Synaptopodin, a prolin-rich actin-binding protein with 2 binding sites for actin, represents a new class of actin-binding proteins which has first been localized in podocytes and a subset of telencephalic postsynaptic densities. In human tissue synaptopodin has a molecular weight of 73.7kD and pI of 9.38 (calculated from sequence data); in mouse the corresponding data are 74kD, pI 9.27. In SDS-PAGE the antigen appears as 100kD polypeptide in brain and 110kD polypeptide in kidney (the difference might be attributed to posttranslational modifications).
Suitable for use in Immunofluorescence, Western Blot and Immunohistochemistry. Other applications have not been tested.
Immunohistochemistry (frozen sections and paraffin-embedded tissue after microwave treatment): 1:5-1:10. Incubate for 1hr at RT.
Optimal dilutions to be determined by the researcher.
Storage and Stability:
Lyophilized powder may be stored at -20°C. Stable for 12 months at -20°C. Reconstitute with sterile ddH2O. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Reconstituted product is stable for 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
|Isolated rat kidney glomeruli.|
|Purified by Protein A affinity chromatography.|
|Supplied as a lyophilized powder from PBS, pH 7.4, 0.5% BSA, 0.09% sodium azide. Reconstitute with 1ml sterile ddH2O.|
|Recognizes rat synaptopodin at ~44kD (degradation product). Species Crossreactivity: human, bovine, guinea pig, mouse, and gerbil. Does not recognize rabbit, frog or chicken. Recognizes differentiated podocytes (glomerular visceral epithelial cells) in vivo and in vitro (weaker additional reaction with arterial endothelial cells); co-localizes with a-actinin. Does not react with parietal cells. Reacts with a subset of exclusively telencephalic synapses. Differentiation-dependent expression in cultured hippocampal neurons and during postnatal maturation of rat brain.|
|Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.|
1. Mundel P, Gilbert P, and W Kriz. Podocytes in Glomerulus of Rat Kidney Express a Characteristic 44 kD Protein. J Histochem and Cytochem Vol 39 No 8:1047-1056 (1991). 2. Mundel P and W Kritz. Structure and function of podocytes: an update. Anat Embryol 192:385-397 (1995). 3. Mundel P, Reiser J, Kriz W. Phenotypic conversion and differentiation of human and rat podocytes in vitro. J Am Soc Nephrol 8:8978-705 (1997). 4. Mundel P, Heid HW, Mundel TM, Krüger M, Reiser J, Kriz W. Synaptopodin, an actin-associated protein in telencephalic dendrites and in renal podocytes. J Cell Biol Vol 139 (1):193-204 (1997)|
5. Mundel P, Reiser J, Zuniga Borja A, Davidson G, Pavenstädt H, Kriz W, Zeller R. Rearrangements of cytoskeleton and cell contacts induce process formation and postmitotic differentiation of conditionally immortalized mouse podocyte cell lines, Exp Cell Res 236: 248-258 (1997) 6. Kobayashi N, Kriz W, Kuriyma R, Mundel P: Non-uniform microtubular polarity, established by CHO1/MKLP1 motor protein, is necessary for process formation of podocytes. J Cell Biol 143: 1961-1970 (1998)
7. Barisoni L, Kriz W, Mundel P, D'Agati V. The dysregulated podocyte phenotype: a novel concept in the pathogenesis of collapsing idiopathic focal segmental glomerulosclerosis and HIV-associated nephropathy. J Am Soc Nephrol 10: 51-61 (1999) 8. Kihara I, Yaoita E, Kawasaki K, Yamamoto T, Hara M, Yanagihara T: Origin of hyperplastic epithelial cells in idiopathic collapsing glomerulopathy. Histopathology 34(6): 537-547 (1999)