Recombinant Human Transforming Growth Factor-Beta 1 (113 a.a.)

SKU:BHP11002537
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ProSpec-Tany TechnoGene Ltd
ProSpec-Tany TechnoGene Ltd
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Overview
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RUO recombinant Transforming Growth Factor-Beta 1 (113 a.a.) (Human) protein for mechanistic studies and assay development. Supplied as a traceable protein input (E. coli; >95% (SDS-PAGE) purity; sterile-filtered solution; MW 12.9 kDa) for reproducible assay inputs.
Target DPD1
Species Human
Options selector
Catalog no. Size
cyt-679-2UG 2 ug
cyt-679-10UG 10 ug
cyt-679-1MG 1 mg
Available Options

Select the variant that best fits your experiment. Availability and lead time may vary by option.

  • Options: Size (3) — 2 ug, 10 ug, 1 mg
  • Lead time: options listed as “in stock at manufacturer” typically ship in 5–7 business days; other statuses may take longer.
  • Storage: Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
  • Shipping: cold-chain shipment (typically with ice packs).
  • Upon receipt: store at the recommended temperature as soon as possible.
  • Sales terms and conditions: Please review prior to ordering.
Field Specification
Mfr No cyt-679
Alternative Names Transforming growth factor beta-1, TGF-beta-1, CED, DPD1, TGFB, TGF-b 1.
Cellular Localization Secreted/Extracellular
Expression System
  • E. coli
Form Sterile Filtered colorless solution.
Formulation The TGF-b 1 solution contains 10mM Sodium Citrate (pH3.5) and 10% glycerol.
Product Type
  • Proteins & Peptides
  • Cytokines and Growth Factors
  • TGF Superfamily
Protein Length 113
Protein Size 12.9 kDa
Purity Greater than 95.0% as determined by SDS-PAGE.
Source Escherichia Coli.
Species Human
Storage Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles.
Target DPD1

Recombinant Human Transforming Growth Factor-Beta 1 (113 a.a.) is supplied as a recombinant protein for in vitro research use.

Background

Transforming growth factor betas (TGFBetas) mediate many cell-cell interactions that occur during embryonic development. Three TGFBetas have been identified in mammals. TGFBeta1, TGFBeta2 and TGFBeta3 are each synthesized as precursor proteins that are very similar in that each is cleaved to yield a 112 amino acid polypeptide that remains associated with the latent portion of the molecule.

Title: Transforming Growth Factor-Beta 1 (113 a.a.) Human Recombinant: A Key Regulator of Cellular Processes with Therapeutic Potential Abstract: Transforming Growth Factor-Beta 1 (TGF-β1) is a multifunctional cytokine that plays a crucial role in various cellular processes, including cell growth, differentiation, and immune modulation. The development of TGF-β1 human recombinant proteins has provided valuable tools for studying its biological functions and therapeutic applications. This research paper explores the production process, characteristics, and potential therapeutic uses of TGF-β1 human recombinant, highlighting its importance and clinical significance. Introduction: TGF-β1 is a pivotal cytokine involved in numerous physiological and pathological processes, such as embryonic development, tissue repair, and immune regulation. Harnessing the therapeutic potential of TGF-β1 has been facilitated by the development of TGF-β1 human recombinant proteins using recombinant DNA technology. These recombinant proteins have become valuable tools for investigating the biological functions of TGF-β1 and exploring its therapeutic applications. Production Process and Characteristics: TGF-β1 human recombinant proteins are produced using recombinant DNA technology, allowing for the expression of the TGF-β1 gene in different host systems. The resulting recombinant proteins possess similar structural and functional characteristics to native TGF-β1. They exhibit the ability to bind to the TGF-β receptor, initiate intracellular signaling pathways, and modulate various cellular responses. Therapeutic Applications: TGF-β1 human recombinant proteins have shown promise in a wide range of therapeutic applications. They have been investigated for their potential in tissue regeneration and wound healing, as TGF-β1 plays a crucial role in promoting cell proliferation and extracellular matrix production. Additionally, TGF-β1 has been studied in the context of fibrotic diseases, such as pulmonary fibrosis and liver fibrosis, where it is implicated in the fibrotic cascade. Furthermore, TGF-β1 has been explored as a potential target for antitumor therapies due to its involvement in tumor progression and immune evasion. Advantages and Challenges: The use of TGF-β1 human recombinant proteins offers several advantages, including the ability to study and manipulate its biological functions in a controlled manner. Recombinant proteins also provide a consistent and reproducible source of TGF-β1, overcoming the challenges associated with sourcing native TGF-β1 from biological samples. However, challenges remain in optimizing production processes, ensuring correct protein folding, and maintaining protein stability. Conclusion: TGF-β1 human recombinant proteins have emerged as valuable tools for studying the biological functions of TGF-β1 and exploring its therapeutic applications. The production of TGF-β1 recombinant proteins using recombinant DNA technology allows for the investigation of its diverse roles in cellular processes. The therapeutic potential of TGF-β1 human recombinant proteins extends to tissue regeneration, fibrotic diseases, and cancer research. Continued research and development efforts are essential to further optimize production processes, address challenges, and fully exploit the clinical benefits of TGF-β1 human recombinant proteins.

