Structural Basis, Transduction Branches, and Research Applications of the TGF-β Signaling Pathway

The TGF-β signaling pathway is an important molecular network that regulates cell fate, tissue homeostasis, and pathological remodeling. This pathway is centered on ligand activation, receptor complex assembly, and Smad-dependent transcriptional regulation, while also intersecting with non-Smad branches such as ERK, JNK, and p38. It is broadly involved in fibrosis, epithelial-mesenchymal transition, immunosuppression, and tumor progression.

 

Keywords: TGF-β; TGFBR1; TGFBR2; Smad3; Smad4; ERK; JNK; p38; EMT; fibrosis

 

1. Ligand and Receptor System

1.1 Ligand Family

In the narrow sense, the TGF-β pathway is mainly mediated by TGF-β1, TGF-β2, and TGF-β3. All three belong to the TGF-β superfamily, but they are not completely identical in tissue distribution, receptor-binding characteristics, or functional context. In most mechanistic studies, TGF-β1 is the most representative isoform, especially in research on fibrosis, immune regulation, and the tumor microenvironment. TGF-β2 and TGF-β3 are more often encountered in development, reproduction, and certain tissue-specific regulatory settings.

 

1.2 Receptor Composition

TGF-β signaling mainly depends on the type II receptor TGFBR2 and the type I receptor TGFBR1. TGF-β first binds to TGFBR2, after which TGFBR2 recruits and activates TGFBR1, forming a receptor complex competent for signal transduction. In many studies, TGFBR1 is also referred to as ALK5 and represents the key kinase node in the canonical TGF-β pathway.

 

1.3 Coreceptors and Auxiliary Regulatory Molecules

In addition to TGFBR1 and TGFBR2, the TGF-β receptor system is also regulated by accessory receptors such as TGF-βRIII. These molecules can influence ligand enrichment, local presentation, and receptor-binding efficiency, thereby altering the intensity of signaling input. In certain cell types, accessory receptors do not directly perform catalytic functions, but they can substantially affect the threshold of pathway output.

 

2. Ligand Activation and Signal Initiation

2.1 Latent Storage Form

TGF-β is not usually secreted directly in a free active form. In most cases, cells release latent TGF-β complexes, which are associated with latency-associated peptide and extracellular matrix components and stored in the local microenvironment. Therefore, activation of the TGF-β pathway depends not only on ligand expression level, but also on whether latent ligand is effectively activated.

 

2.2 Activation Mechanisms

Latent TGF-β can be activated through multiple mechanisms, including integrin-mediated mechanical pulling, proteolytic cleavage, local acidification, oxidative stress, and extracellular matrix remodeling. This feature makes the TGF-β pathway highly relevant to tissue injury, changes in mechanical tension, chronic inflammation, and matrix stiffening. For this reason, even under the same ligand expression background, different tissue microenvironments may display markedly different pathway activity.

 

2.3 Receptor Complex Formation

After activation, TGF-β binds TGFBR2, which then recruits TGFBR1 and activates its intracellular kinase domain. Only after receptor complex formation does the signal truly enter the intracellular transduction stage. For experimental studies, merely measuring total ligand abundance is often insufficient to infer pathway status; activated ligand, receptor expression, and receptor activation readouts are more informative.

 

3. Canonical Smad-Dependent Pathway

3.1 Smad Molecular Framework

The core transducers of the canonical TGF-β pathway are members of the Smad family. Smad2 and Smad3 are receptor-regulated Smads, Smad4 is the common-partner Smad, and Smad6 and Smad7 are inhibitory Smads. After TGFBR1 activation, Smad2 and Smad3 are directly phosphorylated, after which they form complexes with Smad4 and translocate into the nucleus.

 

3.2 Central Role of Smad3

In TGF-β-related fibrosis and EMT research, Smad3 usually has more direct functional significance than Smad2. Smad3 is more tightly linked to the expression of collagen, fibronectin, PAI-1, and multiple mesenchymal-related genes, making it a key intermediary between receptor activation and terminal pathological phenotypes. Therefore, in studies involving matrix deposition, scar formation, and invasive phenotypes, p-Smad3 is usually the preferred core readout.

