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Goat Anti-Silver homologue / Pmel 17 Antibody
Peptide-affinity purified goat antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IF, Pep-ELISA |
|---|---|
| Primary Accession | P40967 |
| Other Accession | NP_008859, 6490, 20431 (mouse), 362818 (rat) |
| Reactivity | Human |
| Predicted | Mouse, Rat |
| Host | Goat |
| Clonality | Polyclonal |
| Concentration | 100ug/200ul |
| Isotype | IgG |
| Calculated MW | 70255 Da |
| Gene ID | 6490 |
|---|---|
| Other Names | Melanocyte protein PMEL, ME20-M, ME20M, Melanocyte protein Pmel 17, Melanocytes lineage-specific antigen GP100, Melanoma-associated ME20 antigen, P1, P100, Premelanosome protein, Silver locus protein homolog, M-alpha, 95 kDa melanocyte-specific secreted glycoprotein, P26, Secreted melanoma-associated ME20 antigen, ME20-S, ME20S, M-beta, PMEL, D12S53E, PMEL17, SILV |
| Format | 0.5 mg IgG/ml in Tris saline (20mM Tris pH7.3, 150mM NaCl), 0.02% sodium azide, with 0.5% bovine serum albumin |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Goat Anti-Silver homologue / Pmel 17 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | PMEL |
|---|---|
| Synonyms | D12S53E, PMEL17, SILV |
| Function | Forms physiological amyloids that play a central role in melanosome morphogenesis and pigmentation. The maturation of unpigmented premelanosomes from stage I to II is marked by assembly of processed amyloidogenic fragments into parallel fibrillar sheets, which elongate the vesicle into a striated ellipsoidal shape. In pigmented stage III and IV melanosomes, the amyloid matrix serves as a platform where eumelanin precursors accumulate at high local concentrations for pigment formation. May prevent pigmentation-associated toxicity by sequestering toxic reaction intermediates of eumelanin biosynthesis pathway. |
| Cellular Location | Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus, cis-Golgi network membrane; Single-pass type I membrane protein. Endosome, multivesicular body. Melanosome Extracellular vesicle. Secreted. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065) Localizes predominantly to intralumenal vesicles (ILVs) within multivesicular bodies. Associates with ILVs found within the lumen of premelanosomes and melanosomes and particularly in compartments that serve as precursors to the striated stage II premelanosomes (PubMed:12643545, PubMed:11694580). Sorted to stage I melanosomes following its processing in the ER and cis-Golgi (PubMed:15096515) Transiently expressed at the cell surface before targeting to early melanosomes (PubMed:30988362, PubMed:16760433). Colocalizes with BACE2 in stage I and II melanosomes (PubMed:23754390). Colocalizes with CD63 and APOE at exosomes and in intraluminal vesicles within multivesicular endosomes (PubMed:26387950, PubMed:21962903) |
| Tissue Location | Normally expressed at low levels in quiescent adult melanocytes but overexpressed by proliferating neonatal melanocytes and during tumor growth. Overexpressed in melanomas. Some expression was found in dysplastic nevi. |
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Provided below are standard protocols that you may find useful for product applications.
References
Endoplasmic reticulum export, subcellular distribution, and fibril formation by Pmel17 require an intact N-terminal domain junction. Leonhardt RM, et al. J Biol Chem, 2010 May 21. PMID 20231267.
The secreted form of a melanocyte membrane-bound glycoprotein (Pmel17/gp100) is released by ectodomain shedding. Hoashi T, et al. FASEB J, 2010 Mar. PMID 19884326.
N-terminal domains elicit formation of functional Pmel17 amyloid fibrils. Watt B, et al. J Biol Chem, 2009 Dec 18. PMID 19840945.
The repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis. McGlinchey RP, et al. Proc Natl Acad Sci U S A, 2009 Aug 18. PMID 19666488.
Formation of Pmel17 amyloid is regulated by juxtamembrane metalloproteinase cleavage, and the resulting C-terminal fragment is a substrate for gamma-secretase. Kummer MP, et al. J Biol Chem, 2009 Jan 23. PMID 19047044.
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