Key Spec Table
|Species Reactivity||Key Applications||Host||Format||Antibody Type|
|Ca, Ch, H, M, Mk, R||IF, WB||M||Affinity Purified||Monoclonal Antibody|
|Description||Anti-Rab11 Antibody, clone 47|
|Safety Information according to GHS|
|Storage and Shipping Information|
|Storage Conditions||1 year at -20°C from date of shipment|
|Material Size||100 µg|
|Anti-Rab11, clone 47 (mouse monoclonal IgG2a) - 2196737||2196737|
|Anti-Rab11, clone 47 - 2011576||2011576|
|Anti-Rab11, clone 47 - 27149||27149|
|Anti-Rab11, clone 47 - DAM1598785||DAM1598785|
|Anti-Rab11, clone 47 - DAM1614912||DAM1614912|
|Anti-Rab11, clone 47 - DAM1661047||DAM1661047|
|Anti-Rab11, clone 47 - DAM1734759||DAM1734759|
|Anti-Rab11, clone 47 - DAM1776426||DAM1776426|
|Anti-Rab11, clone 47 - JBC1363104||JBC1363104|
|Anti-Rab11, clone 47 - JBC1839877||JBC1839877|
|Reference overview||Application||Pub Med ID|
|Prolonged morphine treatment alters δ opioid receptor post-internalization trafficking.|
Ong, EW; Xue, L; Olmstead, MC; Cahill, CM
British journal of pharmacology 172 615-29 2015
The δ opioid receptor (DOP receptor) undergoes internalization both constitutively and in response to agonists. Previous work has shown that DOP receptors traffic from intracellular compartments to neuronal cell membranes following prolonged morphine treatment. Here, we examined the effects of prolonged morphine treatment on the post-internalization trafficking of DOP receptors.Using primary cultures of dorsal root ganglia neurons, we measured the co-localization of endogenous DOP receptors with post-endocytic compartments following both prolonged and acute agonist treatments.A departure from the constitutive trafficking pathway was observed following acute DOP receptor agonist-induced internalization by deltorphin II. That is, the DOP receptor underwent distinct agonist-induced post-endocytic sorting. Following prolonged morphine treatment, constitutive DOP receptor trafficking was augmented. SNC80 following prolonged morphine treatment also caused non-constitutive DOP receptor agonist-induced post-endocytic sorting. The μ opioid receptor (MOP receptor) agonist DAMGO induced DOP receptor internalization and trafficking following prolonged morphine treatment. Finally, all of the alterations to DOP receptor trafficking induced by both DOP and MOP receptor agonists were inhibited or absent when those agonists were co-administered with a DOP receptor antagonist, SDM-25N.The results support the hypothesis that prolonged morphine treatment induces the formation of MOP-DOP receptor interactions and subsequent augmentation of the available cell surface DOP receptors, at least some of which are in the form of a MOP/DOP receptor species. The pharmacology and trafficking of this species appear to be unique compared to those of its individual constituents.This article is part of a themed section on Opioids: New Pathways to Functional Selectivity. To view the other articles in this section visit http://dx.doi.org/10.1111/bph.2015.172.issue-2.
|Secretion of soluble vascular endothelial growth factor receptor 1 (sVEGFR1/sFlt1) requires Arf1, Arf6, and Rab11 GTPases.|
Jung, JJ; Tiwari, A; Inamdar, SM; Thomas, CP; Goel, A; Choudhury, A
PloS one 7 e44572 2012
The soluble form of vascular endothelial growth factor receptor 1 (sVEGFR-1/sFlt1) is generated by alternative splicing of the FLT1 gene. Secretion of sFlt1 from endothelial cells plays an important role in blood vessel sprouting and morphogenesis. However, excess sFlt1 secretion is associated with diseases such as preeclampsia and chronic kidney disease. To date, the secretory transport process involved in the secretion of sFlt1 is poorly understood. In the present study, we investigated the itinerary of sFlt1 trafficking along the secretory pathway. To understand the timecourse of sFlt1 secretion, endothelial cells stably expressing sFlt1 were metabolically radiolabeled with [(35)S]-methionine and cysteine. Our results indicate that after initial synthesis the levels of secreted [(35)S]-sFlt1 in the extracellular medium peaks at 8 hours. Treatment with brefeldin A (BFA), a drug which blocks trafficking between the endoplasmic reticulum (ER) and the Golgi complex, inhibited extracellular release of sFlt1 suggesting that ER to Golgi and intra-Golgi trafficking of sFlt1 are essential for its secretion. Furthermore, we show that ectopic expression of dominant-negative mutant forms of Arf1, Arf6, and Rab11 as well as siRNA-mediated knockdown of these GTPases block secretion of sFlt1 during normoxic and hypoxic conditions suggesting role for these small GTPases. This work is the first to report role of regulatory proteins involved in sFlt1 trafficking along the secretory pathway and may provide insights and new molecular targets for the modulation of sFlt-1 release during physiological and pathological conditions.
