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- Antigen structure
- References [5]
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- Product number
- ABIN2846667 - Provider product page
- Provider
- antibodies-online
- Product name
- anti-Premelanosome Protein (PMEL) (AA 412-440), (Center) antibody
- Antibody type
- Polyclonal
- Description
- This antibody is purified through a protein A column, followed by peptide affinity purification.
- Reactivity
- Human
- Host
- Rabbit
- Epitope
- AA 412-440, Center
- Antibody clone number
- RB33755
- Vial size
- 80 μL
- Storage
- SILV Antibody (Center) can be refrigerated at 2-8°C for up to 6 months. For long term storage, place the at -20°C.
Submitted references Endoplasmic reticulum export, subcellular distribution, and fibril formation by Pmel17 require an intact N-terminal domain junction.
The secreted form of a melanocyte membrane-bound glycoprotein (Pmel17/gp100) is released by ectodomain shedding.
Formation of Pmel17 amyloid is regulated by juxtamembrane metalloproteinase cleavage, and the resulting C-terminal fragment is a substrate for gamma-secretase.
N-terminal domains elicit formation of functional Pmel17 amyloid fibrils.
The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis.
Leonhardt RM, Vigneron N, Rahner C, Van den Eynde BJ, Cresswell P
The Journal of biological chemistry 2010 May 21;285(21):16166-83
The Journal of biological chemistry 2010 May 21;285(21):16166-83
The secreted form of a melanocyte membrane-bound glycoprotein (Pmel17/gp100) is released by ectodomain shedding.
Hoashi T, Tamaki K, Hearing VJ
FASEB journal : official publication of the Federation of American Societies for Experimental Biology 2010 Mar;24(3):916-30
FASEB journal : official publication of the Federation of American Societies for Experimental Biology 2010 Mar;24(3):916-30
Formation of Pmel17 amyloid is regulated by juxtamembrane metalloproteinase cleavage, and the resulting C-terminal fragment is a substrate for gamma-secretase.
Kummer MP, Maruyama H, Huelsmann C, Baches S, Weggen S, Koo EH
The Journal of biological chemistry 2009 Jan 23;284(4):2296-306
The Journal of biological chemistry 2009 Jan 23;284(4):2296-306
N-terminal domains elicit formation of functional Pmel17 amyloid fibrils.
Watt B, van Niel G, Fowler DM, Hurbain I, Luk KC, Stayrook SE, Lemmon MA, Raposo G, Shorter J, Kelly JW, Marks MS
The Journal of biological chemistry 2009 Dec 18;284(51):35543-55
The Journal of biological chemistry 2009 Dec 18;284(51):35543-55
The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis.
McGlinchey RP, Shewmaker F, McPhie P, Monterroso B, Thurber K, Wickner RB
Proceedings of the National Academy of Sciences of the United States of America 2009 Aug 18;106(33):13731-6
Proceedings of the National Academy of Sciences of the United States of America 2009 Aug 18;106(33):13731-6
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