Recombinant Human Syntaxin 12/Syntaxin-13 protein (His tag N-Terminus)

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Syntaxin 12 also known as Syntaxin-13 is a member of the SNARE family of proteins. This protein is essential for vesicular transport mediating the fusion of vesicles with target membranes. Syntaxin 12 has a molecular mass of approximately 35 kDa and is predominantly expressed in human tissues with high presence in the brain. It plays an important role in intracellular trafficking processes influencing the localization and transport of cargo molecules within cells.

Biological function summary

Syntaxin 12 serves in the assembly of SNARE complexes which are important for vesicle docking and membrane fusion events. It particularly associates with other SNARE proteins such as VAMPs and SNAPs to form a complex that drives the merging of vesicles with target membranes. This function is vital in processes such as neurotransmitter release and endocytic recycling where precise coordination of vesicular transport is necessary for cellular and neural functions.

Pathways

Syntaxin 12 actively participates in key intracellular trafficking pathways. It is significantly involved in endocytic recycling and phagocytosis pathways ensuring the proper routing and recycling of receptors and other membrane components. In these pathways Syntaxin 12 interacts with proteins such as SNX27 and small GTPases like Rab proteins which modulate vesicular transport activities. Its function in these pathways highlights its importance for maintaining cellular homeostasis and proper cell communication.

Syntaxin 12 has been linked with neurodegenerative diseases particularly Alzheimer's disease. Abnormal expression or functioning of this protein can disrupt synaptic vesicle trafficking leading to impaired neurotransmission and neural damage. Additionally Syntaxin 12 connections with other proteins such as amyloid precursor protein (APP) suggest its involvement in the pathogenic pathways leading to the accumulation of neurotoxic proteins. Understanding these interactions provides insight into the molecular basis of such neurodegenerative conditions.