Anti-Myopodin antibody produced in rabbit

Myopodin (80-95 kDa), a novel actin bundling protein, is an additional member of the synaptopodin gene family. Myopodin is expressed in skeletal and cardiac muscles. Myopodin contains one PPXY motif, multiple PXXP motifs, and a nuclear export sequence (NES). In the-disc, myopodin colocalizes with α-actinin. Myopodin, like several actin-bundling proteins, has been shown to shuttle between the nucleus and cytoplasm. It is localized in nucleus in myoblasts.

synthetic peptide encoding amino acids 566-585 located at the mid-region of human myopodin, conjugated to KLH. This sequence is highly conserved (77% sequence identity) in mouse myopodin and is not found in human or rat synaptopodin.

Anti-Myopodin has been used in:

• immunohistochemistry
• immunostaining
• western blot analysis

Myopodin directly binds to actin and contains an actin-binding site in the centre of the protein. Myopodin has actin bundling activity as shown by lantraculin - a sensitive cytosolic actin bundles and nuclear actin loops in transfected cells expressing GFP-myopodin. It binds to stress fibres in a punctuated pattern into the Z-disc during myotube differentiation. Myopodin is frequently down-regulated in invasive stages of some types of cancers, including invasive bladder tumors. Frequent complete or partial deletions of the myopodin gene have been shown to occur in 80% of invasive prostate cancer cases. Expression of myopodin induces suppression of tumor growth both in vivo and in vitro. Myopodin inhibits tumor metastasis by functioning as a tumor suppressor gene.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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