Mammalian 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 TGFA, 20 µg

Recombinant Human TGFA (Transforming Growth Factor Alpha), Z101935 by ABM. Expressed in E. coli; 5.8 kDa; &gt;95% purity; tag-free. ED50 0.1–0.4 ng/mL (Balb/3T3). Reconstitute in 10 mM Acetic Acid at 100 µg/mL. For EGFR signaling research.

Organism

Family

Aliases

Gene Symbol

Gene ID

Accession Number

Source

Species

Appearance

Molecular Weight

Endotoxin Level

Purity

Formulation

Function

Reconstitution

Storage

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Quantity

Manufacturer

Shipping Condition

Storage Condition

Recombinant Human THBS1

Recombinant human THBS1 (Z101395) by ABM — 140 kDa, insect cells, &gt;95% purity, tag-free, liquid formulation. Thrombospondin-1 for angiogenesis inhibition and extracellular matrix research.

Recombinant Human THPO

Z101515 by Applied Biological Materials is recombinant human THPO (Thrombopoietin), expressed in HEK293 cells and purified to >95% by SDS-PAGE. This 35 kDa hematopoietic growth factor has an ED50 of 1–2 ng/mL in Mo7e cell proliferation assays. Endotoxin &lt;1.0 EU/µg; reconstitute in sterile PBS with 0.1% endotoxin-free recombinant HSA.

Recombinant Human THPO, 10 µg

Recombinant Human THPO, 1.0 mg

Recombinant Human TNF

Recombinant Human TNF (TNF-alpha) Z100855 by ABM—tag-free, E. coli-expressed, 17.6 kDa, &gt;95% purity, ED50 ≤0.5 ng/mL (cytotoxicity assay). Available from MBP INC.

Recombinant Human TNF, 50 µg

Recombinant Human TNF, 100 µg

Recombinant Human TNF, 1.0 mg

Recombinant Human TNF-alpha, catalog Z101385 by ABM. CHO-expressed, 18 kDa, >95% purity, lyophilized. Bioactive with ED50 ≤0.02 ng/mL and specific activity >5.0×10⁷ units/mg. Endotoxin &lt;1.0 EU/µg.

Recombinant Human TNFRSF10B

Z102245 by Applied Biological Materials is recombinant human TNFRSF10B (DR5/TRAIL-R2), expressed in E. coli with &gt;95% purity by SDS-PAGE and an ED50 of &lt;0.2 ng/mL. This 15 kDa tag-free lyophilized death receptor protein supports TRAIL-mediated apoptosis research, cancer biology, and TRAIL pathway pharmacology studies.

Recombinant Human TNFRSF10B , 50 µg

Recombinant Human TNFRSF10B, 200 µg

Recombinant Human TNFRSF10B, 1.0 mg

Recombinant Human TNFRSF1A

Recombinant human TNFRSF1A (Z102235) by ABM — 18.4 kDa, E. coli, &gt;95% purity, tag-free. Primary TNF-alpha receptor for NF-kB, apoptosis, and inflammation signaling research.

Recombinant Human TNFRSF1A, 20 µg

Recombinant Human TNFRSF1A, 1.0 mg

Recombinant Human TNFRSF1B

Z101745 by Applied Biological Materials is recombinant human TNFRSF1B (TNFR2/p75TNFR), the extracellular domain of TNF Receptor 2, expressed in E. coli with &gt;95% purity by SDS-PAGE and an ED50 of &lt;0.05 ng/mL. This 19 kDa tag-free lyophilized protein supports TNF-alpha signaling research, neuroprotection studies, and regulatory T cell biology.

Recombinant Human TNFRSF1B, 20 µg

Recombinant Human TNFRSF1B, 100 µg

Recombinant Human TNFRSF1B, 1.0 mg

Recombinant Human TNFSF15

Recombinant human TNFSF15 (Z102335) by ABM — E. coli, tag-free, ED50 &lt;0.5 ng/mL in Jurkat cells. TL1/VEGI for T cell activation, DR3 signaling, and IBD research.

Recombinant Human TNFSF15, 50 µg

Recombinant Human TNFSF15, 250 µg

Recombinant Human TNFSF15, 2.0 mg

Recombinant Human TNFSF15, 4.0 mg

Recombinant Human TRAIL (TNFSF10)

Z101755 by Applied Biological Materials is recombinant human TRAIL (TNFSF10), a 19.5 kDa TNF superfamily member expressed in E. coli with >95% purity. TRAIL induces apoptosis in tumor cells via DR4/DR5 death receptors while sparing most normal tissue. Lyophilized from PBS with BSA; reconstitute at 20 µg/mL in sterile PBS with ≥0.1% HSA or BSA. Available from MBP for apoptosis, cancer immunotherapy, and DR4/DR5 signaling research.

Recombinant Human TRAIL (TNFSF10), 10 µg

Recombinant Human TRAIL (TNFSF10), 1.0 mg

Recombinant Human TSLP

Z101095 by Applied Biological Materials is recombinant human TSLP (Thymic Stromal Lymphopoietin), a 15 kDa cytokine expressed in E. coli with >95% purity. TSLP activates dendritic cells and ILC2s to drive Th2 immune responses at epithelial barriers. ED50 &lt;3.0 ng/mL in BaF3/TSLPR-IL-7Rα proliferation assay. Lyophilized from 20 mM PB/150 mM NaCl pH 7.4; reconstitute in distilled water. Available from MBP for allergy, atopic dermatitis, and asthma research.

Recombinant Human TSLP, 10 µg

Recombinant Human TSLP, 100 µg

Recombinant Human TSLP, 1.0 mg

Recombinant Human TWEAK (TNFSF12)

Recombinant Human TWEAK (TNFSF12), Z102275 by ABM. Expressed in E. coli; 17.2 kDa; &gt;95% purity; tag-free. Lyophilized in PBS + BSA. Reconstitute in PBS + ≥0.1% BSA/HSA at 0.1 mg/mL. For Fn14 signaling and apoptosis research.