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

Details for Product No. ABIN361841, Supplier: Log in to see
Antigen
  • rab4a
  • MGC52945
  • fc93b03
  • wu:fc93b03
  • RAB4A
  • HRES-1/RAB4
  • RAB4
  • AI848268
  • Rab4
  • RAB4A, member RAS oncogene family
  • RAB4a, member RAS oncogene family
  • rab4a
  • RAB4A
  • LOC100341137
  • Rab4a
Epitope
C-Term
21
10
8
4
3
2
1
1
Reactivity
Human, Mouse (Murine), Rat (Rattus)
102
69
47
18
9
3
2
1
1
1
1
1
1
1
1
1
Host
Rabbit
55
46
1
Clonality
Polyclonal
Conjugate
Un-conjugated
4
4
4
3
2
2
2
2
2
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
1
Application
Immunocytochemistry (ICC), Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blotting (WB)
80
45
42
26
21
20
13
8
2
1
1
1
1
Options
Supplier
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Supplier Product No.
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Immunogen C-terminal peptide from human Rab4
Specificity Detects ~26 kDa.
Purification Peptide Affinity Purified
Alternative Name Rab4 (RAB4A Antibody Abstract)
Background 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) (1, 2). 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 (3). Through these proteins, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion(1). 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 intracellular localization of Rab proteins (3). Each Rab shows a characteristic sub-cellular distribution (4). 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 (5). 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 (6).
Gene ID 5868
NCBI Accession NP_004569
UniProt P20339
Research Area Cancer, Organelles, Signaling
Application Notes
  • WB (1:1000)
  • IHC (1:100)
  • ICC/IF (1:150)
  • optimal dilutions for assays should be determined by the user.
Comment

A 1:1000 dilution of SPC-141 was sufficient for detection of Rab4 in 10 μg of heat shocked HeLa cell lysate by colorimetric immunoblot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.

Restrictions For Research Use only
Format Liquid
Concentration 1 mg/mL
Buffer PBS pH 7.4, 50 % glycerol, 0.09 % sodium azide
Storage -20 °C
Supplier Images
 image for anti-RAB4A, Member RAS Oncogene Family (RAB4A) (C-Term) antibody (ABIN361841) Rab4, Hela
Product cited in: Ballmer-Hofer, Andersson, Ratcliffe, Berger: "Neuropilin-1 promotes VEGFR-2 trafficking through Rab11 vesicles thereby specifying signal output." in: Blood, Vol. 118, Issue 3, pp. 816-26, 2011 (PubMed).

Background publications Ali, Wasmeier, Lamoreux, Strom, Seabra: "Multiple regions contribute to membrane targeting of Rab GTPases." in: Journal of cell science, Vol. 117, Issue Pt 26, pp. 6401-12, 2004 (PubMed).

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).

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, Mari, van Obberghen, Le Marchand-Brustel: "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, Mâle, Goud, Mellman: "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).

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