Anti-Myoferlin Antibody

Cell membrane; Single-pass type II membrane protein. Nucleus membrane; Single-pass type II membrane protein. Cytoplasmic vesicle membrane; Single-pass type II membrane protein. Note=Concentrated at the membrane sites of both myoblast-myoblast and myoblast-myotube fusions. Detected at the plasmalemma in endothelial cells lining intact blood vessels (By similarity). Found at nuclear and plasma membranes. Enriched in undifferentiated myoblasts near the plasma membrane in puncate structures.

Reconstitute lyophilized antibody using ultrapure to a final concentration no less than 100 ug/mL. Reconstitution with PBS or Tris buffer is acceptable if required. Protein carrier, biocide or cryopreservative can be added as needed. Aliquot and store at -20C for longterm storage. Dilute immediately prior to use.

Calcium/phospholipid-binding protein that plays a role in the plasmalemma repair mechanism of endothelial cells that permits rapid resealing of membranes disrupted by mechanical stress. Involved in endocytic recycling. Implicated in VEGF signal transduction by regulating the levels of the receptor KDR (By similarity). {ECO:0000250}.

Immunoblotting: use at 1-10ug/mL. A band of ~230kDa is detected. <br><br>Immunocytochemistry: use at 1- 20ug/mL. <br><br>These are recommended concentrations. <br><br>Enduser should determine optimal concentrations for their applications.

This product is stable for at least one (1) year at -20°C to -70°C. Reconstituted product should be stored in appropriate aliquots to avoid repeated freeze-thaw cycles.

Ferlin proteins have been implicated in vesicle trafficking in a variety of physio- logical settings. All mammalian ferlins derive their names based on homology to the C. elegans protein FER-1 (FERtilization defective-1). FER1L3 (myoferlin, MYOF), has not yet been directly associated with a distinct mammalian disorder, but recent microarray and proteomic studies in the cancer literature have reported overexpression of MYOF in breast cancer specimens and relevant cell lines. Therefore, MYOF may be an important protein in breast cancer cells for their mobilization during cellular migration and/or invasion.