 

3.3 Nuclear Transcriptional Regulation

After entering the nucleus, Smad complexes do not act alone. Instead, they cooperate with other transcription factors, co-activators, and chromatin regulatory proteins to determine the spectrum of target gene expression. Their downstream targets include not only cell cycle inhibitory genes, but also extracellular matrix-related genes and EMT-associated transcriptional regulators. Thus, the transcriptional output of the TGF-β pathway is not unidirectional, but varies according to cell type and microenvironmental context.

Table 1. Major Components of the Canonical TGF-β Pathway

 

Level	Key molecules	Main role
Ligand level	TGF-β1, TGF-β2, TGF-β3	Provide upstream stimulation and define isoform context
Receptor level	TGFBR2, TGFBR1/ALK5	Form receptor complexes and initiate intracellular transduction
Canonical transduction level	Smad2, Smad3, Smad4	Mediate nuclear transcriptional regulation
Negative regulatory level	Smad7	Provide receptor-level negative feedback inhibition

 

4. Non-Smad Branches and Their Crosstalk with the Canonical Axis

4.1 ERK Branch

In certain cellular contexts, TGF-β can activate the ERK1/2 branch. ERK signaling is usually associated with proliferative adaptation, survival, migration, and enhancement of certain EMT-related effects. In tumor cells and some activated fibroblasts, the ERK branch often cooperates with the Smad axis in phenotypic remodeling.

 

4.2 JNK and c-Jun Branch

The JNK-c-Jun axis is one of the most common stress-response and transcription-enhancing modules among the non-Smad branches of TGF-β signaling. This branch can influence AP-1-related transcriptional programs and enhance migration, inflammation-like responses, and EMT-associated gene expression. In some models, enhanced c-Jun phosphorylation after TGF-β stimulation often indicates that AP-1 cooperative transcription is participating in pathway output.

 

4.3 p38 Branch

p38 MAPK is another important non-Smad branch in TGF-β signaling and is frequently associated with stress adaptation, inflammatory microenvironmental responses, and fibrosis-related phenotypes. Activation of p38 can amplify matrix production, cell contractility, and tissue remodeling signals, making it a high-priority target in fibrosis studies.

 

4.4 Relationship Between the Canonical Axis and Bypass Signals

The Smad-dependent pathway determines the basic direction of TGF-β signaling, whereas non-Smad branches often determine phenotype intensity, response duration, and output bias in specific contexts. In experimental design, measuring only p-Smad2/3 while ignoring ERK, JNK, or p38 often makes it difficult to fully explain why the same receptor stimulation produces different degrees of migration, EMT, or fibrotic phenotypes.

 

5. Major Biological Effects of the TGF-β Pathway

5.1 Growth Inhibition

In normal epithelial cells and certain early-stage tumor cells, TGF-β often acts as a growth-inhibitory signal. It can induce expression of cell cycle inhibitory factors and suppress pro-proliferative programs, thereby maintaining tissue homeostasis and growth restraint.

 

5.2 Cell Differentiation and Fate Regulation

TGF-β plays important roles in development, maintenance of stem cell states, and lineage differentiation. Its specific outputs depend heavily on cell type and the surrounding signaling background; therefore, the same stimulus may promote differentiation, inhibit differentiation, or induce lineage switching in different models.

 

5.3 Extracellular Matrix Deposition and Fibrosis

TGF-β is one of the most central molecules in fibrosis research. Upon pathway activation, it induces the expression of collagen, fibronectin, and multiple matrix remodeling molecules, while promoting the transition of fibroblasts toward a myofibroblast phenotype, ultimately leading to tissue stiffening and functional decline of organs.

