TGFB2 Human, HEK

Transforming Growth Factor-Beta 2 Human Recombinant, HEK

Recombinant Human TGF-b 2, produced in HEK cells, is a non-glycosylated homodimeric protein with a molecular weight of 25 kDa. The purification process of TGF-b 2 involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4785
Source
HEK.
Appearance
White, lyophilized (freeze-dried) powder, sterile filtered.

TGFB3 (207 a.a.) Human

Transforming Growth Factor-Beta 3 (207 a.a.) Human Recombinant

This product consists of the recombinant human TGF-beta 3 protein. It encompasses amino acids 644 to 850 of the full-length protein and has a total molecular weight of 50 kDa, including the GST tag.
Shipped with Ice Packs
Cat. No.
BT4853
Source
Escherichia Coli.
Appearance
The product is a clear solution that has been sterilized by filtration.

TGFB3 (24-412 a.a.) Human

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

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.
Shipped with Ice Packs
Cat. No.
BT4947
Source
Escherichia Coli.
Appearance
The product is a sterile, filtered solution that is colorless.

TGFB3 Human

Transforming Growth Factor-Beta 3 Human Recombinant

Recombinant Human TGF-β3, expressed in E. coli, is a non-glycosylated homodimer linked by disulfide bonds. Each polypeptide chain consists of 113 amino acids, resulting in a total molecular mass of 25.8 kDa for the dimer. The purification process of TGF-β3 involves standard chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT5046
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized through filtration.

TGFB1 Human, His

Transforming Growth Factor-Beta 1 Human Recombinant, His Tag

Recombinant human TGFβ1, expressed in E. coli, is a non-glycosylated polypeptide chain containing 112 amino acids (corresponding to the active fragment spanning positions 279 to 390). This protein has a molecular weight of 17.3 kDa and includes a 4.5 kDa amino-terminal hexahistidine tag for purification purposes. The purification process involves proprietary chromatographic techniques to ensure high purity.
Shipped with Ice Packs
Cat. No.
BT3116
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

TGFB1 (113 a.a.) Human

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

Recombinant Human TGF-beta 1, produced in E. coli, is a single-chain polypeptide lacking glycosylation. It comprises 113 amino acids (residues 279-390) and has a molecular weight of 12.9 kDa. The purification of TGF-beta 1 (113 a.a.) is achieved through specialized chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT2615
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

TGFB1 Human

Transforming Growth Factor-beta 1 Human

This product contains human transforming growth factor-beta 1 (TGF-beta 1), a protein with a molecular weight of 25 kDa. It is purified from human platelets using proprietary chromatography methods.
Shipped with Ice Packs
Cat. No.
BT2720
Source
Human Platelets.
Appearance
The product is a sterile, lyophilized powder that appears white in color.

TGFB1 Human Recombinant

Transforming Growth Factor-Beta 1 Human Recombinant

Recombinant human TGFB1, produced in CHO cells, is a glycosylated homodimeric polypeptide chain consisting of 2 chains of 112 amino acids each. The total molecular weight of the protein is 25.6kDa. TGFB1 is purified using proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT2793
Source

CHO cells.

Appearance

The product appears as a sterile, filtered, white, lyophilized (freeze-dried) powder.

TGFB2 Human

Transforming Growth Factor Beta 2 Human Recombinant

Recombinant human TGFB2, produced in plants, is a homodimeric protein comprising two identical polypeptide chains, each consisting of 118 amino acids. Its total molecular weight is 27.08 kDa. The TGFB2 protein has a 6xHis tag fused at its N-terminus and undergoes purification using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT4700
Source
Nicotiana benthamiana.
Appearance
White powder, sterile and lyophilized (freeze-dried).

TGFB1 Mouse

Transforming Growth Factor-Beta 1 Mouse Recombinant

Recombinant Mouse TGFB1, produced in E. coli, is a single polypeptide chain without any glycosylation modifications. It consists of 135 amino acids (corresponding to amino acid positions 279-390 of the native protein) and has a molecular weight of 15.2 kDa. For purification and detection purposes, a 23 amino acid Histidine tag is attached to the N-terminus of the TGFB1 protein. Purification is carried out using proprietary chromatographic methods.

