<h2 data-section-id="pdko8n" data-start="0" data-end="50">What are recombinant proteins for cell culture?</h2>
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Recombinant proteins for cell culture are biologically active growth factors, cytokines, and signaling molecules produced using recombinant DNA technology to control specific cellular functions in vitro. Growth factors such as FGF (fibroblast growth factor), EGF (epidermal growth factor), and TGF-&beta; (transforming growth factor beta) regulate cell growth, proliferation, survival, and differentiation. Cytokines including IL-2, IL-7, IL-15, and IL-21 influence immune cell activation, expansion, and function. These proteins are widely used in serum-free and chemically defined media, stem cell and iPSC culture, immune cell expansion, organoid development, hybridoma production, and cell and gene therapy workflows where precise control over cellular signaling is required.
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<h2 dir="ltr">What you will find:</h2>
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<ul>
<li>Includes cytokines, chemokines, growth factors, and signaling proteins to support proliferation, differentiation, and maintenance of&nbsp;mammalian cells</li>
<li>Rat, human, and mouse recombinant proteins compatible with translational research models and diverse mammalian cell culture&nbsp;</li>
<li>Optimizing cell metabolic activity, signalling pathways, and experimental reproducibility in vitro using recombinant proteins&nbsp;</li>
<li>Suitable for organoid development, expansion of cells, activation of immune cells, neuronal studies, and protein expression workflow optimization.</li>
</ul>
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<h2 data-section-id="4x59d8" data-start="1050" data-end="1118">How to choose recombinant proteins, cytokines, and growth factors</h2>
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Quality grade: RUO vs. preclinical vs. GMP
Research-use-only (RUO) proteins are suitable for most academic and industrial research applications. Preclinical-grade proteins provide enhanced documentation and quality control for studies supporting clinical development. GMP-grade proteins are manufactured under controlled quality systems with complete traceability and lot-to-lot bioactivity verification, making them appropriate for cell therapy, gene therapy, and other regulated applications.
Expression system and post-translational modifications
The production system can significantly affect protein activity. HEK293 and other mammalian expression systems preserve native human post-translational modifications such as glycosylation and phosphorylation, which are often necessary for full biological function. Bacterial expression systems such as E. coli may offer lower cost and higher yields but cannot reproduce many of these modifications.
Carrier-free formulation
Carrier-free recombinant proteins are formulated without stabilizing proteins such as bovine serum albumin (BSA). This eliminates potential experimental interference from carrier proteins and supports serum-free, animal-component-free, and GMP-compatible workflows. Carrier-free formulations are especially important when studying sensitive signaling pathways or developing clinical manufacturing processes.
Endotoxin level and purity
Endotoxins can stimulate inflammatory responses and alter cell behavior, particularly in immune cell cultures. For T-cell expansion, stem cell culture, and other sensitive applications, low-endotoxin or endotoxin-free proteins with documented purity above 95% are preferred to ensure reproducible results.
Stability format: standard vs. thermostable
Standard recombinant proteins gradually lose activity during prolonged incubation at 37&deg;C. Thermostable variants, such as engineered FGF2 formulations, maintain biological activity for longer periods and reduce the need for frequent media supplementation. These products can improve workflow efficiency in stem cell maintenance and differentiation protocols.
Storage and reconstitution
Lyophilized recombinant proteins offer extended shelf life and are typically stored frozen until use. After reconstitution, proteins should be aliquoted into single-use portions whenever possible to minimize repeated freeze-thaw cycles that can reduce activity. Proper storage conditions vary by product and should follow the manufacturer's recommendations.
<h2 data-section-id="rxnuuy" data-start="3659" data-end="3704">&nbsp;</h2>
<h2 data-section-id="1fljvas" data-start="4451" data-end="4476">Specifications context</h2>
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Modern recombinant cytokines and growth factors are available in a wide range of formats including carrier-free, low-endotoxin, animal-component-free, and GMP-grade formulations. Many GMP-grade cytokines such as IL-2, IL-7, IL-15, and IL-21 undergo lot-specific bioactivity testing using validated reference standards to ensure consistent biological performance. Mammalian-cell-expressed proteins are increasingly preferred for applications requiring native structure and maximum biological activity.
As of 2026, carrier-free, low-endotoxin recombinant proteins produced in mammalian expression systems have become the preferred choice for stem cell culture, immune cell expansion, organoid development, and advanced biomanufacturing workflows.
For basal media used alongside recombinant proteins, see Classic Media. For additional supplementation reagents, see Cell Culture Supplements &amp; Additives. Browse Mammalian Cell Culture for the broader category.
<a href="https://mbpinc.net/contact-us">Contact the expert team</a> at MBP today and get optimized recombinant proteins for your lab.

Recombinant Proteins

MSDS

Growth Factor-eFlyer

Growth Factors and Cytokines-Brochure

Growth Factors and Cytokines-FAQ

Role of Growth Factors in Cell Differentiation-Poster

Recombinant Human IGF2BP2

Recombinant Human IGF2BP2 (Z101185) by ABM — 60 kDa, CHO cells, &gt;95% purity. RNA-binding protein (IMP-2/VICKZ2) and m6A reader for cancer biology, epitranscriptomics, and stem cell research.

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Recombinant Human IGFBP3

Z100375 by Applied Biological Materials is E. coli-expressed recombinant human Insulin-like Growth Factor Binding Protein 3 (IGFBP3 / IBP-3 / BP-53), a 28 kDa IGF-family binding protein. Purity &gt;95% by SDS-PAGE; endotoxin &lt;1.0 EU/µg by LAL. Bioactivity confirmed by IGF-I–induced MCF-7 proliferation inhibition (ED50 ≤0.5 µg/mL). Available in 25 µg and 1.0 mg; contact MBP for pricing.

