Cell Culture

<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 IL6

Z100555 by Applied Biological Materials is E. coli-expressed recombinant human Interleukin-6 (IL-6 / BSF-2 / IFNB2), a 21 kDa non-glycosylated pleiotropic cytokine supplied as lyophilized powder. Purity &gt;95% by SDS-PAGE; endotoxin &lt;1.0 EU/µg by LAL. Bioactivity confirmed by TF-1 cell proliferation (ED50 0.5–1 ng/mL). Available in 20 µg, 100 µg, and 1.0 mg; contact MBP for pricing.

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Recombinant Human IL6, 20 µg

Recombinant Human IL6, 100 µg

Recombinant Human IL6, 1.0 mg

Recombinant Human IL7

Recombinant Human IL-7 (Interleukin-7), catalog Z100975 by ABM. E. coli-expressed, 17.7 kDa, >95% purity, lyophilized. Bioactive with ED50 &lt;0.5 ng/mL. Essential lymphocyte cytokine. Endotoxin &lt;1.0 EU/µg.

Recombinant Human IL7, 10 µg

Recombinant Human IL7, 100 µg

Recombinant Human IL7, 1.0 mg

Recombinant Human IL8 (72aa)

Recombinant Human IL8 (72aa, CXCL8), Z101605 by ABM. Expressed in E. coli; 8.3 kDa; &gt;95% purity; tag-free. ED50 &lt;0.5 ng/mL (endothelial proliferation). Lyophilized in PBS pH 7.0. For neutrophil chemotaxis and CXCR1/CXCR2 research.

Recombinant Human IL8 (72aa), 25 µg

Recombinant Human IL8 (72aa), 200 µg

Recombinant Human IL8 (72aa), 1.0 mg

Recombinant Human IL8 (77aa)

Recombinant Human IL-8 (77aa) / CXCL8, catalog Z101615 by ABM. E. coli-expressed, 9 kDa, >95% purity, lyophilized. Bioactive with ED50 &lt;0.5 ng/mL. CXC chemokine, CXCR1/2 ligand. Endotoxin &lt;1.0 EU/µg.

Recombinant Human IL8 (77aa), 25 µg

Recombinant Human IL8 (77aa), 1.0 mg

Recombinant Human IL9

Recombinant Human IL9 (Interleukin-9), catalog Z102475 by ABM. E. coli-expressed, 14.4 kDa, >85% purity, lyophilized. Th9-derived cytokine; signals through IL9R/CD129 via JAK1/STAT. Endotoxin &lt;1.0 EU/µg.

Recombinant Human IL9, 10 µg

Recombinant Human IL9, 1.0 mg

Recombinant Human IP-10 (CXCL10)

Z100575 by ABM — Recombinant Human IP-10 (CXCL10), 9 kDa, tag-free, expressed in E. coli. Purity &gt;95% by SDS-PAGE, endotoxin &lt;1.0 EU/µg, T-lymphocyte chemotaxis at 10–50 ng/mL. Available in 25 µg, 100 µg, and 1.0 mg.

Recombinant Human IP-10 (CXCL10), 25 µg

Recombinant Human IP-10 (CXCL10), 100 µg

Recombinant Human IP-10 (CXCL10), 1.0 mg

Recombinant Human Insulin  (INS)

Z101065 by Applied Biological Materials is recombinant human Insulin (INS), a 6.0 kDa peptide hormone expressed in E. coli with >95% purity. Insulin activates the insulin receptor (INSR) and downstream PI3K/Akt and mTOR pathways; widely used in cell culture supplementation, differentiation protocols, and diabetes research. Lyophilized without additives; requires reconstitution in acidic solution (pH 2–3). Available from MBP.

Recombinant Human KGF (FGF7)

Z100595 by Applied Biological Materials is a recombinant human KGF (FGF7) expressed in E. coli, supplied lyophilized at &gt;97% purity with endotoxin &lt;0.1 EU/µg and ED50 &lt;10 ng/ml in FGFR2b proliferation assays. KGF selectively activates FGFR2b on epithelial cells, driving keratinocyte proliferation, organoid growth, iPSC pancreatic beta cell differentiation, and lung epithelial repair.

Recombinant Human KGF (FGF7), 10 µg

Recombinant Human KGF (FGF7), 100 µg

Recombinant Human KGF (FGF7), 1.0 mg

Flyer

Brochure

Recombinant Human LEC  (CCL16)

Z100325 by ABM (Applied Biological Materials) is Recombinant Human LEC (CCL16) — 11 kDa, tag-free, E. coli expression, &gt;95% purity by SDS-PAGE, lyophilized from 20 mM PBS/100 mM NaCl pH 7.5, 25 µg/unit. Monocyte chemoattractant at 2.0–40 ng/mL. Research use only.

Recombinant Human LEC  (CCL16), 25 µg

Recombinant Human LEC (CCL16), 1.0 mg

Recombinant Human LIF

Z100605 by Applied Biological Materials is a recombinant human leukemia inhibitory factor (LIF) expressed in E. coli, supplied lyophilized at &gt;95% purity with an ED50 of ~0.01 ng/ml in M1 myeloid differentiation assays. LIF signals through LIFR/gp130 to activate JAK/STAT3, supporting mouse ESC pluripotency, hematopoiesis, neural development, and embryo implantation research.

Recombinant Human LIF, 10 µg

Recombinant Human LIF, 100 µg

Recombinant Human LIF, 1.0 mg

Recombinant Human LTA

Z100865 by ABM — Recombinant Human LTA (TNF-β), 19 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 (L929 cytotoxicity). Available in 20 µg, 100 µg, and 1.0 mg.

Recombinant Human LTA, 20 µg

Recombinant Human LTA, 100 µg

Recombinant Human LTA, 1.0 mg

Recombinant Human Leptin (LEP)

Recombinant Human Leptin (LEP / OB), catalog Z101855 by ABM. E. coli-expressed, 16.4 kDa, >95% purity, lyophilized. Bioactive adipokine, ED50 &lt;0.5 ng/mL. Endotoxin &lt;1.0 EU/µg.