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ABS1026
Sigma-AldrichAnti-Rab27B Antibody
This Anti-Rab27B Antibody is validated for use in Western Blotting and Immunoprecipitation and Immunohistochemistry for the detection of Rab27B.
More>>This Anti-Rab27B Antibody is validated for use in Western Blotting and Immunoprecipitation and Immunohistochemistry for the detection of Rab27B. Less<<
Anti-Rab27B Antibody: SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
RAB27B, also known as C25KG, is a member of the Rab GTPase superfamily. RAB27B acts as a lipid anchoring protein that is prenylated and works in vesicular fusion and protein trafficking within cells. The protein is most highly expressed in testis but can be expressed in other cell types as well. Because Rab27B is widely expressed in various tissues together with Rab27A and RAB27B has been found to have the ability to bind all of the Rab27A effectors that have been tested, Rab27A and Rab27B were initially thought to function redundantly by sharing common Rab27 effectors. However, recent evidence has indicated that by interacting with different Rab27 effectors Rab27A and Rab27B play different roles in special types of secretion (e.g. exosome secretion and mast cell secretion) even within the same cell type. Rab27B is particularly important for regulating protein secretion by pancreatic acinar cells, for instance.
This Anti-Rab27B Antibody is validated for use in Western Blotting and Immunoprecipitation and Immunohistochemistry for the detection of Rab27B.
Key Applications
Western Blotting
Immunoprecipitation
Immunohistochemistry
Application Notes
Western Blotting Analysis: A 1:1,000 dilution from a representative lot detected Rab27B in 10 µg of C2C12, mouse brain, and PC3 lysate. Western Blotting Analysis: A representative lot detected Rab27B in rat parotid gland lysate (Imai, A., et al. (2004). Journal of Cell Science. 117:1945-1953). Immunoprecipitation Analysis: A representative lot immunoprecipitated Rab27B in flg-Rab27B (Imai, A., et al. (2004). Journal of Cell Science. 117:1945-1953). Immunohistochemistry Analysis: A representative lot detected Rab27B in rat parotid acinar cells (Imai, A., et al. (2004). Journal of Cell Science. 117:1945-1953).
Biological Information
Immunogen
GST-tagged recombinant protein corresponding to human Rab27B.
~27 kDa observed. Uncharacterized band(s) may appear in some lysates.
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Evaluated by Western Blotting in mouse brain tissue lysate.
Western Blotting Analysis: A 1:1,000 dilution of this antibody detected Rab27B in 10 µg of mouse brain tissue lysate.
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Stable for 1 year at -20°C from date of receipt. Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
Small GTPase Rab is a large family of putative membrane trafficking proteins, and each member is thought to regulate a specific type(s) of membrane trafficking. However, little is known about the involvement of Rab protein(s) in secretory granule exocytosis in exocrine cells or the molecular mechanism underlying this process. We show that Rab27B, a closely related isoform of Rab27A that regulates lysosome-related granule exocytosis in cytotoxic T lymphocytes, is abundantly expressed on amylase-containing secretory granules in rat parotid gland acinar cells. We also identify the putative Rab27B effector protein, Slac2-c (Slp homologue lacking C2 domains-c)/MyRIP, which was originally described as a myosin Va/VIIa and actin binding protein, in rat parotid glands. The results of subcellular fractionation, immunoprecipitation and immunohistochemical studies indicate that the Rab27B-Slac2-c complex is formed on secretory granules in vivo. The introduction of either a specific Rab27 binding domain (i.e. a recombinant Slp homology domain of Slac2-b that specifically binds Rab27A/B but not other Rabs) or functionally blocking antibodies that specifically disrupt Rab27B-Slac2-c complex in vitro strongly inhibited isoproterenol-stimulated amylase release from streptolysin O-permeabilized parotid acinar cells. Our results indicate that the Rab27B-Slac2-c complex is an important constituent of secretory granule exocytosis in parotid acinar cells.