SYT13 Human
Description
Molecular Structure
SYT13 is a 46.5 kDa recombinant protein produced in Escherichia coli, comprising 420 amino acids (residues 30–426) with an N-terminal His-tag for purification . Key structural features include:
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Domains: Two cytoplasmic C2 domains (C2A and C2B) and an extracellular N-terminal transmembrane domain .
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Atypical Traits: Unlike classical synaptotagmins (e.g., SYT1/2), SYT13 lacks calcium-dependent membrane interactions and an extracellular N-terminal sequence .
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Post-Translational Modifications: Non-glycosylated, with stability enhanced by Tris-HCl buffer, glycerol, and reducing agents .
Biological Functions
SYT13 regulates intracellular vesicle trafficking and polarization in specialized tissues:
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Pancreatic Development:
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Neuroendocrine Signaling:
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Cancer Progression:
3.1. Pancreatic Morphogenesis
3.2. Oncology
3.3. Neurobiology
Clinical Implications
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Diagnostics: SYT13 overexpression correlates with poor prognosis in CRC and ER+ breast cancer .
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Therapeutics: Targeting SYT13 in CRC models reduces metastasis , while overexpression protects motor neurons in ALS .
Recombinant Production and Applications
Evolutionary and Functional Associations
From the Harmonizome database :
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Pathways: Vesicle docking, lipid binding, cell adhesion.
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Diseases: Colorectal/breast cancer, ALS, spinal muscular atrophy.
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Co-Expressed Genes: FOXA2, NGN3, NKX6-1 (pancreatic development); TP53, BCL2 (apoptosis).
Product Specs
Synaptotagmin XIII, KIAA1427, synaptotagmin-13, sytXIII.
Product Science Overview
Synaptotagmin XIII (SYT13) is a member of the synaptotagmin family, which consists of membrane-trafficking proteins characterized by an N-terminal transmembrane region, a variable linker, and two C-terminal C2 domains (C2A and C2B) . Synaptotagmins play crucial roles in the regulation of neurotransmitter release and hormone secretion.
Synaptotagmin XIII, like other synaptotagmins, has a transmembrane region that anchors it to the membrane, and two C2 domains that are involved in calcium binding and interactions with other proteins . The C2 domains are essential for the protein’s role in exocytosis, where it acts as a calcium sensor to trigger the fusion of synaptic vesicles with the presynaptic membrane .
The human recombinant form of Synaptotagmin XIII is produced in E. coli and is a single, non-glycosylated polypeptide chain containing 420 amino acids (30-426) with a molecular mass of 46.5 kDa . This recombinant protein is often used in research to study its function and interactions in a controlled environment.
Synaptotagmin XIII is involved in the regulation of neurotransmitter release. It acts as a calcium sensor, and upon binding calcium, it triggers the fusion of synaptic vesicles with the presynaptic membrane, leading to the release of neurotransmitters into the synaptic cleft . This process is crucial for the proper functioning of synaptic transmission and communication between neurons.
The recombinant form of Synaptotagmin XIII is used in various research applications to study its biochemical properties, interactions with other proteins, and its role in neurotransmission. Understanding the function of Synaptotagmin XIII can provide insights into the mechanisms of synaptic transmission and potential therapeutic targets for neurological disorders.
