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Anti-Cofilin 1 (N-terminus) Antibody
- SPECIFICATION
- CITATIONS
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- BACKGROUND
Application 
| WB |
|---|---|
| Primary Accession | P23528 |
| Reactivity | Bovine, Chicken |
| Host | Rabbit |
| Clonality | Rabbit Polyclonal |
| Isotype | IgG |
| Calculated MW | 18502 Da |
| Gene ID | 1072 |
|---|---|
| Other Names | ADF, p18 |
| Target/Specificity | 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. |
| Format | Antigen Affinity Purified |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Anti-Cofilin 1 (N-terminus) Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Shipping | Blue Ice |
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Provided below are standard protocols that you may find useful for product applications.
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.
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