TGFB3 (24-412 a.a.) Human

Transforming Growth Factor-Beta 3 (24-412 a.a.) Human Recombinant
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Description

Molecular Structure and Isoforms

TGFB3 (24-412 a.a.) corresponds to the proprotein region after cleavage of the 20 a.a. signal peptide. It includes:

  • Latency-associated peptide (LAP): 24-220 a.a., regulates TGFB3 activation .

  • Mature TGFB3: 301-412 a.a., the bioactive domain responsible for receptor binding .

Biological Functions

TGFB3 regulates:

  • Embryogenesis: Critical for palatogenesis, pulmonary development, and cardiac morphogenesis .

  • Wound healing: Accelerates repair by modulating cell adhesion and extracellular matrix synthesis .

  • Immune regulation: Inhibits IL-4-dependent T-cell proliferation (ED50: 40 ng/ml) .

Table 2: Functional Activity Data

Assay ModelActivityEC50/ED50Source
Mink lung epithelial cellsInhibition of proliferation40 ng/ml
HT-2 T cellsNeutralization of IL-4-induced proliferation<1 ng/ml
TGFBR2 bindingLinear range: 0.2-2 ng/mL (SPR/BLI)

Recombinant Production

TGFB3 (24-412 a.a.) is produced in multiple systems with varying characteristics:

Table 3: Recombinant Variants

Expression SystemTag/PurityMolecular WeightKey ApplicationsSource
HEK293AVI/Biotin, >95%27.2 kDa (monomer)Receptor binding assays
E. coliHis tag, >95%25.7 kDa (dimer)Cell proliferation assays
Plant (N. benthamiana)His tag, >95%27.2 kDaStructural studies

Clinical and Research Relevance

  • Genetic mutations: Heterozygous TGFB3 mutations (e.g., c.754+2T>C) cause syndromic aortic aneurysms, mitral valve disease, and skeletal abnormalities .

  • Therapeutic potential:

    • Promotes osteoblast proliferation and collagen synthesis .

    • Drives epithelial-mesenchymal transition in cancer and fibrosis .

  • Signaling paradox: Mutations upregulate canonical (Smad2/3) and noncanonical (ERK, JNK) TGF-β pathways, contributing to vascular pathology .

Product Specs

Introduction
Transforming growth factor betas (TGF-betas) are crucial for cell-to-cell communication during embryonic development. Mammals possess three identified TGF-betas: TGF-beta 1, TGF-beta 2, and TGF-beta 3. Each is initially synthesized as a precursor protein. These precursors share a similar structure, undergoing cleavage to produce a 112 amino acid polypeptide. This polypeptide remains linked to the latent segment of the molecule.
Description
Recombinant human TGFB3, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 412 amino acids (specifically, amino acids 24 to 412). It has a molecular weight of 47.2 kDa. This TGFB3 protein is engineered with a 23 amino acid His-tag at its N-terminus and undergoes purification using proprietary chromatographic methods.
Physical Appearance
The product is a sterile, filtered solution that is colorless.
Formulation
The TGFB3 protein solution has a concentration of 0.5 mg/ml and is supplied in a buffer of 20mM Tris-HCl with a pH of 8.0 and 10% glycerol.
Stability
For short-term storage (2-4 weeks), the product should be kept at 4°C. For extended storage, freezing at -20°C is recommended. The addition of a carrier protein (either 0.1% HSA or BSA) is advisable for long-term storage. Repeated freezing and thawing should be avoided.
Purity
The purity of this product is greater than 85.0%, as assessed by SDS-PAGE analysis.
Synonyms
Transforming Growth Factor, Beta 3, Prepro-Transforming Growth Factor Beta-3, TGF-Beta-3, ARVD1, RNHF, Arrhythmogenic Right Ventricular Dysplasia 1, Transforming Growth Factor Beta-3, TGF-Beta3, ARVD, Transforming growth factor beta-3, TGF-beta-3.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSLSTCTTL DFGHIKKKRV EAIRGQILSK LRLTSPPEPT VMTHVPYQVL ALYNSTRELL EEMHGEREEG CTQENTESEY YAKEIHKFDM IQGLAEHNEL AVCPKGITSK VFRFNVSSVE KNRTNLFRAE FRVLRVPNPS SKRNEQRIEL FQILRPDEHI AKQRYIGGKN LPTRGTAEWL SFDVTDTVRE WLLRRESNLG LEISIHCPCH TFQPNGDILE NIHEVMEIKF KGVDNEDDHG RGDLGRLKKQ KDHHNPHLIL MMIPPHRLDN PGQGGQRKKR ALDTNYCFRN LEENCCVRPL YIDFRQDLGW KWVHEPKGYY ANFCSGPCPY LRSADTTHST VLGLYNTLNP EASASPCCVP QDLEPLTILY YVGRTPKVEQ LSNMVVKSCK CS.

Product Science Overview

Structure and Production

The human recombinant TGF-β3 (24-412 a.a.) is produced in E. coli and consists of a single, non-glycosylated polypeptide chain containing 412 amino acids, with a molecular mass of approximately 47.2 kDa . This recombinant protein is fused to a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques .

Biological Functions

TGF-β3 plays a crucial role in various biological processes, including:

  • Cell Differentiation: It regulates the differentiation of various cell types, contributing to tissue development and repair .
  • Embryogenesis: TGF-β3 is essential for proper embryonic development, particularly in the formation of the palate and lungs .
  • Wound Healing: It orchestrates the movements of epidermal and dermal cells during the wound healing process .
  • Extracellular Matrix Formation: TGF-β3 regulates molecules involved in cellular adhesion and extracellular matrix (ECM) formation .
Clinical Significance

Mutations in the TGFB3 gene are associated with several medical conditions, including:

  • Loeys-Dietz Syndrome 5: A connective tissue disorder characterized by aortic aneurysms and dissections .
  • Arrhythmogenic Right Ventricular Dysplasia (ARVD1): A condition affecting the heart’s muscle tissue, leading to arrhythmias .
Research and Applications

Recombinant TGF-β3 is widely used in research to study its role in various cellular processes and its potential therapeutic applications. Despite its promising effects in preclinical studies, human recombinant TGF-β3 (avotermin) failed in Phase III clinical trials for wound healing .

In summary, TGF-β3 is a vital cytokine with significant roles in cell differentiation, embryogenesis, and wound healing. Its recombinant form, produced in E. coli, is a valuable tool for scientific research and potential therapeutic applications.

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