The melanocyte-specific protein PMEL (also known as Pmel17, gp100, melanocyte protein, premelanosome protein or silver locus protein homolog (SILV)) is a type I transmembrane glycoprotein that is expressed primarily in pigment cells of the skin and eye. In melanosomes, the protein forms a fibrillar matrix on which the UV-shielding pigment melanin is deposited.1-2
특이성
Anti-PMEL antibody specifically recognizes human PMEL protein.
애플리케이션
The antibody may be used in various immunochemical techniques including Immunoblotting (~100 kDa), Immunohistochemistry and Immunofluorescence. Detection of the PMEL band by Immunoblotting is specifically inhibited by the immunogen.
생화학적/생리학적 작용
PMEL fibrils are a major functional component of the melanosomal compartment as they optimize melanin polymerization, condensation and storage.1,3 PMEL fibrils have an amyloidogenic nature and share features with pathological amyloids.4 Mutations in PMEL are associated with pigmentation disorders and/or impairments in eye development in various species.1,5,6 PMEL is suggested an excellent model system to study mechanisms of intracellular amyloid formation.1
물리적 형태
Supplied as a solution in 0.01 M phosphate buffered saline pH 7.4, containing 15 mM sodium azide as a preservative.
저장 및 안정성
For continuous use, store at 2-8°C for up to one month. For extended storage, freeze in working aliquots. Repeated freezing and thawing is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilution samples should be discarded if not used within 12 hours.
면책조항
Unless otherwise stated in our catalog 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.
PMEL is a pigment cell protein that forms physiological amyloid in melanosomes. Many amyloids and/or their oligomeric precursors are toxic, causing or contributing to severe, incurable diseases including Alzheimer's and prion diseases. Striking similarities in intracellular formation pathways between PMEL
Forward genetic screens have been instrumental in defining molecular components of visual function. The zebrafish mutant fading vision (fdv) has been identified in such a screen due to defects in vision accompanied by hypopigmentation in the retinal pigment epithelium (RPE)
Journal of cell science, 128(7), 1400-1407 (2015-02-19)
Analysis of melanosome biogenesis in the retinal pigment epithelium (RPE) is challenging because it occurs predominantly in a short embryonic time window. Here, we show that the zebrafish provides an ideal model system for studying this process because in the
Amyloid is a generally insoluble, fibrous cross-beta sheet protein aggregate. The process of amyloidogenesis is associated with a variety of neurodegenerative diseases including Alzheimer, Parkinson, and Huntington disease. We report the discovery of an unprecedented functional mammalian amyloid structure generated
PMEL is a pigment cell-specific protein responsible for the formation of fibrillar sheets within the pigment organelle, the melanosome. The fibrillar sheets serve as a template upon which melanins polymerize as they are synthesized. The PMEL fibrils are required for