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Western blot analysis of Ral A on a rat cerebrum lysate. Lane 1: 1:5000, lane 2: 1:10,000, lane 3: 1:20,000 dilution of the anti-Ral A antibody.
Immunofluorescence staining of rat neurons at 5 µg/ml of the anti-Ral A antibody.
BD Transduction Laboratories™ Purified Mouse Anti-Ral A
BD Transduction Laboratories™ Purified Mouse Anti-Ral A
Regulatory Status Legend
Any use of products other than the permitted use without the express written authorization of Becton, Dickinson and Company is strictly prohibited.
Preparation And Storage
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
- Source of all serum proteins is from USDA inspected abattoirs located in the United States.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
Companion Products
Ral is a low molecular weight GTP-binding protein belonging to the Ras superfamily of GTP-binding proteins and shows 50% amino acid identity to Ras. Ral cDNA clones have been isolated from human placenta, human pheochromocytoma, simian ß-lymphocyte, and marine ray electric lobe cDNA libraries. In humans, cDNA sequences for Ral A and RalB have been determined. The predicted amino acid sequences show 85% identity. Both proteins consist of 206 amino acids with a predicted molecular weight of 24kDa. However, Ral A isolated from human platelets shows an apparent molecular weight of 26-28kDa. Ral A mRNA levels in adult mouse tissues appear to be highest in testes, ovary, and brain, with lower levels found in the liver, spleen, kidney, thymus, heart, and salivary glands. Similar results have been observed in rat tissues.
Development References (5)
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Goi T, Rusanescu G, Urano T, Feig LA. Ral-specific guanine nucleotide exchange factor activity opposes other Ras effectors in PC12 cells by inhibiting neurite outgrowth. Mol Cell Biol. 1999; 19(3):1731-1741. (Biology: Immunofluorescence). View Reference
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Kinashi T, Katagiri K, Watanabe S, Vanhaesebroeck B, Downward J, Takatsu K. Distinct mechanisms of alpha 5beta 1 integrin activation by Ha-Ras and R-Ras. J Biol Chem. 2000; 275(29):22590-22596. (Biology: Western blot). View Reference
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Olofsson B, Chardin P, Touchot N, Zahraoui A, Tavitian A. Expression of the ras-related ralA, rho12 and rab genes in adult mouse tissues. Oncogene. 1988; 3(2):231-234. (Biology). View Reference
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Polakis PG, Weber RF, Nevins B, Didsbury JR, Evans T, Snyderman R. Identification of the ral and rac1 gene products, low molecular mass GTP-binding proteins from human platelets. J Biol Chem. 1989; 264(28):16383-16389. (Biology). View Reference
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Xu L, Frankel P, Jackson D, et al. Elevated phospholipase D activity in H-Ras- but not K-Ras-transformed cells by the synergistic action of RalA and ARF6. Mol Cell Biol. 2003; 23(2):645-654. (Biology: Immunoprecipitation, Western blot). View Reference
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