Product Pathways - Cytoskeletal Signaling
Desmin Antibody #4024
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PhosphoSitePlus® protein, site, and accession data: desmin
| Applications | Reactivity | Sensitivity | MW (kDa) | Source |
|---|---|---|---|---|
| W IF-F | M R (H) (Mk) | Endogenous | 53 | Rabbit |
Applications Key:
W=Western Blotting
IF-F=Immunofluorescence (Frozen)
Reactivity Key:
H=Human
M=Mouse
R=Rat
Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.
Protocols
Specificity / Sensitivity
Desmin Antibody detects endogenous levels of total desmin protein.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human desmin. Antibodies are purified by peptide affinity chromatography.
Background
The cytoskeleton consists of three types of cytosolic fibers: microfilaments (actin filaments), intermediate filaments and microtubules. Major types of intermediate filaments are distinguished and expressed in particular cell types: cytokeratins (epithelial cells), glial fibrillary acidic protein or GFAP (glial cells), desmin (skeletal, visceral and certain vascular smooth muscle cells), vimentin (mesenchyme origin) and neurofilaments (neurons). GFAP and vimentin form intermediate filaments in astroglial cells and modulate their motility and shape (1). In particular, vimentin filaments are present at early developmental stages, while GFAP filaments are characteristic of differentiated and mature brain astrocytes. Thus, GFAP is commonly used as a marker for intracranial and intraspinal tumors arising from astrocytes (2). Vimentin is present in sarcomas, but not carcinomas, and its expression is examined relative to other markers to distinguish between the two forms of neoplasm (3). Desmin is a myogenic marker expressed in early development that forms a network of filaments that extends across the myofibril and surrounds Z discs. The desmin cytoskeleton provides a connection among myofibrils, organelles and the cytoskeleton (4). Desmin knockout mice develop cardiomyopathy, skeletal and smooth muscle defects (5). In humans, desmin related myopathies might be caused by mutations in the corresponding desmin gene or in proteins with which desmin interacts, including αB-crystallin and synemin. Disorganized desmin filaments and the accumulation of protein aggregates comprised predominantly of desmin characterize desmin-related myopathies (reviewed in 6,7).
- Eng, L.F. et al. (2000) Neurochem Res 25, 1439-51.
- Goebel, H.H. et al. (1987) Acta Histochem Suppl 34, 81-93.
- Leader, M. et al. (1987) Histopathology 11, 63-72.
- Capetanaki, Y. et al. (2007) Exp Cell Res 313, 2063-76.
- Li, Z. et al. (1996) Dev Biol 175, 362-6.
- Paulin, D. and Li, Z. (2004) Exp Cell Res 301, 1-7.
- Paulin, D. et al. (2004) J Pathol 204, 418-27.
Application References
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For Research Use Only. Not For Use In Diagnostic Procedures.