Our Anti-Rab 3 rabbit polyclonal primary antibody from PhosphoSolutions is produced in-house. It detects rat Rab 3 and is antigen affinity purified from pooled serum. It is great for use in WB.
Western blot of rat cortical lysate showing specific labeling of the ~27 kDa Rab3 protein.
Rab proteins belong to the Ras small GTPase superfamily. The GTP-binding Rab3 subfamily has 4 known isoforms: 3A, 3B, 3C, and 3D (Schluter et al., 2004). These proteins are expressed in highest concentrations in brain and endocrine tissues and involved in regulated exocytosis of hormones and neurotransmitters (Coppola et al., 2002). Specifically, Rab3’s are thought to play a key role in presynaptic vesicle trafficking and priming (Schluter et al., 2006).
Antigen Affinity Purified from Pooled Serum
Polyclonal
IgG
ELISA, WB
Rabbit
RAB3A
27 kDa
Synthetic peptide corresponding to amino acid residues from the N-terminal region of rat Rab 3, conjugated to keyhole limpet hemocyanin (KLH).
Rat
Rat
Human, Mouse, Non-Human Primate, Xenopus
AB_2492220
Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.
Liquid
Prepared from pooled rabbit serum by affinity purification via chromatography on an affinity column made with the N-terminal peptide used as antigen.
10 mM HEPES (pH 7.5), 150 mM NaCl, 100 µg per ml BSA and 50% glycerol.
WB: 1:1000
WB Brain: 1:1000
Unconjugated
Specific for endogenous levels of the ~27 kDa Rab3 protein.
Western blots performed on each lot.
For research use only. Not intended for therapeutic or diagnostic use. Use of all products is subject to our terms and conditions, which can be viewed on our website.
After date of receipt, stable for at least 1 year at -20°C.
Rab 3A; RAB 3A member RAS oncogene family; Rab3a; RAB3A member RAS oncogene family; RAB3A_HUMAN; RAS associated protein RAB 3A; RAS associated protein RAB3A; Ras related protein Rab 3A; Ras related protein Rab3A; Ras-related protein Rab-3A
P63012
UniProt Summary: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (PubMed:2501306). Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different sets of downstream effectors directly responsible for vesicle formation, movement, tethering and fusion (PubMed:2501306). RAB3A plays a central role in regulated exocytosis and secretion. Controls the recruitment, tethering and docking of secretory vesicles to the plasma membrane (PubMed:2501306). Upon stimulation, switches to its active GTP-bound form, cycles to vesicles and recruits effectors such as RIMS1, RIMS2, Rabphilin-3A/RPH3A, RPH3AL or SYTL4 to help the docking of vesicules onto the plasma membrane (By similarity). Upon GTP hydrolysis by GTPase-activating protein, dissociates from the vesicle membrane allowing the exocytosis to proceed (By similarity). Stimulates insulin secretion through interaction with RIMS2 or RPH3AL effectors in pancreatic beta cells (By similarity). Regulates calcium-dependent lysosome exocytosis and plasma membrane repair (PMR) via the interaction with 2 effectors, SYTL4 and myosin-9/MYH9 (PubMed:27325790). Acts as a positive regulator of acrosome content secretion in sperm cells by interacting with RIMS1 (PubMed:22248876, PubMed:30599141). Also plays a role in the regulation of dopamine release by interacting with synaptotagmin I/SYT (By similarity). {ECO:0000250|UniProtKB:P63011, ECO:0000250|UniProtKB:P63012, ECO:0000269|PubMed:22248876, ECO:0000269|PubMed:2501306, ECO:0000269|PubMed:27325790, ECO:0000269|PubMed:30599141}.
Schlüter, O.M., Schmitz, F., Jahn, R., Rosenmund, C. and Südhof, T.C., 2004. A complete genetic analysis of neuronal Rab3 function. Journal of Neuroscience, 24(29), pp.6629-6637. PMID: 15269275
Schlüter, O.M., Basu, J., Südhof, T.C. and Rosenmund, C., 2006. Rab3 superprimes synaptic vesicles for release: implications for short-term synaptic plasticity. Journal of Neuroscience, 26(4), pp.1239-1246. PMID: 16436611
Coppola, T., Perret-Menoud, V., Gattesco, S., Magnin, S., Pombo, I., Blank, U. and Regazzi, R., 2002. The death domain of Rab3 guanine nucleotide exchange protein in GDP/GTP exchange activity in living cells. Biochemical Journal, 362(2), pp.273-279. PMID: 11853534
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