Recombinant Rat Ras-related protein Rab-3A (Rab3a)

Code CSB-YP019194RA
MSDS
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Source Yeast
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Code CSB-EP019194RA
MSDS
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Source E.coli
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Code CSB-EP019194RA-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP019194RA
MSDS
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Source Baculovirus
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Code CSB-MP019194RA
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Uniprot No.
Alternative Names
Rab3a; Ras-related protein Rab-3A
Species
Rattus norvegicus (Rat)
Expression Region
1-220
Target Protein Sequence
MASATDSRYG QKESSDQNFD YMFKILIIGN SSVGKTSFLF RYADDSFTPA FVSTVGIDFK VKTIYRNDKR IKLQIWDTAG QERYRTITTA YYRGAMGFIL MYDITNEESF NAVQDWSTQI KTYSWDNAQV LLVGNKCDME DERVVSSERG RQLADHLGFE FFEASAKDNI NVKQTFERLV DVICEKMSES LDTADPAVTG AKQGPQLTDQ QAPPHQDCAC
Protein Length
Full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Small GTP-binding protein that plays a central role in regulated exocytosis and secretion. Controls the recruitment, tethering and docking of secretory vesicles to the plasma membrane. 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. Upon GTP hydrolysis by GTPase-activating protein, dissociates from the vesicle membrane allowing the exocytosis to proceed. Stimulates insulin secretion through interaction with RIMS2 and RPH3AL effectors in pancreatic beta cells. Regulates calcium-dependent lysosome exocytosis and plasma membrane repair (PMR) via the interaction with 2 effectors, SYTL4 and myosin-9/MYH9. Acts as a positive regulator of acrosome content secretion in sperm cells by interacting with RIMS1. Plays a role in the regulation of dopamine release by interacting with synaptotagmin I/SYT. Interacts with MADD (via uDENN domain); the GTP-bound form is preferred for interaction.
Gene References into Functions
  1. analysis of crystal structures and biochemical analyses of Rabphilin-3A C2B-SNAP25 and C2B-phosphatidylinositol 4,5-bisphosphate (PIP2) complexes, revealing how Rabphilin-3A C2 domains operate in cooperation with PIP2/Ca(2+) and SNAP25 to bind the plasma membrane, adopting a conformation compatible to interact with the complete SNARE complex PMID: 28634303
  2. This work has shed new light on the molecular mechanism for Rab3 and synaptotamin regulation of neurotransmitter release. PMID: 28370453
  3. Rab3A-binding site on C2A domain of synaptotagmin I PMID: 28057568
  4. discovery of the involvement of Rab3 and Noc2 in an insulin-regulated step in GLUT4 translocation suggests that the control of this translocation process is unexpectedly similar to regulated secretion and particularly pancreatic insulin-vesicle release. PMID: 26024738
  5. Rab3A has been found to be a novel interacting protein of synaptotagmin I. Rab3A binds to synaptotagmin I in a Ca2+-independent manner. PMID: 24472545
  6. the Rab3A cycle is coupled with the activation of Munc13-1 via RIM, which accounts for the regulation of secretion by Rab3A. PMID: 21689256
  7. Myo5a and Rab3A are direct binding partners and interact on synaptic vesicles and the Myo5a/Rab3A complex is involved in transport of neuronal vesicles PMID: 21349835
  8. Selective modulation of the GTP/GDP switch mechanism of Rab27b impairs synaptic vesicle recycling and suggests that Rab27b, in concert with Rab3a, is involved in synaptic vesicle exocytosis. PMID: 20926670
  9. Localization of the small monomeric GTPases Rab3D and Rab3A in the AtT-20 rat pituitary cell line. PMID: 11846002
  10. role for Ca(2+)/CaM in modulating both the binding of guanine nucleotides to Rab3A and the GTPase activity of Rab3A PMID: 11879192
  11. binds to granuphilin and controls exocytosis of pancreatic beta cells PMID: 12058058
  12. Rabphilin-3A and Rab3A are present in normal mouse, rat, and human kidneys, with an exclusively glomerular expression and a comma-like pattern of positivity along the glomerular capillary wall, suggestive for podocyte staining. PMID: 12937130
  13. The combination of Growth Inhibitory Factor with Rab3A could significantly enhance the survival of the hippocampal neurons, suggesting that GIF may inhibit Zn(2+)-induced neuronal death via its interaction with Rab3A. PMID: 15039103
  14. We propose that while Rab3a preferentially associates with recycling synaptic vesicles and modulates their trafficking, Rab5a is largely excluded from recycling vesicles. PMID: 16141272
  15. Rab3A-interacting molecule RIM regulates the presynaptic recruitment of Munc13-1 and ubMunc13-2 PMID: 16704978
  16. Rab3A, but not Rab3B, enhances secretory output from rat melanotrophs and that their function is not redundant. PMID: 16822953
  17. In neurons GTP hydrolysis and rabphilin are involved in Rab3A dissociation from the vesicles and the occurrence of exocytosis. PMID: 17149709
  18. Young secretory granules have a higher capacity for binding Rab3A and Rab27A is functionally important for preferential exocytosis from these granules. PMID: 17311845
  19. The results of this study indicated widespread distribution of RIM3gamma in diverse CNS neuronal cell types. The mRNA was found mainly in the cell bodies, the protein was localized chiefly to neuronal dendrites and to the postsynaptic densities. PMID: 17534942
  20. Rab3a specifically stimulates morphological differentiation of mature oligodendrocytes PMID: 18798275
  21. FLJ13130 is a novel type of Rab-GAP that exhibits broad GAP specificity and inactivates several distinct Rab isoforms, including Rab3A, just near the plasma membrane. PMID: 19077034

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Subcellular Location
Cytoplasm, cytosol. Lysosome. Cytoplasmic vesicle, secretory vesicle. Cell projection, axon. Cell membrane; Lipid-anchor; Cytoplasmic side.
Protein Families
Small GTPase superfamily, Rab family
Tissue Specificity
Detected in brain.
Database Links
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