocytes in leech Hirudo medicinalis. Sci Rep. 2017 Oct; 7(1):13580. doi: 10.1038/s41598-017-13202-9
- Seo, W. et al. Investigation of rabies virus glycoprotein carboxyl terminus as an in vitro predictive tool of neurovirulence. A 3R approach. Microbes Infect. 2017 Sep-Oct; 19(9-10):476-484. doi: 10.1016/j.micinf.2017.05.006
- El Kfoury, K. A. et al. Bifidobacteria-derived lipoproteins inhibit infection with coxsackievirus B4 in vitro. Int J Antimicrob Agents. 2017 Aug; 50(2):177-185. doi: 10.1016/j.ijantimicag.2017.03.010
- Chaux, F. et al. Flavodiiron Proteins Promote Fast and Transient O2 Photoreduction in Chlamydomonas. Plant Physiol. 2017 Jul; 174(3):1825-1836. doi: 10.1104/pp.17.00421
- Martenot, C. et al. Haemocytes collected from experimentally infected Pacific oysters, Crassostrea gigas: Detection of ostreid herpesvirus 1 DNA, RNA, and proteins in relation with inhibition of apoptosis. PLoS One. 2017 May; 12(5):e0177448. doi: 10.1371/journal.pone.0177448
- Dubois, E. et al. Multimerization properties of PiggyMac, a domesticated piggyBac transposase involved in programmed genome rearrangements. Nucleic Acids Res. 2017 Apr; 45(6):3204-3216. doi: 10.1093/nar/gkw1359
- 2020
- 2019
- 2018
- 2017
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Stapane, L. et al. Avian eggshell formation reveals a new paradigm for vertebrate mineralization via vesicular amorphous calcium carbonate. J Biol Chem. 2020 Nov; 295(47):15853-15869. doi: 10.1074/jbc.RA120.014542
-
Liebers, M. et al. Nucleo‐plastidic PAP 8/pTAC 6 couples chloroplast formation with photomorphogenesis. EMBO J. 2020 Nov; 39(22):e104941. doi: 10.15252/embj.2020104941
-
Jaouannet, M. et al. Atypical Membrane-Anchored Cytokine MIF in a Marine Dinoflagellate. Microorganisms. 2020 Aug; 8(9):1263. doi: 10.3390/microorganisms8091263
-
Ślęzak, P. et al. Porphyromonas gingivalis HmuY and Streptococcus gordonii GAPDH-Novel Heme Acquisition Strategy in the Oral Microbiome. Int J Mol Sci. 2020 Jun; 21(11):4150. doi: 10.3390/ijms21114150
-
Dziuba, M. V. et al. Single-step transfer of biosynthetic operons endows a non-magnetotactic Magnetospirillum strain from wetland with magnetosome biosynthesis. Environ Microbiol. 2020 Apr; 22(4):1603-1618. doi: 10.1111/1462-2920.14950
- Raman, S. C. et al. The Envelope-Based Fusion Antigen GP120C14K Forming Hexamer-Like Structures Triggers T Cell and Neutralizing Antibody Responses Against HIV-1. Front Immunol. 2019 Dec; 10:2793. doi: 10.3389/fimmu.2019.02793
- Stapane, L. et al. The glycoproteins EDIL3 and MFGE8 regulate vesicle-mediated eggshell calcification in a new model for avian biomineralization. J Biol Chem. 2019 Oct;294(40):14526-14545. doi: 10.1074/jbc.RA119.009799
- Perrier, A. et al. The C-terminal domain of the MERS coronavirus M protein contains a trans-Golgi network localization signal. J Biol Chem. 2019 Sep; 294(39):14406-14421. doi: 10.1074/jbc.RA119.008964
- Cheval, L. et al. ANP-stimulated Na+ secretion in the collecting duct prevents Na+ retention in the renal adaptation to acid load. Am J Physiol Renal Physiol. 2019 Aug;317(2):F435-F443. doi: 10.1152/ajprenal.00059.2019
- Martenot, C. et al. Exploring First Interactions Between Ostreid Herpesvirus 1 (OsHV-1) and Its Host, Crassostrea gigas: Effects of Specific Antiviral Antibodies and Dextran Sulfate. Front Microbiol. 2019 May; 10:1128. doi: 10.3389/fmicb.2019.01128
- Liang, Y. et al. Branched-Chain Amino Acid Catabolism Impacts Triacylglycerol Homeostasis in Chlamydomonas reinhardtii. Plant Physiol. 2019 Apr; 179(4): 1502–1514. doi: 10.1104/pp.18.01584
- Marsolier, J. et al. Secreted parasite Pin1 isomerase stabilizes host PKM2 to reprogram host cell metabolism. Commun. Biol. 2019 Apr; 2:152. doi: 10.1038/s42003-019-0386-6
- Kenno, S. et al. Candida albicans Factor H Binding Molecule Hgt1p - A Low Glucose-Induced Transmembrane Protein Is Trafficked to the Cell Wall and Impairs Phagocytosis and Killing by Human Neutrophils. Front Microbiol. 2019 Jan; 9:3319. doi: 10.3389/fmicb.2018.03319