Recombinant Human IGFBP3, 25 µg

Recombinant Human IGFBP3, 4 x 25 µg (Z100375)

Recombinant Human IGFBP3, 1.0 mg

Recombinant Human IGFBP5

Z102015 by Applied Biological Materials — recombinant human IGFBP5 (IBP5), E. coli, 26.5 kDa, tag-free, &gt;95% purity. Sodium citrate pH 3.0 formulation. For IGF bioavailability, bone metabolism, and cancer biology research.

Recombinant Human IGFBP7

Z102035 by Applied Biological Materials (ABM) is a tag-free recombinant human IGFBP-7 (Insulin-like Growth Factor Binding Protein 7) expressed in E. coli, with greater than 95% purity by SDS-PAGE, 26.7 kDa molecular weight, and biological activity confirmed by CCL21 binding ELISA. Supplied as lyophilized powder for IGF signaling, tumor suppression, angiogenesis, and myogenesis research.

Recombinant Human IGFBP7, 25 µg

Recombinant Human IGFBP7, 100 µg

Recombinant Human IGFBP7, 1.0 mg

Recombinant Human IL10

Recombinant Human IL10 (Interleukin-10), Z101495 by ABM. Expressed in E. coli; 19 kDa; &gt;95% purity; tag-free. ED50 ≤2.0 ng/mL (MC/9 co-stimulation). Lyophilized in PBS pH 7.0. For immunosuppression and STAT3 signaling research.

Recombinant Human IL10, 10 µg

Recombinant Human IL10, 1.0 mg

Z100425-Growth Factor eFlyer

Z100425-Growth Factors and Cytokines Brochure

Z100425-Growth Factors and Cytokines FAQ

Z100425-Role of Growth Factors in Cell Differentiation (Poster)

Recombinant Human IL11

Recombinant human IL-11 (Z100425) by ABM — tag-free, E. coli-expressed, &gt;95% pure, lyophilized, ED50 ≤1.0 ng/mL. For hematopoietic and cytokine signaling research.

Recombinant Human IL11, 10 µg

Recombinant Human IL11, 100 µg

Recombinant Human IL11, 1.0 mg

Recombinant Human IL13

Z100445 by Applied Biological Materials is a recombinant human IL-13 expressed in E. coli, supplied lyophilized at &gt;95% purity with an ED50 &lt;1 ng/ml in TF-1 proliferation assays. IL-13 is the key Th2 cytokine in asthma and atopic dermatitis, signaling through IL-13Rα1/IL-4Rα to activate STAT6, and is the reference antigen for dupilumab, lebrikizumab, and tralokinumab neutralization studies.

Recombinant Human IL13, 10 µg

Recombinant Human IL13, 1.0 mg

Z100455-Growth Factor eFlyer

Z100455-Growth Factors and Cytokines Brochure

Z100455-Growth Factors and Cytokines FAQ

Z100455-Role of Growth Factors in Cell Differentiation (Poster)

Recombinant Human IL15

Z100455 by ABM — Recombinant Human IL-15, 13 kDa, tag-free, expressed in E. coli. Purity &gt;95% by SDS-PAGE, endotoxin &lt;1.0 EU/µg, ED50 &lt;0.1 ng/mL. Available in 10 µg and 1.0 mg.

Recombinant Human IL15, 10 µg

Recombinant Human IL15, 1.0 mg

Recombinant Human IL16

Recombinant Human IL16 (Z102415) by ABM — 13.5 kDa E. coli-expressed CD4 ligand and T-cell chemoattractant, >95% pure, ED50 7.5–37.5 ng/mL. Order from MBP INC for fast delivery.

Recombinant Human IL16, 25 µg

Recombinant Human IL16, 100 µg

Recombinant Human IL16, 1.0 mg

Z100465-Growth Factor eFlyer

Z100465-Growth Factors and Cytokines Brochure

Z100465-Growth Factors and Cytokines FAQ

Z100465-Role of Growth Factors in Cell Differentiation (Poster)

Recombinant Human IL17A

Z100465 by ABM — Recombinant Human IL-17A, 16 kDa monomer / 32 kDa homodimer, tag-free, E. coli. Purity &gt;95% by SDS-PAGE, endotoxin &lt;1.0 EU/µg, ED50 ~2.0 ng/mL. Available in 25 µg, 100 µg, and 500 µg.

Recombinant Human IL17A, 25 µg

Recombinant Human IL17A, 100 µg

Recombinant Human IL17A, 500 µg

Recombinant Human IL17D

Recombinant Human IL17D (Interleukin-17D), Z102425 by ABM. Expressed in E. coli; 20.5 kDa; &gt;95% purity; tag-free. ED50 &lt;0.2 ng/mL. Reconstitute in 4 mM HCl + ≥0.1% BSA/HSA at 100 µg/mL. For NK cell and immuno-oncology research.

Recombinant Human IL17D, 5 µg

Recombinant Human IL17D, 100 µg

Recombinant Human IL17D, 1.0 mg

Recombinant Human IL17F

Recombinant Human IL17F (Z102435) by ABM — E. coli-expressed disulfide-linked homodimer, 15.2 kDa, ED50 8.0–40.0 ng/mL (NIH-3T3 IL-6 assay). For Th17, mucosal immunity, and inflammatory cytokine research. 25 µg or 1.0 mg.