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Western blot analysis of Moesin on a Jurkat cell lysate (Human T-cell leukemia; ATCC TIB-152). Lane 1: 1:5000, lane 2: 1:10,000, lane 3: 1:20,000 dilution of the mouse anti-Moesin antibody.
Immunofluorescence staining of A498 cells (Human kidney carcinoma; ATCC HTB-44).
BD Transduction Laboratories™ Purified Mouse Anti-Moesin
BD Transduction Laboratories™ Purified Mouse Anti-Moesin
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
Recommended Assay Procedures
Western blot: Please refer to http://www.bdbiosciences.com/pharmingen/protocols/Western_Blotting.shtml
Product Notices
- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
- Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
- 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.
Companion Products
Moesin belongs to a family of proteins that includes ezrin and radixin. These proteins are co-expressed in a variety of cells. They localize to the cytoskeleton and modify interactions between cytoskeletal and membrane proteins. There is approximately 70% homology between moesin and ezrin and 80% homology between moesin and radixin. Moesin is intracellular and contains multiple conserved domains that are putative phosphorylation sites. It has a calculated molecular weight of 67.8 kDa, but migrates in SDS-PAGE at approximately 78 kDa. This discrepancy is likely due to a charged alpha-helical region within the protein.
Development References (5)
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Lankes WT, Furthmayr H. Moesin: a member of the protein 4.1-talin-ezrin family of proteins. Proc Natl Acad Sci U S A. 1991; 88(19):8297-8301. (Biology). View Reference
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Lankes WT, Schwartz-Albiez R, Furthmayr H. Cloning and sequencing of porcine moesin and radixin cDNA and identification of highly conserved domains. Biochim Biophys Acta. 1993; 1216(3):479-482. (Biology). View Reference
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Parlato S, Giammarioli AM, Logozzi M, et al. CD95 (APO-1/Fas) linkage to the actin cytoskeleton through ezrin in human T lymphocytes: a novel regulatory mechanism of the CD95 apoptotic pathway. EMBO J. 2000; 19(19):5123-5134. (Biology: Immunofluorescence, Western blot). View Reference
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Poliak S, Matlis S, Ullmer C, Scherer SS, Peles E. Distinct claudins and associated PDZ proteins form different autotypic tight junctions in myelinating Schwann cells. J Cell Biol. 2002; 159(2):361-371. (Biology: Immunofluorescence). View Reference
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Seveau S, Keller H, Maxfield FR, Piller F, Halbwachs-Mecarelli L. Neutrophil polarity and locomotion are associated with surface redistribution of leukosialin (CD43), an antiadhesive membrane molecule. Blood. 2000; 95(8):2462-2470. (Biology: Immunofluorescence, Western blot). View Reference
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