Shipped with Ice Packs
Cat. No.
BT4603
Source
Escherichia Coli.
Appearance

The product is a clear, colorless solution that has been sterilized by filtration.

Definition and Classification

Transforming Growth Factor (TGF) refers to a group of proteins that play crucial roles in cellular processes such as proliferation, differentiation, and apoptosis. TGFs are classified into two main types: TGF-α and TGF-β. TGF-α is primarily involved in epithelial cell proliferation, while TGF-β has a broader range of functions, including regulation of immune responses and maintenance of tissue homeostasis.

Biological Properties

Key Biological Properties: TGFs are multifunctional cytokines that influence various cellular activities. They are involved in cell growth, differentiation, and repair processes.

Expression Patterns: TGF-β is expressed in almost all cell types, whereas TGF-α expression is more restricted, primarily found in epithelial cells and certain tumor cells.

Tissue Distribution: TGF-β is ubiquitously distributed across various tissues, including the immune system, skin, and connective tissues. TGF-α is mainly found in tissues with high regenerative capacity, such as the skin and gastrointestinal tract.

Biological Functions

Primary Biological Functions: TGFs are essential for regulating cell growth and differentiation. TGF-β, in particular, plays a critical role in wound healing, fibrosis, and immune regulation.

Role in Immune Responses: TGF-β modulates immune responses by inhibiting the proliferation and activation of lymphocytes and macrophages. It also promotes the differentiation of regulatory T cells, which help maintain immune tolerance.

Pathogen Recognition: TGF-β can influence the immune system’s ability to recognize and respond to pathogens by modulating the activity of various immune cells.

Modes of Action

Mechanisms with Other Molecules and Cells: TGFs interact with specific receptors on the cell surface, initiating a cascade of intracellular signaling events. TGF-β binds to TGF-β receptors, leading to the activation of Smad proteins, which translocate to the nucleus and regulate gene expression.

Binding Partners: TGF-β interacts with various co-receptors and binding proteins, such as betaglycan and endoglin, which modulate its activity and signaling.

Downstream Signaling Cascades: The TGF-β signaling pathway involves the phosphorylation of receptor-regulated Smads (R-Smads), which form complexes with common-partner Smads (Co-Smads) and translocate to the nucleus to regulate target gene expression.

Regulatory Mechanisms

Expression and Activity Control: The expression and activity of TGFs are tightly regulated at multiple levels, including transcriptional, post-transcriptional, and post-translational modifications.

Transcriptional Regulation: TGF-β gene expression is controlled by various transcription factors and regulatory elements within its promoter region.

Post-Translational Modifications: TGF-β undergoes several post-translational modifications, such as proteolytic cleavage and glycosylation, which are essential for its activation and function.

Applications

Biomedical Research: TGFs are widely studied in biomedical research due to their roles in cell growth, differentiation, and immune regulation. They are used as tools to understand various cellular processes and disease mechanisms.

Diagnostic Tools: Elevated levels of TGF-β are associated with various diseases, including cancer and fibrosis, making it a potential biomarker for diagnostic purposes.

Therapeutic Strategies: TGFs are being explored as therapeutic targets for treating diseases such as cancer, fibrosis, and autoimmune disorders. Inhibitors of TGF-β signaling are being developed to counteract its pro-fibrotic and immunosuppressive effects.

Role in the Life Cycle

Development: TGFs play crucial roles in embryonic development, including the formation of the extracellular matrix and the regulation of cell differentiation.

Aging: TGF-β signaling is implicated in the aging process, particularly in the context of tissue repair and fibrosis. Dysregulation of TGF-β signaling can contribute to age-related diseases.

Disease: Aberrant TGF-β signaling is associated with various pathological conditions, including cancer, fibrosis, and autoimmune diseases. Understanding the role of TGFs in these diseases can provide insights into potential therapeutic interventions.

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