R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
STRN (E9V5M) Rabbit mAb #93019
Filter:
- WB
- IP
Supporting Data
REACTIVITY | H M |
SENSITIVITY | Endogenous |
MW (kDa) | 105 |
Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
Product Information
Product Usage Information
Application | Dilution |
---|---|
Western Blotting | 1:1000 |
Immunoprecipitation | 1:100 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
STRN (E9V5M) Rabbit mAb recognizes endogenous levels of total STRN protein.
Species Reactivity:
Human, Mouse
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Pro273 of human STRN protein.
Background
The mammalian striatin family consists of three proteins: Striatin (STRN), Striatin S/G2 nuclear autoantigen (STRN3), and Zinedin (STRN4). It is a component of STRIPAK complexes that function as a scaffold in various signaling pathways (1). The multi-protein STRIPAK complexes play important roles in various biological processes associated with signal transduction pathways, cell division, differentiation, and survival. These complexes have also been linked to several pathological conditions, including cancer, heart disease, diabetes, and neurological diseases. One of the major functions of STRIPAK complexes is to anchor and regulate protein phosphatase 2A (PP2A) activity (2). Phosphorylation of Striatin by ULK1 promotes activation of PP2A and autophagy (3). Striatin is predominantly found in the central and peripheral nervous systems, but its expression can be found in other tissues (4,5). Downregulation of Striatin in motor neurons impaired dendritic growth (6). The STRN gene has been identified as a rare fusion partner with tyrosine kinases PDGFRA and ALK observed in several cancers (7-9).
- Hwang, J. and Pallas, D.C. (2014) Int J Biochem Cell Biol 47, 118-48.
- Moreno, C.S. et al. (2000) J Biol Chem 275, 5257-63.
- Hu, Z. et al. (2021) Cell Rep 36, 109762.
- Moqrich, A. et al. (1998) Genomics 51, 136-9.
- Salin, P. et al. (1998) J Comp Neurol 397, 41-59.
- Bartoli, M. et al. (1999) J Neurobiol 40, 234-43.
- Curtis, C.E. et al. (2007) Br J Haematol 138, 77-81.
- Pérot, G. et al. (2014) PLoS One 9, e87170.
- Kelly, L.M. et al. (2014) Proc Natl Acad Sci USA 111, 4233-8.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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