Recombinant Proteins

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TBCA Human

Tubulin Folding Cofactor A Human Recombinant

Recombinant human TBCA, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 108 amino acids (1-108 a.a.). It has a molecular mass of 12.8 kDa. TBCA is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT19987
Source
Escherichia Coli.
Appearance
Sterile, colorless solution.

TBCB Human

Tubulin Folding Cofactor B Human Recombinant

Recombinant TBCB Human, produced in E. coli, is a single polypeptide chain comprising 268 amino acids (1-244) with a molecular weight of 29.9 kDa. It includes a 24 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT20076
Source
E.coli.
Appearance
Clear, colorless solution, sterile-filtered.

TBCC Human

Tubulin Folding Cofactor C Human Recombinant

Recombinant human TBCC, produced in E. coli, is a single polypeptide chain consisting of 369 amino acids (residues 1-346) with a molecular weight of 41.7 kDa. It includes a 23 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT20167
Source
E.coli.
Appearance
Clear, colorless solution, sterile-filtered.

TBCEL Human

Tubulin Folding Cofactor E-Like Human Recombinant

Recombinant Human TBCEL, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 447 amino acids. It has a molecular weight of 50.6 kDa. The purification of TBCEL is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT20282
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterilized by filtration.

TPPP3 Human

Tubulin Polymerization-Promoting Protein Family Member 3 Human Recombinant

Recombinant human TPPP3, expressed in E. coli, is a non-glycosylated polypeptide chain lacking any glycosylation modifications. It consists of 199 amino acids, with a sequence spanning from position 1 to 176, and has a molecular weight of 21.4 kDa. The protein is engineered with a 23 amino acid His-tag fused to its N-terminus to facilitate purification, which is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT20369
Source
Escherichia Coli.
Appearance
The product is a clear, colorless solution that has undergone sterile filtration.
Definition and Classification

Tubulin Folding Cofactors (TFCs) are a group of proteins essential for the proper folding and assembly of tubulin, the building block of microtubules. These cofactors are classified into five main types: TFC A, TFC B, TFC C, TFC D, and TFC E . Each cofactor plays a specific role in the tubulin folding pathway, ensuring the correct formation of α/β-tubulin heterodimers .

Biological Properties

Key Biological Properties: TFCs are involved in the folding and stabilization of tubulin monomers, preventing the formation of non-functional aggregates . They are crucial for maintaining the stoichiometric balance of α- and β-tubulin .

Expression Patterns and Tissue Distribution: TFCs are ubiquitously expressed in eukaryotic cells, with varying levels depending on the tissue type and developmental stage . For instance, TFC A is highly expressed in plant cells, where it plays a significant role in microtubule organization .

Biological Functions

Primary Biological Functions: TFCs facilitate the proper folding of tubulin monomers, leading to the formation of functional microtubules . These microtubules are essential for various cellular processes, including cell division, intracellular transport, and maintenance of cell shape .

Role in Immune Responses and Pathogen Recognition: While TFCs are primarily involved in tubulin folding, their role in immune responses and pathogen recognition is less direct. However, the proper functioning of microtubules, facilitated by TFCs, is crucial for the immune system’s ability to respond to pathogens .

Modes of Action

Mechanisms with Other Molecules and Cells: TFCs interact with tubulin monomers and chaperonins to facilitate the correct folding of tubulin . For example, TFC B initially binds to α-tubulin, while TFC A binds to β-tubulin. These are then replaced by TFCs E and D, respectively, to form a quaternary complex .

Binding Partners and Downstream Signaling Cascades: TFCs form complexes with tubulin monomers and other cofactors to ensure the proper assembly of microtubules . The release of assembly-competent α/β-tubulin heterodimers is triggered by the binding of TFC C .

Regulatory Mechanisms
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