The Phospho-CFL1/CFL2 (Tyr88) Antibody (PAC02437) is a valuable tool for researchers studying cell signaling pathways involving cofilin proteins. This polyclonal antibody, raised in mice, specifically recognizes the phosphorylated form of both CFL1 and CFL2 at Tyrosine 88. Validated for use in Western blot and immunohistochemistry applications, this antibody allows for the detection and analysis of phospho-CFL1/CFL2 in various cell types and tissue samples.Cofilins are actin-binding proteins that play a crucial role in regulating actin dynamics, cell motility, and cytoskeletal organization. Phosphorylation of CFL1 and CFL2 at Tyr88 is known to influence their activity and function in processes such as cell migration, adhesion, and invasion.
Understanding the regulation of cofilin phosphorylation is important for research in cell biology, cancer metastasis, and other cellular processes.With its high specificity and sensitivity, the Phospho-CFL1/CFL2 (Tyr88) Antibody is a valuable tool for investigating the role of cofilin phosphorylation in various physiological and pathological conditions. Its use can lead to valuable insights into cell signaling pathways and potential therapeutic targets for diseases involving dysregulated actin dynamics.
Peptide sequence around phosphorylation site of tyrosine 88 (A-T-Y(p)-E-T) derived from Human coflin1/cofilin2.
Form:
Liquid
Storage Buffer:
Supplied at 1.0mg/mL in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
Purification Method:
Antibodies were produced by immunizing rabbits with synthetic phosphopeptide and KLH conjugates. Antibodies were purified by affinity-chromatography using epitope-specific phosphopeptide. Non-phospho specific antibodies were removed by chromatogramphy using non-phosphopeptide.
Clonality:
Polyclonal
Isotype:
IgG
Conjugate:
Non-conjugated
Western blot analysis of extracts from Mouse heart tissue using cofilin1/cofilin2(phospho-Tyr88) Antibody.
Immunohistochemical analysis of paraffin-embedded human breast carcinoma tissue using cofilin1/cofilin2(Phospho-Tyr88) Antibody(left) or the same antibody preincubated with blocking peptide(right).
Background:
Controls reversibly actin polymerization and depolymerization in a pH-sensitive manner. It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It is the major component of intranuclear and cytoplasmic actin rods.
Synonyms:
CFL1/CFL2
UniProt Protein Function:
Cofilin-1: a cytoskeletal protein that controls actin depolymerization. Has a 5-10-fold higher affinity for ATP-actin monomers than cofilin-1. May promote filament assembly rather than disassembly. Two alternatively spliced variants are described. Isoform b is expressed predominantly in skeletal muscle and heart, while isoform a is expressed in various tissues.
UniProt Protein Details:
Protein type:Motility/polarity/chemotaxis; Nuclear receptor co-regulator; Cytoskeletal
Biological Process: actin cytoskeleton organization and biogenesis; actin filament depolymerization; axon guidance; blood coagulation; cytokinesis after mitosis; cytoskeleton organization and biogenesis; ephrin receptor signaling pathway; establishment of cell polarity; innate immune response; negative regulation of apoptosis; neural crest cell migration; neural fold formation; platelet activation; platelet degranulation; positive regulation of actin filament depolymerization; protein amino acid phosphorylation; regulation of cell morphogenesis; response to amino acid stimulus; response to virus; Rho protein signal transduction
NCBI Summary:
The protein encoded by this gene can polymerize and depolymerize F-actin and G-actin in a pH-dependent manner. Increased phosphorylation of this protein by LIM kinase aids in Rho-induced reorganization of the actin cytoskeleton. Cofilin is a widely distributed intracellular actin-modulating protein that binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. It is involved in the translocation of actin-cofilin complex from cytoplasm to nucleus.[supplied by OMIM, Apr 2004]
