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07-794
Sigma-AldrichAnti-Rab13 Antibody
Detect Rab13 using this Anti-Rab13 Antibody validated for use in WB, IP & IF.
More>>Detect Rab13 using this Anti-Rab13 Antibody validated for use in WB, IP & IF. Less<<
Anti-Rab13 Antibody: SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
Rab proteins are members of the Ras superfamily of small G-Proteins. At least 60 isoforms have been identified. These GTPases are primarily involved in vesicle trafficking and it is believed that a different Rab protein may be needed for each step of the vesicular transport. It is thought Rab4 and Rab11 are involved in internalization, sorting, and transport to lysosomes or recycling, of several membrane proteins, including GPCRs, GLUT-4, Aquaporin-2, or the H+/K+ ATPase.
References
Product Information
Format
Affinity Purified
Control
PC12 Cell Lysate
Presentation
Affinity Purified rabbit IgG in storage buffer containing tri-citrate-phosphate, pH 7-8 and 0.1% sodium azide.
FUNCTION: Could participate in polarized transport, in the assembly and/or the activity of tight junctions. SIZE: 203 amino acids; 22,774 Da SUBCELLULAR LOCATION:Cell junction › tight junction. Cell membrane; Lipid-anchor; Cytoplasmic side. Cytoplasmic vesicle membrane; Lipid-anchor; Cytoplasmic side. Note= Cytoplasmic tight junctions or associated with vesicles scattered throughout the cytoplasm in cells lacking tight junctions. TISSUE SPECIFICITY: Detected in several types of epithelia, including intestine, kidney, liver and in endothelial cells. SIMILARITY: Belongs to the small GTPase superfamily. Rab family.
Molecular Weight
25 kDa
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Western Blot Analysis: This lot detected Rab13 at 1:1,000 (1g/mL) dilution in lysates from PC12 lysate resolved via SDS-PAGE and transferred to PVDF (Immobilon-P).
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 2-8°C from date of receipt. Handling Recommendations: Upon receipt, and prior to removing the cap, centrifuge the vial and gently mix the solution. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
In vivo and in vitro characterization of novel neuronal plasticity factors identified following spinal cord injury. Di Giovanni, Simone, et al. J. Biol. Chem., 280: 2084-91 (2005)
2004
During epithelial morphogenesis, adherens junctions (AJs) and tight junctions (TJs) undergo dynamic reorganization, whereas epithelial polarity is transiently lost and reestablished. Although ARF6-mediated endocytic recycling of E-cadherin has been characterized and implicated in the rapid remodeling of AJs, the molecular basis for the dynamic rearrangement of TJs remains elusive. Occludin and claudins are integral membrane proteins comprising TJ strands and are thought to be responsible for establishing and maintaining epithelial polarity. Here we investigated the intracellular transport of occludin and claudins to and from the cell surface. Using cell surface biotinylation and immunofluorescence, we found that a pool of occludin was continuously endocytosed and recycled back to the cell surface in both fibroblastic baby hamster kidney cells and epithelial MTD-1A cells. Biochemical endocytosis and recycling assays revealed that a Rab13 dominant active mutant (Rab13 Q67L) inhibited the postendocytic recycling of occludin, but not that of transferrin receptor and polymeric immunoglobulin receptor in MTD-1A cells. Double immunolabelings showed that a fraction of endocytosed occludin was colocalized with Rab13 in MTD-1A cells. These results suggest that Rab13 specifically mediates the continuous endocytic recycling of occludin to the cell surface in both fibroblastic and epithelial cells.
The GTPase Rab13 regulates the assembly of functional epithelial tight junctions (TJs) through a yet unknown mechanism. Here, we show that expression of the GTP-bound form of Rab13 inhibits PKA-dependent phosphorylation and TJ recruitment of the vasodilator-stimulated phosphoprotein, an actin remodelling protein. We demonstrate that Rab13GTP directly binds to PKA and inhibits its activity. Interestingly, activation of PKA abrogates the inhibitory effect of Rab13 on the recruitment of vasodilator-stimulated phosphoprotein, ZO-1, and claudin1 to cell-cell junctions. Rab13 is, therefore, the first GTPase that controls PKA activity and provides an unexpected link between PKA signaling and the dynamics of TJ assembly.
