TFF1 Human

Trefoil Factor-1 Human Recombinant

Recombinant Human TFF-1, produced in E. coli, is a non-glycosylated polypeptide chain arranged as a homodimer. Each chain comprises 60 amino acids, including a 40 amino acid trefoil motif with three conserved intramolecular disulfide bonds. The total molecular mass of the protein is 13.2 kDa. The purification process of Recombinant Human TFF-1 involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT22925
Source
Escherichia Coli.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.

TFF1 Human, His

Trefoil Factor-1 Human Recombinant, His Tag

Recombinant Human TFF-1, produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 70 amino acids (residues 25-84), including a 10 amino acid His tag, resulting in a total molecular mass of 7.9 kDa. The purification of Recombinant Human TFF-1 is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23026
Source
Escherichia Coli.
Appearance
White, lyophilized (freeze-dried) powder after filtration.

TFF2 Human

Trefoil Factor-2 Human Recombinant

Recombinant Human TFF2, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 106 amino acids (residues 24-129) with a molecular weight of 12 kDa. This protein contains a 40-amino acid trefoil motif characterized by three conserved intramolecular disulfide bonds and undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23112
Source
Escherichia Coli.
Appearance
White lyophilized (freeze-dried) powder, sterile filtered.

TFF2 Human, His

Trefoil Factor-2 Human Recombinant, His Tag

Recombinant Human TFF-2, expressed in E. coli, is a single, non-glycosylated polypeptide chain. This protein consists of 116 amino acids (residues 24-129), including a 10-amino acid His Tag fused at the N-terminus, resulting in a total molecular mass of 13.2 kDa. The purification of Recombinant Human TFF2 is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23199
Source
Escherichia Coli.
Appearance
White lyophilized (freeze-dried) powder.

TFF3 Human

Trefoil Factor-3 Human Recombinant

Recombinant human TFF-3, produced in E. coli, is a homodimeric polypeptide chain that is not glycosylated. It consists of two chains, each containing 59 amino acids, totaling 118 amino acids. A key feature of TFF-3 is the presence of a 40 amino acid trefoil motif, which includes three conserved intermolecular disulfide bonds. The total molecular mass of the protein is 13.2 kDa. The purification of recombinant human TFF-3 is carried out using specialized chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT23285
Source
Escherichia Coli.
Appearance
The product is a sterile, white powder that has been lyophilized (freeze-dried) after filtration.

TFF3 Human, His

Trefoil Factor-3 Human Recombinant, His Tag

Recombinant human TFF3, expressed in E. coli, is a non-glycosylated polypeptide chain containing 69 amino acids (residues 22-80). It includes a 10-amino acid His tag fused at the N-terminus, resulting in a total molecular mass of 7.82 kDa. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT23351
Source
Escherichia Coli.
Appearance
A white powder in lyophilized form.

TFF3 Rat

Trefoil Factor-3 Rat Recombinant

This product is a recombinant Trefoil Factor-3 protein of rat origin (TFF3 Rat). It has been engineered with a C-terminal Flag-tag (9 amino acids total: 1 N-terminal + 8 C-terminal) and produced in E. coli. The resulting protein is 7.7 kDa in size and comprises 68 amino acid residues.
Shipped with Ice Packs
Cat. No.
BT23427
Source
Escherichia Coli.
Appearance
The product appears as a white lyophilized (freeze-dried) powder after filtration.
Definition and Classification

Trefoil factors (TFFs) are a family of small, secreted proteins characterized by the presence of a three-loop structure known as the trefoil domain . These proteins are highly resistant to heat, acid, and protease degradation . The TFF family consists of three members: TFF1, TFF2, and TFF3, each encoded by distinct genes located on chromosome 21q22.3 .

Biological Properties

Key Biological Properties: TFFs are primarily synthesized and secreted by mucin-secreting epithelial cells lining the gastrointestinal tract . They are highly conserved during evolution and exhibit resistance to thermal and enzymatic digestion .

Expression Patterns and Tissue Distribution: TFF1 and TFF2 are predominantly expressed in the stomach, while TFF3 is mainly found in the small and large intestines . Additionally, TFFs are expressed in various tissues, including the brain, urogenital system, lymphoid tissue, respiratory tract, and conjunctival goblet cells .

Biological Functions

Primary Biological Functions: TFFs play a crucial role in maintaining the integrity and repair of mucosal surfaces . They are involved in mucosal defense, wound healing, and epithelial restitution .

Role in Immune Responses and Pathogen Recognition: TFFs contribute to the innate immune defense by stabilizing the mucus layer and protecting the mucosa from insults . They also interact with immune cells and participate in immune regulation .

Modes of Action

Mechanisms with Other Molecules and Cells: TFFs interact with mucins to enhance the protective properties of the mucus layer . They also bind to various molecules, including growth factors and cytokines, to modulate cellular responses .

Binding Partners and Downstream Signaling Cascades: TFFs form complexes with other proteins, such as gastrokine-2 and IgG Fc binding protein (FCGBP), to mediate their effects . They activate signaling pathways, including the MAPK/ERK and STAT3 pathways, to regulate cellular processes .

Regulatory Mechanisms

Regulatory Mechanisms Controlling Expression and Activity: TFF expression is regulated by genetic, epigenetic, and tissue-specific mechanisms . These include promoter methylation, chromatin modification, histone acetylation, and transcription factor binding .

Transcriptional Regulation and Post-Translational Modifications: TFFs are subject to transcriptional regulation by factors such as STAT3 . Post-translational modifications, including glycosylation, also play a role in modulating TFF activity .

Applications

Biomedical Research: TFFs are valuable tools in studying mucosal biology and gastrointestinal diseases . They are used to investigate the mechanisms of mucosal protection and repair .

Diagnostic Tools and Therapeutic Strategies: TFFs have potential applications in diagnostics and therapeutics. They are being explored as biomarkers for gastrointestinal diseases and as therapeutic agents for conditions such as inflammatory bowel disease and gastric ulcers .

Role in the Life Cycle

Role Throughout the Life Cycle: TFFs are involved in various stages of life, from development to aging . They play a role in tissue development, maintenance, and repair . In pathological conditions, TFF expression and function can be altered, contributing to disease progression .

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