 

5.4 Epithelial-Mesenchymal Transition

TGF-β is a classical inducer in EMT research. During this process, epithelial markers such as E-cadherin decrease, while mesenchymal markers such as N-cadherin, Vimentin, and related transcriptional regulators increase, accompanied by enhanced cell migration, invasiveness, and plasticity.

 

5.5 Immunosuppression and Microenvironmental Remodeling

TGF-β can suppress effector T-cell function, promote regulatory T-cell formation, and influence the state of macrophages, dendritic cells, and stromal cells. Therefore, this pathway is not only an intracellular signaling axis, but also an important regulatory network shaping an immunosuppressive microenvironment.

 

6. Disease Relevance

6.1 Fibrotic Diseases

In the fibrosis of organs such as liver, lung, kidney, and myocardium, the TGF-β pathway is often maintained in a persistently high-activity state. Its pathological significance lies in driving long-term maintenance of Smad3-dominant matrix production programs while cooperating with bypass branches such as p38 to amplify tissue remodeling effects.

 

6.2 Stage-Dependent Roles in Tumors

TGF-β exerts different functions at different stages of tumor development. In early tumors, TGF-β often suppresses proliferation and maintains growth restraint. During tumor progression, tumor cells gradually become insensitive to its growth-inhibitory effects, yet may retain or even enhance outputs related to EMT, immunosuppression, invasion, and metastasis. Therefore, the role of TGF-β in tumors is strongly stage-dependent and cannot be simply classified as exclusively oncogenic or tumor-suppressive.

 

6.3 Immune and Inflammatory Tolerance

In chronic inflammation, tumor immune evasion, and parasite-associated immune regulation, the TGF-β pathway may participate in establishing a tolerant environment. Research on these problems usually requires simultaneous attention to ligand level, Smad3 activation, and whether non-Smad branches are also involved.

 

7. Common Experimental Readouts in Research

7.1 Ligand and Receptor Level

Common indicators include expression of TGF-β1, TGF-β2, and TGF-β3, levels of activated TGF-β, and the expression status of TGFBR1 and TGFBR2. If the research focus is the true degree of pathway activation, total TGF-β should be distinguished as much as possible from latent or activated TGF-β.

 

7.2 Canonical Transduction Level

p-Smad2, p-Smad3, and nuclear translocation of Smad4 are the most commonly used canonical transduction readouts. Smad7 is often used to evaluate negative feedback status. In fibrosis- and EMT-related studies, p-Smad3 is usually more directly informative than total Smad3.

 

7.3 Non-Smad Branch Level

Phosphorylation states of ERK1/2, JNK-c-Jun, and p38 are common bypass readouts. If the study concerns enhanced migration, stress amplification, or invasive phenotypes, measuring only the Smad axis is often insufficient, and combined analysis of these bypass signals is necessary.

 

7.4 Functional Level

Functional readouts usually include the expression of matrix molecules such as collagen, FN1, and SERPINE1; changes in EMT markers such as E-cadherin, N-cadherin, and Vimentin; and results from migration, invasion, contraction, and morphological remodeling assays. Functional conclusions should not be based solely on a single phosphorylation event, but should instead be judged in combination with terminal phenotypes.

Table 2. Common Experimental Readouts in TGF-β Pathway Research

 

Research level	Common indicators	Main significance
Ligand/receptor level	TGF-β1, TGFBR1, TGFBR2	Determine upstream stimulatory conditions
Canonical transduction level	p-Smad2, p-Smad3, Smad4	Determine whether Smad-dependent signaling is established
Non-Smad branch level	ERK, JNK/c-Jun, p38	Determine whether bypass signaling participates in output
Functional level	Collagen, FN1, EMT markers, migration/invasion	Determine terminal phenotypic changes

 

Table 3. Core Ligand, Receptor, and Direct Intervention Products for the TGF-β Pathway

 

