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48-602MAG
Buffer Detection Kit for Magnetic Beads
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Anti-Desmoplakin 1& 2 Antibody, clone DP2.15 detects level of Desmoplakin 1& 2 & has been published & validated for use in IF, WB & IC.
Key Applications
Immunofluorescence
Western Blotting
Immunocytochemistry
Application Notes
Western blot Immunohistochemistry: 1:10; Frozen tissue Immunofluorescence
Optimal working dilutions must be determined by the end user.
Biological Information
Immunogen
Bovine desmoplakin 1 & 2
Clone
DP2.15
Host
Mouse
Specificity
This antibody shows distinct punctate membrane staining of desmoplakins 1 (MW 250 kDa) and 2 (MW 215 kDa) in stratified epithelia and simple epithelia, including glands, urothelium, thymic reticular epithelium, hepatocytes, intercalated disks of myocardium and arachnoid cells of meninges.
Desmosomes are intercellular junctions that tightly link adjacent cells. Desmoplakin is an obligate component of functional desmosomes that anchors intermediate filaments to desmosomal plaques. The N-terminus of desmoplakin is required for localization to the desmosome and interacts with the N-terminal region of plakophilin 1 and plakoglobin. The C-terminus of desmoplakin binds with intermediate filaments. In the mid-region of desmoplakin, a coiled-coiled rod domain is responsible for homodimerization. Mutations in this gene are the cause of several cardiomyopathies and keratodermas as well as the autoimmune disease paraneoplastic pemphigus.
FUNCTION: SwissProt: P15924 # Major high molecular weight protein of desmosomes. Involved in the organization of the desmosomal cadherin- plakoglobin complexes into discrete plasma membrane domains and in the anchoring of intermediate filaments to the desmosomes. SIZE: 2871 amino acids; 331774 Da SUBUNIT: Homodimer. SUBCELLULAR LOCATION: Note=Innermost portion of the desmosomal plaque. TISSUE SPECIFICITY: Isoform DPI is apparently an obligate constituent of all desmosomes; Isoform DPII resides predominantly in tissues and cells of stratified origin. DOMAIN: SwissProt: P15924 The N-terminal region is required for localization to the desmosomal plaque and interacts with the N-terminal region of plakophilin 1. The C-terminal region interacts with intermediate filaments. PTM: Substrate of transglutaminase. Some glutamines and lysines are cross-linked to other desmoplakin molecules, to other proteins such as keratin, envoplakin, periplakin and involucrin, and to lipids like omega-hydroxyceramide. DISEASE: "SwissProt: P15924 # Defects in DSP are the cause of keratosis palmoplantaris striata II (PPKS2) [MIM:125647]; also known as striate palmoplantar keratoderma II (SPPK2). PPKS2 is characterized by skin thickening in the palms (linear pattern) and the soles (island-like pattern) and flexor aspect of the fingers; and rarely by abnormalities of the nails, the teeth and the hair. & Defects in DSP are the cause of dilated cardiomyopathy with woolly hair and keratoderma (DCWHK) [MIM:605676]; also known as Carvajal syndrome or palmoplantar keratoderma with left ventricular cardiomyopathy and woolly hair. DCWHK is an autosomal recessive cardiocutaneous syndrome characterized by a generalized striate keratoderma particularly affecting the palmoplantar epidermis, woolly hair, and dilated left ventricular cardiomyopathy. & Defects in DSP are the cause of familial arrhythmogenic right ventricular dysplasia 8 (ARVD8) [MIM:607450]; also known as arrhythmogenic right ventricular cardiomyopathy 8 (ARVC8). ARVD is an autosomal dominant disease characterized by partial degeneration of the myocardium of the right ventricle, electrical instability, and sudden death. It is clinically defined by electrocardiographic and angiographic criteria; pathologic findings, replacement of ventricular myocardium with fatty and fibrous elements, preferentially involve the right ventricular free wall. & Defects in DSP are the cause of skin fragility-woolly hair syndrome (SFWHS) [MIM:607655]. SFWHS is an autosomal recessive genodermatosis characterized by focal and diffuse palmoplantar keratoderma, hyperkeratotic plaques on the trunk and limbs, and woolly hair with varying degrees of alopecia. & Defects in DSP are the cause of lethal acantholytic epidermolysis bullosa [MIM:609638]. Lethal acantholytic epidermolysis bullosa is characterized by severe fragility of skin and mucous membranes. The phenotype is lethal in the neonatal period because of immense transcutaneous fluid loss. Typical features include universal alopecia, neonatal teeth, and nail loss. Histopathology of the skin shows suprabasal clefting and acantholysis throughout the spinous layer, mimicking pemphigus." SIMILARITY: Belongs to the plakin or cytolinker family. & Contains 17 plectin repeats. & Contains 2 spectrin repeats.
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Storage and Shipping Information
Storage Conditions
Reconstituted antibody can be stored at 2°-8°C for up to 12 months from date of receipt. Antibody can also be stored at -20°C in undiluted aliquots.
Immunocytochemical identification of epithelium-derived human tumors with antibodies to desmosomal plaque proteins. Franke, W W, et al. Proc. Natl. Acad. Sci. U.S.A., 80: 543-7 (1983)
1982
Epithelial cells contain desmosomes, special intercellular junctions providing sites of membrane attachment for intermediate-sized filaments of the cytokeratin type (tonofilaments). Such sites of anchorage of tonofilaments appear as dense plaques on the cytoplasmic side of the desmosomal membrane. We have isolated desmosome-enriched fractions from bovine snout epidermis and tongue mucosa and have characterized the major protein associated with the desmosomal plaque. This protein occurs in equimolar amounts of two polypeptides of Mr 250,000 (desmoplakin I) and Mr 215,000 (desmoplakin II) which are chemically and immunologically related. Antibodies raised against desmoplakins allow the identification and localization of this protein in epithelial cells grown in tissues or in vitro and show crossreaction in species as diverse as man, mouse, and chicken. Using immunolocalization at the light and electron microscope levels, we show that these antibodies bind specifically to desmosomal plaques. Antibodies to desmoplakins have been used successfully for detection of desmosomal proteins in a broad variety of epithelium-derived human tumors, including primary carcinomas and their metastases, irrespective of the morphology of the specific tumor. Nonepithelial tumors examined have been negative. We propose to use antibodies to desmoplakins and to cytokeratins in pathological diagnosis as two independent markers for the positive immunocytochemical identification and classification of epithelium derived tumors.
