Rabbit Polyclonal
ELISA | 1:2000 |
ICC | 1:250 |
IHC | 1:100 |
WB | 1:1000 |
Size 100 μl
Species Reactivity Hu, Rt, Ms
MW 150 kDa
Members of the ADF/cofilin (AC) family are actin-severing proteins that regulate actin remodeling during cell motility. Regulation of cofilin activity can occur through serine phosphorylation and dephosphorylation. Activation of cofilin kinases, LIMK1 or LIMK2, leads to phosphorylation of cofilin at serine 3. This phosphorylation disrupts cofilin binding to actin in vitro and in vivo. Multiple phosphatases, Slingshot, PP1, PP2A, PP2B, and chronophin can dephosphorylate Ser-3 and activate actin binding. In mammals, the Slingshot family includes SSH1L, SSH2L, and SSH3L. SSH1L and SSH2L mRNAs are widely expressed, while SSH3L has high expression in epithelial tissues. SSH1L can associate with F-actin and may be the major phosphatase regulating cofilin activity. Disruption of SSH1L expression using RNA interference impairs directional cell migration. Thus, Slingshot phosphatases may be critical for regulating cytoskeletal protein activity and cell motility.
References
Soosairajah, J. et al. (2005) EMBO J. 24(3):473.
Endo, M. et al. (2003) J Neurosci. 23(7):2527.
Niwa, R. et al. (2002) Cell 108:233.
Western blot of human recombinant SSH1L untreated (lanes 1 & 3) or treated with lambda phosphatase (lanes 2 & 4) and rat PC12 cells unstimulated (lanes 5 & 7) or stimulated with calyculin A (lanes 6 & 8). The blots were probed with anti-SSH1L (C-term.) (lanes 1, 2, 5, & 6) or anti-SSH1L (Ser-978) (lanes 3, 4, 7, & 8).
Formalin fixed, citric acid treated parafin sections of mouse cerebral cortex. Sections were probed with anti-Slingshot-1L (SP1711) then anti-Rabbit:HRP before detection using DAB. (Image provided by Carl Hobbs and Dr. Pat Doherty at Wolfson Centre for Age-Related Diseases, King's College London).
*For more information, see UniProt Accession Q8WYL5
The products are are safely shipped at ambient temperature for both domestic and international shipments. Each product is guaranteed to match the specifications as indicated on the corresponding technical data sheet. Please store at -20C upon arrival for long term storage.
*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
Product References:
Tedeschi, A. et al. (2019) Neuron. Online Aug. 7. (WB: rat DRG neurons)Lauterborn, J.C. et al. (2017) Cereb Cortex. 27(4):2640. (WB: rat hippocampus)
Wang, Y. et al. (2015) Cancer Lett. 360(2):171 (ICC: Prostate cancer cell lines)
Xiang, S.Y. et al. (2013) Sci Signal. 6(306):ra108. (WB: rat cardiomyocytes, siRNA)
Cho, IH et al. (2013) Cell Mol Life Sci 70(22):4369. (WB, ICC: HEK293T and HeLa cells)
Zhang, H. et al. (2013) J Biol Chem. 288(29):20966. (WB: Cap1 KD cells)
DiPaolo, B.C. et al. (2013) Am Jou of Phys 305(2): L141. (WB: rat alveolar type II)
Wang, Y. et al. (2013) J Neurosci. 33(15):6423. (WB: rat infralimbic cortex)
Blangy, et al. (2012) PLoS ONE 7(9):e45909. (WB: mouse osteoclast)
Vitolo, M. et al. (2013) Oncogene. 32(17):2200. (WB: MCF-10A, 293T)
Sparrow, N. et al. (2012) J Neurosci. 32(15):5284. (WB & ICC: rat Schwann cells)
Posadas, I. et al. (2012) J Neurochem. 120(4):515. (WB: rat neurons)
Kim, J. et al. (2011) J Cell Physiol 226(11):3014. (WB: human keratinocytes, siRNA )
Chiu, T. et al. (2010) Mol Biol Cell 21:3529. (WB: rat L6, siRNA )
Yuen, E. et al. (2010) J Physiol 588:2361. (WB: rat coritcal neurons, siRNA)
Kim, J.S. et al. (2009) Mol Biol Cell. 20(11):2650. (WB: human HeLa, siRNA)
Eiseler, T. et al. (2009) Nat Cell Biol. 11(5):545. (WB, IP, ICC: human HeLa cells)
Yuen, E.Y. & Yan, Z. (2009) J Neurosci. 29:550. (ICC: rat interneurons, siRNA)
Huang, Y. et al. (2008) Dev Cell 15(5):691. (WB: SSH transfectants .)
This kit contains: