Dysferlin (DYSF) Rabbit Polyclonal Antibody (ER1511-12)

UNIPROT #

O75923

PROTEIN NAME

Dysferlin (DYSF)

SYNONYMS

DMAT antibody;DYSF antibody;DYSF_HUMAN antibody;Dysferlin antibody;Dysferlin limb girdle muscular dystrophy 2B (autosomal recessive) antibody;Dysferlin limb girdle muscular dystrophy 2B antibody;Dystrophy associated fer 1 like 1 antibody;Dystrophy associated fer 1 like protein antibody;Dystrophy associated fer1 like 1 antibody;Dystrophy associated fer1 like protein antibody;Dystrophy-associated fer-1-like protein antibody;Fer 1 like protein 1 antibody;Fer-1-like protein 1 antibody;Fer1 like protein 1 antibody;FER1L1 antibody;FLJ00175 antibody;FLJ90168 antibody;LGMD 2B antibody;LGMD2B antibody;Limb girdle muscular dystrophy 2B (autosomal recessive) antibody;Limb girdle muscular dystrophy 2B antibody;Miyoshi myopathy antibody;MM antibody;MMD1 antibody

SEQUENCE SIMILARITIES

Belongs to the ferlin family.

TISSUE SPECIFICITY

Expressed in skeletal muscle, myoblast, myotube and in the syncytiotrophoblast (STB) of the placenta (at protein level). Ubiquitous. Highly expressed in skeletal muscle. Also found in heart, brain, spleen, intestine, placenta and at lower levels in liver, lung, kidney and pancreas.

DEVELOPMENTAL STAGE

Expression in limb tissue from 5-6 weeks embryos; persists throughout development.

SUBCELLULAR LOCATION

Plasma membrane, Cytoplasmic vesicle.

FUNCTION

The most intensively studied role for dysferlin is in a cellular process called membrane repair. Membrane repair is a critical mechanism by which cells are able to seal dramatic wounds to the plasma membrane. Muscle is thought to be particularly prone to membrane wounds given that muscle cells transmit high force and undergo cycles of contraction. Dysferlin is highly expressed in muscle, and is homologous to the ferlin family of proteins, which are thought to regulate membrane fusion across a wide variety of species and cell types. Several lines of evidence suggest that dysferlin may be involved in membrane repair in muscle. First, dysferlin-deficient muscle fibers show accumulation of vesicles (which are critical for membrane repair in non-muscle cell types) near membrane lesions, indicating that dysferlin may be required for fusion of repair vesicles with the plasma membrane. Further, dysferlin-deficient muscle fibers take up extracellular dyes to a greater extent than wild-type muscle fibers following laser-induced wounding in-vitro.