- Signes, A. et al. APOPT1/COA8 assists COX assembly and is oppositely regulated by UPS and ROS. EMBO Mol Med. 2019 Jan; 11(1): e9582. doi: 10.15252/emmm.201809582
- Werth, E. G. et al. Investigating the effect of target of rapamycin kinase inhibition on the Chlamydomonas reinhardtii phosphoproteome: from known homologs to new targets. New Phytol. 2019 Jan; 221(1):247-260. doi: 10.1111/nph.15339
- Gassias, E. et al. The insect HR38 nuclear receptor, a member of the NR4A subfamily, is a synchronizer of reproductive activity in a moth. FEBS J. 2018 Nov; 285(21):4019-4040. doi: 10.1111/febs.14648
- Grandi, A. et al. Vaccination With a FAT1-Derived B Cell Epitope Combined With Tumor-Specific B and T Cell Epitopes Elicits Additive Protection in Cancer Mouse Models. Front Oncol. 2018 Oct; 8: 481. doi: 10.3389/fonc.2018.00481
- Moscatiello, R. et al. The Hydrophobin HYTLO1 Secreted by the Biocontrol Fungus Trichoderma longibrachiatum Triggers a NAADP-Mediated Calcium Signalling Pathway in Lotus japonicas. Int J Mol Sci. 2018 Sep; 19(9):2596. doi: 10.3390/ijms19092596
- Kong, F. et al. Interorganelle Communication: Peroxisomal MALATE DEHYDROGENASE2 Connects Lipid Catabolism to Photosynthesis through Redox Coupling in Chlamydomonas. Plant Cell. 2018 Aug; 30(8):1824-1847. doi: 10.1105/tpc.18.00361
- Bastet, A. et al. Trans-species synthetic gene design allows resistance pyramiding and broad-spectrum engineering of virus resistance in plants. Plant Biotechnol J. 2018 Mar 5;16(9):1569-1581. doi: 10.1111/pbi.12896
- De Sousa, N. et al. Hippo signaling controls cell cycle and restricts cell plasticity in planarians. PLoS Biol. 2018 Jan; 16(1):e2002399. doi: 10.1371/journal.pbio.2002399
- Tirado-Duarte, D. et al. The Akt-like kinase of Leishmania panamensis: As a new molecular target for drug discovery. Acta Trop. 2018 Jan; 177:171-178. doi: 10.1016/j.actatropica.2017.10.008
- Barca, A. et al. Molecular and expression analysis of the Allograft inflammatory factor 1 (AIF-1) in the coelomocytes of the common sea urchin Paracentrotus lividus. Fish Shellfish Immunol. 2017 Dec; 71:136-143. doi: 10.1016/j.fsi.2017.09.078
- Paiola, M. et al. Oestrogen receptor distribution related to functional thymus anatomy of the European sea bass, Dicentrarchus labrax. Dev Comp Immunol. 2017 Dec; 77:106-120. doi: 10.1016/j.dci.2017.07.023
- Langer, N. et al. Determination of cross-reactivity of poly- and monoclonal antibodies for synthetic cannabinoids by direct SPR and ELISA. Forensic Sci Int. 2017 Nov; 280:25-34. doi: 10.1016/j.forsciint.2017.09.011
- Pulze, L. et al. A new cellular type in invertebrates: first evidence of telocytes in leech Hirudo medicinalis. Sci Rep. 2017 Oct; 7(1):13580. doi: 10.1038/s41598-017-13202-9
- Seo, W. et al. Investigation of rabies virus glycoprotein carboxyl terminus as an in vitro predictive tool of neurovirulence. A 3R approach. Microbes Infect. 2017 Sep-Oct; 19(9-10):476-484. doi: 10.1016/j.micinf.2017.05.006
- El Kfoury, K. A. et al. Bifidobacteria-derived lipoproteins inhibit infection with coxsackievirus B4 in vitro. Int J Antimicrob Agents. 2017 Aug; 50(2):177-185. doi: 10.1016/j.ijantimicag.2017.03.010
- Chaux, F. et al. Flavodiiron Proteins Promote Fast and Transient O2 Photoreduction in Chlamydomonas. Plant Physiol. 2017 Jul; 174(3):1825-1836. doi: 10.1104/pp.17.00421
- Martenot, C. et al. Haemocytes collected from experimentally infected Pacific oysters, Crassostrea gigas: Detection of ostreid herpesvirus 1 DNA, RNA, and proteins in relation with inhibition of apoptosis. PLoS One. 2017 May; 12(5):e0177448. doi: 10.1371/journal.pone.0177448
- Dubois, E. et al. Multimerization properties of PiggyMac, a domesticated piggyBac transposase involved in programmed genome rearrangements. Nucleic Acids Res. 2017 Apr; 45(6):3204-3216. doi: 10.1093/nar/gkw1359