Recombinant Proteins

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SYT5 Human

Synaptotagmin V Human Recombinant

Recombinant human SYT5, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 301 amino acids (109-386aa). It has a molecular mass of 33.6kDa. A 23 amino acid His-tag is fused to the N-terminus of SYT5, and the protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6991
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

SYT1 Human

Synaptotagmin I Human Recombinant

Produced in E. coli, this non-glycosylated SYT1 polypeptide comprises amino acids 136-382, resulting in a 29.5 kDa protein. An 8-amino acid His-tag is fused to the C-terminus to facilitate purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6594
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

SYT11 Human

Synaptotagmin XI Human Recombinant

This product consists of a single, non-glycosylated polypeptide chain of the human SYT11 protein, containing 418 amino acids (residues 37-431) with a molecular weight of 47kDa. It is produced through recombinant expression in E. coli. The protein includes a 23 amino acid His-tag at the N-terminus to facilitate purification, which is carried out using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT6717
Source
E.coli.
Appearance
The product appears as a clear, colorless solution that has been sterilized through filtration.

SYT13 Human

Synaptotagmin XIII Human Recombinant

Recombinant human SYT13, expressed in E. coli, is a single, non-glycosylated polypeptide chain comprising 420 amino acids (residues 30-426). It has a molecular weight of 46.5 kDa. The protein is fused to a 23 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6797
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

SYT3 Human

Synaptotagmin III Human Recombinant

Recombinantly produced in E.coli, SYT3 Human is a single, non-glycosylated polypeptide chain. It comprises 540 amino acids (76-590) and has a molecular weight of 57.7 kDa. The protein includes a 25 amino acid His-tag at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6839
Source
Escherichia Coli.
Appearance
A clear solution that has undergone sterile filtration.

SYT4 Human

Synaptotagmin IV Human Recombinant

Recombinant human SYT4, expressed in E. coli, is a non-glycosylated polypeptide chain consisting of 409 amino acids (residues 38-425). With a molecular weight of 46.1 kDa, this protein is engineered with a 21 amino acid His-tag at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT6906
Source
E.coli.
Appearance
Clear, colorless, and sterile-filtered solution.
Definition and Classification

Synaptotagmins (SYTs) are a family of membrane-trafficking proteins characterized by an N-terminal transmembrane region, a variable linker, and two C-terminal C2 domains (C2A and C2B) . There are 17 isoforms in the mammalian synaptotagmin family . These proteins play a crucial role in the regulation of neurotransmitter release and hormone secretion .

Biological Properties

Key Biological Properties: Synaptotagmins are known for their role as calcium sensors in the regulation of neurotransmitter release . They have a high degree of homology in the C2 domains, although not all synaptotagmins bind to calcium .

Expression Patterns and Tissue Distribution: Synaptotagmins are widely distributed in the brain and endocrine tissues . For example, synaptotagmin-1 is localized to synaptic vesicles in the pre-synaptic axon terminal .

Biological Functions

Primary Biological Functions: Synaptotagmins function as calcium sensors that regulate neurotransmitter release and hormone secretion . They are involved in early synaptic vesicle docking to the presynaptic membrane and late steps of calcium-evoked synaptic vesicle fusion .

Role in Immune Responses and Pathogen Recognition: While synaptotagmins are primarily known for their role in neurotransmission, they may also play a role in immune responses and pathogen recognition, although this area requires further research.

Modes of Action

Mechanisms with Other Molecules and Cells: Synaptotagmins interact with various molecules such as β-neurexin and SNAP-25 . Calcium-binding alters the protein-protein interactions of synaptotagmin, increasing its affinity for syntaxin .

Binding Partners and Downstream Signaling Cascades: Synaptotagmins bind to phosphatidylinositol bisphosphate (PIP2) in the presence of calcium ions, suggesting a role in lipid signaling .

Regulatory Mechanisms

Regulatory Mechanisms: The expression and activity of synaptotagmins are regulated through various mechanisms, including transcriptional regulation and post-translational modifications . For instance, synaptotagmin-1 undergoes phase separation to regulate its calcium-sensitive oligomerization .

Applications

Biomedical Research: Synaptotagmins are extensively studied in the context of neurotransmission and synaptic vesicle exocytosis .

Diagnostic Tools and Therapeutic Strategies: Synaptotagmins have potential applications in developing diagnostic tools and therapeutic strategies for neurological disorders .

Role in the Life Cycle

Role Throughout the Life Cycle: Synaptotagmins play a crucial role throughout the life cycle, from development to aging and disease . They are involved in synaptic plasticity, which is essential for learning and memory .

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