Product category	Catalog No.	Name	Specification or purity	Suitable research direction/use
Mimetic ligand	rp174274	H. polygyrus TGF-β mimic	Moligand™	For TGF-β-like signaling simulation and host-parasite immune regulation studies
Human recombinant ligand	rp168406-GMP	Recombinant Human TGF-beta 1 GMP Protein	Animal Free,Carrier Free,Bioactive,ActiBioPure™,High Performance,≥97%(SDS-PAGE&SEC-HPLC)	For high-standard TGF-β1 stimulation experiments and functional studies
Human recombinant ligand	rp176238	Recombinant Human TGF-beta 1 Monomer Protein	Carrier Free,Bioactive,ActiBioPure™,His Tag,≥95%(SDS-PAGE)	For monomeric TGF-β1 studies and structure-function analysis
Human recombinant ligand	rp152261	Recombinant Human TGF-beta 1 Protein	Animal Free,Carrier Free,Bioactive,ActiBioPure™,High Performance,His Tag,≥95%(SDS-PAGE)	For canonical TGF-β1 pathway stimulation, EMT, and fibrosis model establishment
Human recombinant ligand	rp231117	Recombinant Human TGF-beta 1 Protein	Animal Free,Carrier Free,Bioactive,ActiBioPure™,High Performance,His Tag,≥95%(SDS-PAGE),expressed in HEK293; See COA	For human TGF-β1 stimulation and mammalian expression system-related studies
Human recombinant ligand	rp156015	Recombinant Human TGF-beta 1 Protein	Animal Free,Carrier Free,Bioactive,ActiBioPure™,His Tag,≥95%(SDS-PAGE),See COA	For TGF-β1 induction experiments and dose-response analysis
Human recombinant ligand	rp181279	Recombinant Human TGF-beta 2 Protein	Animal Free,Carrier Free,Bioactive,ActiBioPure™,High Performance,His Tag,≥95%(SDS-PAGE),expressed in HEK293; See COA	For TGF-β2 isoform studies and functional comparison with TGF-β1
Mouse recombinant ligand	rp167840	Recombinant Mouse TGF-beta 1 Protein	Animal Free,Carrier Free,Bioactive,ActiBioPure™,Azide Free,High Performance,His Tag,≥95%(SDS-PAGE)	For mouse TGF-β1 stimulation experiments and animal model validation
Mouse recombinant ligand	rp168042	Recombinant Mouse TGF-beta 2 Protein	Animal Free,Carrier Free,Bioactive,ActiBioPure™,High Performance,His Tag,≥95%(SDS-PAGE)	For mouse TGF-β2 pathway studies
Receptor protein	rp154716	Recombinant Mouse TGF-beta RII Protein	Animal Free,Carrier Free,Bioactive,ActiBioPure™,High Performance,His Tag,Fc tag,≥95%(SDS-PAGE)	For TGFBR2 binding, blockade, and receptor-level functional studies
Coreceptor/accessory receptor protein	rp181281	Recombinant Human TGF-beta RIII Protein	Animal Free,Carrier Free,His Tag,≥90%(SDS-PAGE)	For studies of TGF-β accessory receptor function and ligand presentation
Pathway inhibitor	T1453184	TGF-β1/Smad3-IN-1	Moligand™,≥98%	For inhibition studies of the TGF-β1/Smad3 axis
Pathway inhibitor	T1498544	TGF-β1/Smad3-IN-1	Moligand™, 10 mM in DMSO	For inhibition of the TGF-β1/Smad3 axis in cell-based experiments
Receptor inhibitor	T1454414	TGF-βRI inhibitor 1		For validation of TGFBR1/ALK5 dependence
Receptor inhibitor	T1454415	TGF-βRI inhibitor 1 methylbenzenesulfonate		For validation of TGFBR1/ALK5 dependence
Functional peptide tool	P1454571	pm26TGF-β1 peptide		For functional peptide studies related to TGF-β1
Functional peptide tool	P1454676	pm26TGF-β1 peptide TFA	≥99%	For high-purity TGF-β1 functional peptide studies
Compound library	Lib412060	TGF-beta/Smad compound library		For TGF-β/Smad pathway screening and mechanistic studies

