RAB4A, Member RAS Oncogene Family (RAB4A) (C-Term) antibody

Details for Product No. ABIN361840
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Synonyms rab4a, MGC52945, fc93b03, wu:fc93b03, RAB4A, HRES-1/RAB4, RAB4, AI848268, Rab4
(8), (6), (5), (2), (1), (1), (1)
Human, Mouse (Murine), Rat (Rattus)
(52), (18), (18), (3)
(30), (20), (2)
(2), (2), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Western Blotting (WB), Immunofluorescence (IF)
(39), (20), (10), (7), (6), (6), (3), (2), (2), (2), (1), (1), (1), (1)
Pubmed 7 references available
Quantity 25 μL
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Catalog No. ABIN361840
190.30 $
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Immunogen C-terminal peptide from human Rab4
Isotype IgG
Specificity Detects approx. 26 kDa.
Alternative Name Rab4
Background Synonyms:
Oncogene Rab4, Rab4A, Ras related protein
Rab4 is a 25 kDa member of the Rab family of small guanosine triphosphatases (GTPases), Ras superfamily. Rab GTPases are central regulators of membrane trafficking in the eukaryotic cell. Their regulatory capacity depends on their ability to cycle between the GDP -bound inactive and GTP-bound active states. This conversion is regulated by GDP/GTP exchange factors (GEPs), GDP dissociation inhibitors (GDIs) and GTPase-activating proteins (GAPs). Activation of a Rab protein is coupled to its association with intracellular membranes, allowing it to recruit downstream effector proteins to the cytoplasmic surface of a sub-cellular compartment. Through these proteins, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion. Rab proteins contain conserved regions involved in guanine-nucleotide binding, and hyper-variable COHO-terminal domains with a cysteine motif implicated in sub-cellular targeting. Post-translational modification of the cysteine motif with one or two geranylgeranyl groups is essential for the membrane association and correct intracellularlocalization of Rab proteins. Each Rab shows a characteristic sub-cellular distribution.In particular, over-expression of Rab4 causes a redistribution of receptors on plasma membrane versus endocytic compartments. The presence of excessive Rab4 leads to the accumulation of tranferrin receptors in non-acidic, post-endosomal recycling vesicles considered an intermediate compartment between endosomes and plasma membranes. Rab4 also plays a role in the translocation of glucose transporter (Glu4) in adipocytes in response to insulin. Mediating the association of Rab4 with transferring receptor-containing early endosomes takes place through the geranylgeranyl groups at its carboxyl-terminus. Membrane association is also cell cycle dependent, as phosphorylation at its c-terminal cdc2 kinase consensus sequence in mitotic cells leads to dissociation of Rab4 into the cytosol.
Gene ID 5867
NCBI Accession NP_004569
UniProt P20338
Research Area Cancer, Organelles, Signaling, Cell Signaling, Neurology
Application Notes Recommended Dilution: 1:1000-2000 (WB)
Restrictions For Research Use only
Format Liquid
Storage -20 °C
Supplier Images
anti-RAB4A, Member RAS Oncogene Family (RAB4A) (C-Term) antibody Rab4, Hela
Background publications Ali, Wasmeier, Lamoreux et al.: "Multiple regions contribute to membrane targeting of Rab GTPases." in: Journal of cell science, Vol. 117, Issue Pt 26, pp. 6401-12, 2004 (PubMed).

Zerial, McBride: "Rab proteins as membrane organizers." in: Nature reviews. Molecular cell biology, Vol. 2, Issue 2, pp. 107-17, 2001 (PubMed).

Ayad, Hull, Mellman: "Mitotic phosphorylation of rab4 prevents binding to a specific receptor on endosome membranes." in: The EMBO journal, Vol. 16, Issue 15, pp. 4497-507, 1997 (PubMed).

Cormont, Bortoluzzi, Gautier et al.: "Potential role of Rab4 in the regulation of subcellular localization of Glut4 in adipocytes." in: Molecular and cellular biology, Vol. 16, Issue 12, pp. 6879-86, 1997 (PubMed).

van der Sluijs, Hull, Huber et al.: "Reversible phosphorylation--dephosphorylation determines the localization of rab4 during the cell cycle." in: The EMBO journal, Vol. 11, Issue 12, pp. 4379-89, 1992 (PubMed).

General Stenmark, Olkkonen: "The Rab GTPase family." in: Genome biology, Vol. 2, Issue 5, pp. REVIEWS3007, 2001 (PubMed).

Takai, Sasaki, Matozaki: "Small GTP-binding proteins." in: Physiological reviews, Vol. 81, Issue 1, pp. 153-208, 2001 (PubMed).

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