Product format

Provided as a recombinant protein suitable for in vitro workflows such as binding studies, screening, and assay development. Refer to the specifications table for expression format and molecular properties.

What is the purity of Recombinant Human Transforming Growth Factor-Beta 1 (113 a.a.) (Human)?
Greater than 95.0% as determined by SDS-PAGE. BioHippo includes a Certificate of Analysis (CoA) confirming purity per lot with every order.
What buffer / formulation is this protein supplied in?
Supplied as: The TGF-b 1 solution contains 10mM Sodium Citrate (pH3.5) and 10% glycerol. Reconstitute lyophilized material in sterile ultrapure water or the recommended buffer per the datasheet prior to use.
How should Recombinant Human Transforming Growth Factor-Beta 1 (113 a.a.) (Human) be stored?
Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid multiple freeze-thaw cycles. Prepare single-use aliquots after reconstitution to avoid repeated freeze–thaw cycles.
What expression system was used to produce this protein?
This recombinant protein was expressed in E. coli. The system was selected to achieve high yield, correct folding, and appropriate post-translational modifications.
Is this protein approved for clinical or in vitro diagnostic use?
No. Supplied for Research Use Only (RUO) — not intended for therapeutic applications or in vitro diagnostic procedures.
Can I request a custom size, tag variant, or formulation?
Yes. BioHippo can accommodate custom requests including alternative sizes, His/GST/Fc tag variants, bulk quantities, and custom formulations. See the Customization & Add-ons tab or email support@biohippo.com.

Can’t Find What You’re Looking For? We can help you source the best match or customize a recombinant protein solution for your study. Options may include species (human/mouse/rat), protein region/domain (full-length vs fragment), tag or label (His/GST/FLAG/biotin/fluorescent), expression system (E. coli/HEK293/insect), purity grade, formulation (buffer, carrier-free, glycerol-free), activity/functional validation (binding or enzymatic assays), endotoxin level (low-endotoxin for cell-based work), mutants/variants (point mutations, isoforms), and bulk or custom packaging. Click Talk to a Scientist to submit a request form, email us at support@biohippo.com, or explore our Research Services for additional support. Our team will be in contact with you shortly.

Bibliography: Derynck R, Jarrett JA, Chen EY, et al. Human transforming growth factor-beta complementary DNA sequence and expression in normal and transformed cells. Nature. 1985;316(6030):701-705. Massagué J. TGF-beta signal transduction. Annu Rev Biochem. 1998;67:753-791. Blobe GC, Schiemann WP, Lodish HF. Role of transforming growth factor beta in human disease. N Engl J Med. 2000;342(18):1350-1358. Akhurst RJ, Hata A. Targeting the TGFβ signaling pathway in disease. Nat Rev Drug Discov. 2012;11(10):790-811. Prud'homme GJ. Pathobiology of transforming growth factor beta in cancer, fibrosis, and immunologic disease, and therapeutic considerations. Lab Invest. 2007;87(11):1077-1091.
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