|Molecular characterization of Rab11 interactions with members of the family of Rab11-interacting proteins.|
Junutula, Jagath R, et al.
J. Biol. Chem., 279: 33430-7 (2004) 2004
The Rab11 subfamily of GTPases plays an important role in vesicle trafficking from endosomes to the plasma membrane. At least six Rab11 effectors (family of Rab11-interacting proteins (FIPs)) have been shown to interact with Rab11 and are hypothesized to regulate various membrane trafficking pathways such as transferrin recycling, cytokinesis, and epidermal growth factor trafficking. In this study, we characterized interactions of FIPs with the Rab11 GTPase using isothermal titration calorimetric studies and mutational analysis. Our data suggest that FIPs cannot differentiate between GTP-bound Rab11a and Rab11b in vitro (50-100 nm affinity) and in vivo. We also show that, although FIPs interact with the GDP-bound form of Rab11 in vitro, the binding affinity (>1000 nm) is not sufficient for FIP and GDP-bound Rab11 interactions to occur in vivo. Mutational analysis revealed that both the conserved hydrophobic patch and Tyr628 are important for the GTP-dependent binding of Rab11 to FIPs. The entropy and enthalpy analyses suggest that binding to Rab11a/b may induce conformational changes in FIPs.
|Regulation of G protein-coupled receptor endocytosis and trafficking by Rab GTPases.|
Seachrist, Jennifer L and Ferguson, Stephen S G
Life Sci., 74: 225-35 (2003) 2003
G protein-coupled receptors (GPCRs) are integral membrane proteins that, in response to activation by extracellular stimuli, regulate intracellular second messenger levels via their coupling to heterotrimeric G proteins. GPCR activation also initiates a series of molecular events that leads to G protein-coupled receptor kinase-mediated receptor phosphorylation and the binding of beta-arrestin proteins to the intracellular face of the receptor. beta-Arrestin binding not only contributes to the G protein-uncoupling of GPCRs, but also mediates the targeting of many GPCRs for endocytosis in clathrin-coated pits. Several GPCRs internalize as a stable complex with beta-arrestin and the stability of this complex appears to regulate, at least in part, whether the receptors are dephosphorylated in early endosomes and recycled back to the cell surface as fully functional receptors, retained in early endosomes or targeted for degradation in lysosomes. More recently, it has become appreciated that the movement of GPCRs through functionally distinct intracellular membrane compartments is regulated by a variety of Rab GTPases and that the activity of these Rab GTPases may influence GPCR function. Moreover, it appears that GPCRs are not simply passive cargo molecules, but that GPCR activation may directly influence Rab GTPase activity and as such, GPCRs may directly control their own targeting between intracellular compartments. This review provides a synopsis of the current knowledge regarding the role of beta-arrestins and Rab GTPases in regulating the intracellular trafficking and function of GPCRs.
|Regulation of G-protein-coupled receptor activity by rab GTPases.|
Rosenfeld, Jennifer L, et al.
Recept. Channels, 8: 87-97 (2002) 2002
The regulation of G-protein-coupled receptor (GPCR) activity involves a diversity of vesicular transport processes. Receptor desensitization and resensitization are intimately connected with membrane trafficking events such as endocytosis, intracellular sorting, transport to lysosomes, and recycling to the plasma membrane. Ras-related GTPases of the rab family are known to regulate these processes, including a subset of rab proteins that are specific for endosomes and lysosomes. While much study has been given to endocytic rabs using standard models such as transferrin receptors, less is known about how rabs regulate signal-transducing receptors. This article reviews recent work concerning rab GTPases and their regulation of GPCR activity via membrane transport mechanisms.
|Paxillin associates with poly(A)-binding protein 1 at the dense endoplasmic reticulum and the leading edge of migrating cells.|
Woods, Alison J, et al.
