SAB4200867
Anti-PMEL antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
Synonym(s):
ME20-M (ME20M) Melanoma-associated ME20 antigen, Melanocyte protein, Melanocyte protein Pmel 17, Melanocytes lineage-specific antigen GP100, Melanoma gp100, P1, P100, Premelanosome protein, Silver locus protein homolog
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About This Item
NACRES:
NA.43
UNSPSC Code:
12352203
Conjugate:
unconjugated
Clone:
polyclonal
Application:
—
Citations:
6
conjugate
unconjugated
antibody form
affinity isolated antibody
clone
polyclonal
form
liquid
species reactivity
human
concentration
~1 mg/mL
technique(s)
immunoblotting: 1:1000-1:2000 using human melanoma SK-MEL-28 cell lysate
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
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General description
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
Application
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.
Detection of the PMEL band by Immunoblotting is specifically inhibited by the immunogen.
Biochem/physiol Actions
Anti-PMEL antibody specifically recognizes human PMEL protein.
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
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
Physical form
Supplied as a solution in 0.01 M phosphate buffered saline pH 7.4, containing 15 mM sodium azide as a preservative.
Preparation Note
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.
Disclaimer
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.
Storage Class
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
常规特殊物品
低风险生物材料
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Christin Bissig et al.
International journal of molecular sciences, 17(9) (2016-09-03)
In pigment cells, melanin synthesis takes place in specialized organelles, called melanosomes. The biogenesis and maturation of melanosomes is initiated by an unpigmented step that takes place prior to the initiation of melanin synthesis and leads to the formation of
Thomas Burgoyne et al.
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
Douglas M Fowler et al.
PLoS biology, 4(1), e6-e6 (2005-11-23)
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
Jia Shee Hee et al.
Scientific reports, 7, 44064-44064 (2017-03-09)
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
Brenda Watt et al.
Pigment cell & melanoma research, 26(3), 300-315 (2013-01-29)
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
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