R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
Twinfilin-1 (D7C6J) Rabbit mAb #14138
Filter:
- WB
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 40 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
Twinfilin-1 (D7C6J) Rabbit mAb recognizes endogenous levels of total twinfilin protein. In some cell lines, this antibody also recognizes a 48 kDa band of unknown origin.
Species Reactivity:
Human, Mouse, Rat, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu222 of human twinfilin-1 protein.
Background
Twinfilin is an actin monomer-binding protein found in all eukaryotes (1). Mammals have three isoforms. Twinfilin-1 and twinfilin-2a are expressed in most non-muscle cell types, whereas twinfilin-2b is the main isoform in adult heart and skeletal muscle (2). Twinfilins are composed of two ADF-homology domains connected by a 30 kDa linker region. All twinfilins have been shown to form a 1:1 complex with G-actin, but not F-actin (reviewed in 3). Twinfilin-1 was originally known as A6 protein tyrosine kinase and thought to be part of a novel class of protein kinases. However, the protein was renamed after further studies showed no evidence of tyrosine kinase activity (4). Twinfilin-1 helps to prevent the actin filament assembly by forming a complex with actin monomers and, in mammals, has been shown to cap the filament barbed ends. It has been suggested that this regulates cell motility (5). Suppression of twinfilin-1 has also been shown to slow lymphoma cell migration to lymph nodes (6).
- Goode, B.L. et al. (1998) J Cell Biol 142, 723-33.
- Nevalainen, E.M. et al. (2009) Biochem J 417, 593-600.
- Palmgren, S. et al. (2002) J Cell Sci 115, 881-6.
- Vartiainen, M. et al. (2000) Mol Cell Biol 20, 1772-83.
- Helfer, E. et al. (2006) EMBO J 25, 1184-95.
- Meacham, C.E. et al. (2009) Nat Genet 41, 1133-7.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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