J. Biol. Chem., 277: 6428-37 (2002) 2002
Using mass spectrometry we have identified proteins which co-immunoprecipitate with paxillin, an adaptor protein implicated in the integrin-mediated signaling pathways of cell motility. A major component of paxillin immunoprecipitates was poly(A)-binding protein 1, a 70-kDa mRNA-binding protein. Poly(A)-binding protein 1 associated with both the alpha and beta isoforms of paxillin, and this was unaffected by RNase treatment consistent with a protein-protein interaction. The NH(2)-terminal region of paxillin (residues 54-313) associated directly with poly(A)-binding protein 1 in cell lysates, and with His-poly(A)-binding protein 1 immobilized in microtiter wells. Binding was specific, saturable and of high affinity (K(d) of approximately 10 nm). Cell fractionation studies showed that at steady state, the bulk of paxillin and poly(A)-binding protein 1 was present in the "dense" polyribosome-associated endoplasmic reticulum. However, inhibition of nuclear export with leptomycin B caused paxillin and poly(A)-binding protein 1 to accumulate in the nucleus, indicating that they shuttle between the nuclear and cytoplasmic compartments. When cells migrate, poly(A)-binding protein 1 colocalized with paxillin-beta at the tips of lamellipodia. Our results suggest a new mechanism whereby a paxillin x poly(A)-binding protein 1 complex facilitates transport of mRNA from the nucleus to sites of protein synthesis at the endoplasmic reticulum and the leading lamella during cell migration.
|Modulation of receptor cycling by neuron-enriched endosomal protein of 21 kD|
Steiner, P., et al
J Cell Biol, 157:1197-209 (2002) 2002
|Immunoblotting (Western), Immunofluorescence||12070131|
|Rab proteins mediate Golgi transport of caveola-internalized glycosphingolipids and correct lipid trafficking in Niemann-Pick C cells.|
Choudhury, Amit, et al.
J. Clin. Invest., 109: 1541-50 (2002) 2002
We recently showed that human skin fibroblasts internalize fluorescent analogues of the glycosphingolipids lactosylceramide and globoside almost exclusively by a clathrin-independent mechanism involving caveolae. In contrast, a sphingomyelin analogue is internalized approximately equally via clathrin-dependent and caveolar routes. Here, we further characterized the caveolar pathway for glycosphingolipids, showing that Golgi targeting of sphingolipids internalized via caveolae required microtubules and phosphoinositol 3-kinases and was inhibited in cells expressing dominant-negative Rab7 and Rab9 constructs. In addition, overexpression of wild-type Rab7 or Rab9 (but not Rab11) in Niemann-Pick type C (NP-C) lipid storage disease fibroblasts resulted in correction of lipid trafficking defects, including restoration of Golgi targeting of fluorescent lactosylceramide and endogenous GM(1) ganglioside, and a dramatic reduction in intracellular cholesterol stores. Our results demonstrate a role for Rab7 and Rab9 in the Golgi targeting of glycosphingolipids and suggest a new therapeutic approach for restoring normal lipid trafficking in NP-C cells.
|Regulation of membrane transport through the endocytic pathway by rabGTPases.|
Mohrmann, K and van der Sluijs, P
Mol. Membr. Biol., 16: 81-7 (1999) 1999
Small GTP binding proteins of the rab family are associated with the cytoplasmic surface of compartments of the central vacuolar system. Several of them, including rab5, rab4 and rab11, are localized to early endocytic organelles where they regulate distinct events in the transferrin receptor pathway. Whereas rab5 is controlling transport to early endosomes, rab4 and rab11 are involved in the regulation of recycling back to the plasma membrane. How GTP-hydrolysis of rab bound GTP is related to the role of these proteins in endocytosis is not yet known, but quick progress is being made towards this goal through the identification of proteins regulating the activity of these rab proteins.