 

Table 4. Products for Validation of the Smad3 Axis and Non-Smad Branches in the TGF-β Pathway

 

Product category	Catalog No.	Name	Specification or purity	Suitable research direction/use
Smad3 recombinant protein	rp329390	Recombinant Human SMAD3 Protein	≥95%(SDS-PAGE)	For in vitro functional studies of Smad3
Smad3 recombinant protein	rp156654	Recombinant Human Smad3 Protein	Carrier Free,Azide Free,His Tag,≥95%(SDS-PAGE)	For Smad3 function and binding studies
Smad3 recombinant protein	rp184657	Recombinant Human Smad3 Protein	Carrier Free,Azide Free,His Tag,≥90%(SDS-PAGE)	For Smad3 functional studies
Phospho-Smad3 detection	Ab325713	Recombinant Phospho-Smad3 (S423 + S425) Antibody	KO Validation	For detection of canonical TGF-β pathway activation
Smad3 detection antibody	Ab128212	Recombinant SMAD3 Antibody	ExactAb™, Validated, Recombinant, 1 mg/mL	For SMAD3 protein detection
Smad3 gene intervention	S1476244	SMAD3 Human Pre-designed siRNA Set A		For SMAD3 knockdown and validation of pathway dependence
Smad3 knockout control	P750544	pLenti-SMAD3-sgRNA		For SMAD3 protein-negative control
Smad3 knockout control	P750545	pLenti-SMAD3-sgRNA		For RNA-level control of SMAD3 knockout
Smad3 detection antibody	Ab186978	Smad3 Mouse mAb	Carrier Free,ExactAb™,Azide Free,Validated,High Performance,PBS Only,≥95%(SDS-PAGE),1.0 mg/mL	For Smad3 protein detection
Smad3 detection antibody	Ab188096	Smad3 Mouse mAb	Carrier Free,ExactAb™,Azide Free,Validated,High Performance,PBS Only,≥95%(SDS-PAGE),1.0 mg/mL	For Smad3 protein detection
Smad3 detection antibody	Ab156560	Smad3 Mouse mAb	Carrier Free,ExactAb™,Azide Free,Validated,High Performance,PBS Only,≥95%(SDS-PAGE),1.0 mg/mL	For Smad3 protein detection
c-Jun branch	rp214406	Recombinant Human c-Jun Protein	Carrier Free,His Tag,≥95%(SDS-PAGE),See COA	For functional studies of the AP-1/c-Jun branch
c-Jun branch	Ab326843	Recombinant Phospho-c-Jun (T91) Antibody	KD Validation	For detection of c-Jun activation in the non-Smad branch of TGF-β signaling
c-Jun branch	Ab096607	Recombinant c-Jun Antibody	Recombinant,ExactAb™,Validated,See COA	For c-Jun protein detection
c-Jun branch	Ab327302	Recombinant c-Jun Antibody	KD Validation	For c-Jun protein detection
ERK branch	E656204	ERK1/2 inhibitor 1	10mM in DMSO	For validation of ERK1/2 dependence
