Anti-RALBP1 Antibody Picoband™ (monoclonal, 2E11)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application ![]()
| WB, FC |
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Primary Accession | Q15311 |
Host | Mouse |
Isotype | Mouse IgG2a |
Reactivity | Human |
Clonality | Monoclonal |
Format | Lyophilized |
Description | Anti-RALBP1 Antibody Picoband™ (monoclonal, 2E11) . Tested in Flow Cytometry, WB applications. This antibody reacts with Human. |
Reconstitution | Add 0.2ml of distilled water will yield a concentration of 500ug/ml. |
Gene ID | 10928 |
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Other Names | RalA-binding protein 1, 76 kDa Ral-interacting protein, Dinitrophenyl S-glutathione ATPase, DNP-SG ATPase, 7.6.2.2, 7.6.2.3, Ral-interacting protein 1, RALBP1 (HGNC:9841) |
Calculated MW | 95 kDa |
Application Details | Western blot, 0.25-0.5 µg/ml, Human Flow Cytometry, 1-3 µg/1x10^6 cells, Human |
Contents | Each vial contains 4mg Trehalose, 0.9mg NaCl and 0.2mg Na2HPO4. |
Clone Names | Clone: 2E11 |
Immunogen | E. coli-derived human RALBP1 recombinant protein (Position: K239-Q506). |
Purification | Immunogen affinity purified. |
Storage | Store at -20˚C for one year from date of receipt. After reconstitution, at 4˚C for one month. It can also be aliquotted and stored frozen at -20˚C for six months. Avoid repeated freeze-thaw cycles. |
Name | RALBP1 (HGNC:9841) |
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Function | Multifunctional protein that functions as a downstream effector of RALA and RALB (PubMed:7673236). As a GTPase-activating protein/GAP can inactivate CDC42 and RAC1 by stimulating their GTPase activity (PubMed:7673236). As part of the Ral signaling pathway, may also regulate ligand-dependent EGF and insulin receptors-mediated endocytosis (PubMed:10910768, PubMed:12775724). During mitosis, may act as a scaffold protein in the phosphorylation of EPSIN/EPN1 by the mitotic kinase cyclin B-CDK1, preventing endocytosis during that phase of the cell cycle (PubMed:12775724). During mitosis, also controls mitochondrial fission as an effector of RALA (PubMed:21822277). Recruited to mitochondrion by RALA, acts as a scaffold to foster the mitotic kinase cyclin B-CDK1-mediated phosphorylation and activation of DNM1L (PubMed:21822277). |
Cellular Location | Cell membrane; Peripheral membrane protein. Cytoplasm, cytosol Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q62796} Nucleus. Mitochondrion. Note=Cytosolic protein that transiently associates with the mitotic spindle poles in early prophase, and dissociates from them after completion of mitosis (By similarity) Targeted to the plasma membrane through its interaction with RALB, directed by FGF signaling. Docking on the membrane is required to transduce the Ral signal (By similarity). Recruited by RALA to the mitochondrion during mitosis where it regulates mitochondrial fission (PubMed:21822277). Nuclear localization is cell cycle dependent while membrane localization is seen in adherent cells (PubMed:22319010). The region involved in membrane association could form transmembrane domains and expose a part of the protein extracellularly (Probable) {ECO:0000250|UniProtKB:Q62796, ECO:0000250|UniProtKB:Q9PT60, ECO:0000269|PubMed:21822277, ECO:0000269|PubMed:22319010, ECO:0000305|PubMed:15610018} |
Tissue Location | Expressed ubiquitously but at low levels. Shows a strong expression in the erythrocytes. |

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Provided below are standard protocols that you may find useful for product applications.
Background
RalA-binding protein 1 is a protein that in humans is encoded by the RALBP1 gene. Small G proteins, such as RAL, have GDP-bound inactive and GTP-bound active forms, which shift from the inactive to the active state through the action of RALGDS, which in turn is activated by RAS. RALBP1 plays a role in receptor-mediated endocytosis and is a downstream effector of the small GTP-binding protein RAL. RALBP1 is also the dominant transporter of lipid peroxidation-derived glutathione conjugates and participates in several mitotic events, including inactivation of endocytosis and separation and polar movement of centrioles and appropriate distribution of mitochondria to daughter cells following mitosis.

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