- CITATIONS: 1
|Reactivity||Human, Mouse, Rat|
|Calculated MW||20648 Da|
|Other Names||Prenylated Rab acceptor protein 1, PRA1 family protein 1, RABAC1, PRA1, PRAF1|
|Target/Specificity||A synthetic peptide corresponding to residues near the C-terminus of human PRA1 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||PRA1 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||General Rab protein regulator required for vesicle formation from the Golgi complex. May control vesicle docking and fusion by mediating the action of Rab GTPases to the SNARE complexes. In addition it inhibits the removal of Rab GTPases from the membrane by GDI (By similarity).|
|Cellular Location||Cell membrane; Multi-pass membrane protein. Cytoplasm. Golgi apparatus. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle. Note=According to some authors, it is an integral membrane protein, while others showed that it is cytoplasmic and membrane-associated to Golgi and synaptic vesicles.|
|Tissue Location||Ubiquitous. Strongest expression found in placenta, pituitary gland, kidney, lung and stomach|
Provided below are standard protocols that you may find useful for product applications.
PRA1 (prenylated Rab acceptor) is a general regulator of Rab proteins. It has been shown that PRA1 interacts with Rab proteins and with VAMP2. Therefore PRA1 is probably an important factor for membrane traffic, linking together the function of Rab proteins and SNAREs (1). Human cells contain more than 60 small G proteins of the Rab family, which are localized to the surfaces of distinct membrane compartments and regulate transport vesicle formation, motility, docking and fusion. Prenylated Rabs also occur in the cytosol bound to GDI (guanine nucleotide dissociation inhibitor), which binds to Rabs in their inactive state (2).
1. Bucci C, et al. Biochem Biophys Res Commun 286(4): 815-9, 2001
2. Sivars U, et al. Nature 425: 856-859, 2003
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