ERK branch	E650276	ERK1/2 inhibitor 1	≥99%	For validation of ERK1/2 dependence
ERK branch	Ab102223	Recombinant ERK1 Antibody	ExactAb™, Validated, Recombinant, High performance, 2mg/mL	For ERK1 protein detection
ERK branch	Ab326841	Recombinant ERK1/2 Antibody	KD Validation	For ERK1/2 protein detection
ERK branch	rp184918	Recombinant Human ERK1 Protein	Carrier Free,Bioactive,ActiBioPure™,His Tag,≥85%(SDS-PAGE),See COA	For in vitro functional studies of ERK1
ERK branch	Ab102232	ERK2 Mouse mAb	Carrier Free, ExactAb™, Azide Free, Validated, High Performance, See COA	For ERK2 protein detection
ERK branch	Ab102233	Recombinant ERK2 Antibody	ExactAb™, Validated, Recombinant, 0.5 mg/mL	For ERK2 protein detection
ERK branch	rp184960	Recombinant Human ERK2 Protein	Carrier Free, Bioactive, ActiBioPure™, ≥90%(SDS-PAGE), See COA	For in vitro functional studies of ERK2
JNK branch	rp183743	Recombinant Human JNK1 Protein	Carrier Free,Bioactive,ActiBioPure™,His Tag,≥85%(SDS-PAGE),See COA	For JNK1 functional studies
JNK branch	Ab111518	Recombinant JNK1 Antibody	ExactAb™, Validated, Recombinant, 1.0 mg/mL	For JNK1 protein detection
JNK branch	Ab111513	Recombinant JNK1/JNK2/JNK3 Antibody	Recombinant, ExactAb™, Validated, See COA	For detection of JNK family proteins
p38 branch	rp184106	Recombinant Human p38 alpha Protein	Carrier Free,His Tag,≥90%(SDS-PAGE),See COA	For in vitro functional studies of p38α
p38 branch	Ab326787	Recombinant Phospho-p38 (T180) Antibody	KD Validation	For detection of p38 activation
p38 branch	Ab119717	Recombinant p38 alpha/MAPK14 Antibody	Recombinant, ExactAb™, Validated, High Performance, See COA	For p38α/MAPK14 detection
p38 branch	Ab184697	p38 alpha Mouse mAb	Carrier Free,ExactAb™,Azide Free,Validated,High Performance,PBS Only,≥95%(SDS-PAGE),1.0 mg/mL	For p38α protein detection
p38 branch	P338122	p38 MAP Kinase Inhibitor IV	≥95%	For validation of p38 dependence
p38 branch	P647352	p38 MAPK-IN-1	≥99%	For p38 pathway inhibition studies
p38 branch	P654996	p38 MAPK-IN-1	10mM in DMSO	For inhibition of p38 in cell-based experiments
p38 branch	P649886	p38-α MAPK-IN-1	≥99%	For validation of p38α dependence
p38 branch	P656040	p38-α MAPK-IN-1	10mM in DMSO	For inhibition of p38α in cell-based experiments

