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Technical Data Sheet

CP1131

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Cofilin 1 (N-terminus)
Rabbit Polyclonal
Price
Size
Species Reactivity
MW

$295
100 μl
Hu, Rt, Ms, Ck
19 kDa

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Western blot of cofilin in jurkat cells. The blots were untreated (lanes 1 & 4) or treated (lanes 2, 3, 5 & 6) with lambda phosphatase. In lanes 3 & 6, the phosphatase was inhibited with phospho-Cofilin 1 (Ser-3) peptide. The blots were probed with anti-Cofilin 1 (Ser-3) phospho-specific (lanes 1-3) or anti-Cofilin 1 (N-terminus) (lanes 4-6).

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Immunocytochemical labeling in chick dorsal root ganglion neurons using anti-Cofilin (N-terminus; CP1131), anti-Cofilin (Ser-3; CP1151), anti-βIII-Tubulin (C-terminus; TP1691) and anti-β-Tubulin (TM1541) antibodies. (Images provided by Dr. Diane Snow, Department of Anatomy & Neurobiology, University of Kentucky).

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Application
Dilution


ELISA
1:2000


ICC
1:50


WB
1:1000



End user should determine optimal dilution for their particular applications and experiments.Western blot membranes were incubated with diluted antibody in 5% non-fat milk, PBS, 0.04% Tween20 for 1hour at room temperature.
Product References
Giacobbe, A. et al. (2015) Oncogene. doi: 10.1038 WB: MCF-7
Amelio, I. et al. (2012) J Cell Biol. 199(2):347. WB: human primary epidermal keratinocytes
Ghia, E.M. et al. (2011) J Immunology. 186:6338. WB: human U937 cells
Couch, B.A. et al. (2010) J Alzheimer’s Disease. 20:1003. WB: mouse hippocampus, fasudil
Garg, P. et al. (2010) J Biol Chem. 285:22676. WB: human, mouse podocytes
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Background
Members of the ADF/cofilin (AC) family are actin-severing proteins that regulate actin remodeling during cellular events such as cell migration, cytokinesis, phagocytosis, endocytosis, axon development, and immune cell activation. In mammals, there are three members of the AC family, muscle-specific cofilin (cofilin 2), non-muscle cofilin (cofilin 1), and ADF. In humans, cofilin 1 and ADF have 72% identity, with the major amino acid differences found in the C-terminal region. Regulation of cofilin activity can occur through serine phosphorylation. 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, PP1, PP2A, PP2B, slingshot, and chronophin can dephosphorylate Ser-3 and activate actin binding. Thus, Ser-3 phosphorylation is a major site for the regulation of cofilin activity.


Background References
Bamburg, J.R. (1999). Annu Rev Cell Dev Biol. 15:185.
Aizawa, H., et al. (2001). Nature Neurosci. 4(4):367.
Maciver, S.K. & Hussey, P.J. (2002). Genome Biol. 3(5):3007.
Immunogen
A synthetic peptide (coupled to KLH) corresponding to amino acid residues at the N-terminus of human Cofilin 1. This sequence has 100% homology with similar regions of rat and mouse Cofilin 1, and has 3 amino acid differences from human Cofilin 2.
Buffer and Storage
Rabbit polyclonal, affinity-purified antibody is supplied in 100µl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.
Specificity
This antibody was affinity purified using Cofilin 1 peptide (without carrier). The antibody detects a 19 kDa* protein corresponding to the molecular mass of Cofilin 1 on SDS-PAGE immunoblots of Jurkat cells.

*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
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