Recombinant Proteins

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TRAPPC2 Human

Trafficking Protein Particle Complex 2 Human Recombinant

This product consists of the human TRAPPC2 protein, manufactured in a lab using E. coli bacteria. It is a single chain of 163 amino acids, with a molecular weight of 18.8kDa. The protein is not glycosylated, meaning it does not have sugar molecules attached. For purification and detection purposes, a 23 amino acid His-tag is attached to its N-terminus.
Shipped with Ice Packs
Cat. No.
BT13998
Source
Escherichia Coli.
Appearance
A clear solution that has been sterilized by filtration.

TRAPPC2L Human

Trafficking Protein Particle Complex 2-Like Human Recombinant

This recombinant TRAPPC2L protein is produced in E. coli and consists of a single polypeptide chain of 162 amino acids (amino acids 1-139 of the native protein sequence) with a molecular weight of 18.4 kDa. It includes a 23 amino acid His-tag at the N-terminus to facilitate purification by chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14562
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

TRAPPC3 Human

Trafficking Protein Particle Complex 3 Human Recombinant

Recombinant human TRAPPC3, expressed in E. coli, is a single polypeptide chain comprising 200 amino acids (residues 1-180) with a molecular weight of 22.4 kDa. This protein is fused to a 20 amino acid His-tag at its N-terminus and purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14618
Source
E.coli.
Appearance
A clear, sterile solution.

TRAPPC4 Human

Trafficking Protein Particle Complex 4 Human Recombinant

Recombinant human TRAPPC4, expressed in E. coli, is a non-glycosylated polypeptide chain containing 242 amino acids (residues 1-219) with a molecular weight of 26.7 kDa. It includes a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT14728
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile filtered solution.
Definition and Classification

The Trafficking Protein Particle Complex (TRAPP) is a multi-subunit complex involved in the regulation of vesicular trafficking within cells. It is classified into two main types: TRAPP I and TRAPP II, each with distinct subunit compositions and functions. TRAPP I is primarily involved in the early stages of vesicle formation, while TRAPP II plays a role in later stages, including vesicle tethering and fusion.

Biological Properties

Key Biological Properties: TRAPP complexes are essential for maintaining cellular homeostasis by regulating the transport of proteins and lipids between different cellular compartments. They are highly conserved across species, indicating their fundamental role in cellular processes.

Expression Patterns: TRAPP components are ubiquitously expressed in various tissues, with higher expression levels observed in metabolically active tissues such as the liver, brain, and pancreas.

Tissue Distribution: TRAPP complexes are found in multiple cellular compartments, including the endoplasmic reticulum, Golgi apparatus, and endosomes. Their distribution is crucial for their role in vesicular trafficking.

Biological Functions

Primary Biological Functions: The primary function of TRAPP complexes is to facilitate the transport of vesicles between different cellular compartments. This includes the formation, tethering, and fusion of vesicles, ensuring the proper delivery of cargo molecules.

Role in Immune Responses: TRAPP complexes play a role in the immune response by regulating the trafficking of immune-related proteins and receptors. This ensures the proper functioning of immune cells and the effective recognition and response to pathogens.

Pathogen Recognition: TRAPP complexes are involved in the recognition and processing of pathogen-derived molecules, aiding in the activation of immune responses and the clearance of infections.

Modes of Action
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