 

Table 5. Quantitative Detection Reagents for the TGF-β Pathway

 

Product category	Catalog No.	Name	Specification or purity	Suitable research direction/use
Smad3 quantitative detection	H1510082	Human SMAD3 ELISA Kit	BioReagent	For quantitative detection of human SMAD3
Smad3 quantitative detection	EJ1513636	Human SMAD Family Member 3 (SMAD3) ELISA Kit	BioReagent	For quantitative detection of human Smad3
Smad3 quantitative detection	R1510089	Rat SMAD3 ELISA Kit	BioReagent	For quantitative detection of rat SMAD3
Smad3 quantitative detection	EJ1511911	Rat Mothers Against Decapentaplegic Homolog 3 (Smad3) ELISA Kit	BioReagent	For quantitative detection of rat Smad3
Smad3 quantitative detection	M1510090	Mouse SMAD3 ELISA Kit	BioReagent	For quantitative detection of mouse SMAD3
Ligand quantitative detection	EJ1515200	Human LAP Transforming Growth Factor Beta 1 (LAP TGF-β1) ELISA Kit	BioReagent	For detection of latent TGF-β1
Ligand quantitative detection	EJ1514990	Human transforming growth factor-β (TGF-β) ELISA Kit	BioReagent	For quantitative detection of total human TGF-β
Ligand quantitative detection	EJ1514991	Human Transforming Growth Factor Beta 1 (TGF-β1) ELISA Kit	BioReagent	For quantitative detection of human TGF-β1
Ligand quantitative detection	H1509813	Human TGF-β1 ELISA Kit	BioReagent	For quantitative detection of human TGF-β1
Ligand quantitative detection	EJ1514992	Human Transforming Growth Factor Beta 2 (TGF-β2) ELISA Kit	BioReagent	For quantitative detection of human TGF-β2
Ligand quantitative detection	EJ1514993	Human Transforming Growth Factor Beta 3 (TGF-β3) ELISA Kit	BioReagent	For quantitative detection of human TGF-β3
Ligand quantitative detection	EJ1512363	Rat Transforming Growth Factor Beta (TGF-β) ELISA Kit	BioReagent	For quantitative detection of total rat TGF-β
Ligand quantitative detection	EJ1512364	Rat Transforming Growth Factor Beta 1 (TGF-β1) ELISA Kit	BioReagent	For quantitative detection of rat TGF-β1
Ligand quantitative detection	R1509833	Rat TGF-β1 ELISA Kit	BioReagent	For quantitative detection of rat TGF-β1
Ligand quantitative detection	EJ1512365	Rat Transforming Growth Factor Beta 2 (TGF-β2) ELISA Kit	BioReagent	For quantitative detection of rat TGF-β2
Ligand quantitative detection	EJ1512366	Rat Transforming Growth Factor Beta 3 (TGF-β3) ELISA Kit	BioReagent	For quantitative detection of rat TGF-β3
Ligand quantitative detection	EJ1513280	Mouse Transforming Growth Factor Beta (TGF-β) ELISA Kit	BioReagent	For quantitative detection of total mouse TGF-β
Ligand quantitative detection	EJ1513281	Mouse Transforming Growth Factor β1(TGF-β1) ELISA Kit	BioReagent	For quantitative detection of mouse TGF-β1
Ligand quantitative detection	M1509858	Mouse TGF-β1 ELISA Kit	BioReagent	For quantitative detection of mouse TGF-β1
Ligand quantitative detection	EJ1513282	Mouse Transforming Growth Factor β2(TGF-β2) ELISA Kit	BioReagent	For quantitative detection of mouse TGF-β2
Ligand quantitative detection	EJ1513283	Mouse Transforming Growth Factor β3(TGF-β3) ELISA Kit	BioReagent	For quantitative detection of mouse TGF-β3
Ligand quantitative detection	EJ1511824	Monkey Transforming Growth Factor Beta (TGF-β) ELISA Kit	BioReagent	For quantitative detection of total monkey TGF-β
Ligand quantitative detection	EJ1511825	Monkey Transforming Growth Factor Beta 1 (TGF-β1) ELISA Kit	BioReagent	For quantitative detection of monkey TGF-β1
Ligand quantitative detection	EJ1511826	Monkey Transforming Growth Factor Beta 2 (TGF-β2) ELISA Kit	BioReagent	For quantitative detection of monkey TGF-β2
Ligand quantitative detection	EJ1511834	Guinea Pig Transforming Growth Factor Beta (TGF-β) ELISA Kit	BioReagent	For quantitative detection of total guinea pig TGF-β

 

The research value of the TGF-β signaling pathway lies in its integration of ligand activation, receptor assembly, Smad transduction, non-Smad branches, and microenvironmental remodeling into a continuous regulatory system.

 

For more related articles, please see below:

[1] Ras-Raf-MEK-ERK Signaling

[2] Wnt/β-Catenin Signaling Pathway

[3] How to Map the NF-κB Pathway and Choose Inhibitors: Bringing Inflammatory Transcriptional Output into a “Controllable Range” (Tables A–F)

[4] Metabolic signaling pathway

[5] Wnt Signaling

[6] Hedgehog Signaling

[7] JAK-STAT Cell Signaling Pathway

[8] PD-1/PD-L1 Signaling Pathway

 

References

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[2] Deheuninck J, Luo K. Ski and SnoN, potent negative regulators of TGF-beta signaling. Cell Res. 2009;19(1):47-57.

[3] Otten J, Bokemeyer C, Fiedler W. TGF-beta superfamily receptors-targets for antiangiogenic therapy? J Oncol. 2010;2010:317068.