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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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Premelanosome protein (PMEL) is a melanocyte lineage-associated glycoprotein encoded by the PMEL gene that functions as a key structural component of developing melanosomes where melanin deposition occurs. The protein is widely known in the literature as gp100 or Pmel17 and plays an essential role in the formation of fibrillar matrices that organize pigment polymerization within melanosomes. PMEL17 Antibody Glycosylated Protein recognizes this melanocyte-associated protein and supports studies examining the glycosylated gp100 protein species present in melanocytes and melanoma cells. The protein is frequently referred to as gp100, Pmel17, or premelanosome protein in the scientific literature and is widely used as a melanocytic lineage marker in melanoma and pigment cell biology research. In western blot studies, PMEL is synthesized as a heavily glycosylated precursor that migrates near approximately 100 kDa due to extensive glycosylation before undergoing additional proteolytic processing events during melanosome maturation.
PMEL belongs to a group of melanosome-associated proteins that regulate pigment granule formation in melanocytes. During early melanosome development, the glycosylated PMEL precursor is transported through the secretory pathway and delivered to premelanosomes where it undergoes proteolytic processing and structural rearrangement. These processing steps generate fibrillar structures that form the internal matrix of melanosomes and provide the scaffold upon which eumelanin and pheomelanin pigments accumulate during melanogenesis. Proper assembly of this matrix is essential for normal pigment synthesis and melanosome architecture.
The gp100 protein is extensively glycosylated, and this post-translational modification contributes to the higher apparent molecular weight typically observed in biochemical studies. Glycosylation influences PMEL folding, intracellular trafficking, and targeting to developing melanosomes. Because the glycosylated gp100 precursor represents one of the dominant forms detected during protein analysis, PMEL17 Antibody Glycosylated Protein provides a useful reagent for investigating gp100 glycoprotein expression and the role of glycosylated PMEL in melanosome biology.
Expression of PMEL is largely restricted to melanocytes and melanocytic tumors, making gp100 one of the most widely studied melanocyte lineage markers in melanoma biology. Researchers frequently analyze gp100 together with other melanocytic proteins such as Melan-A, tyrosinase, and MITF to characterize melanocyte differentiation and melanoma tumors. Detection of glycosylated gp100 protein species therefore helps investigators study pigment cell development, melanosome biogenesis, and melanoma-associated molecular pathways.
PMEL17 Antibody Glycosylated Protein detects the glycosylated gp100 protein present in melanocytes and melanoma cells and supports investigation of melanosome-associated structural proteins. By recognizing glycosylated PMEL species commonly observed during protein analysis, this antibody enables researchers to examine melanosome formation, pigment cell differentiation, and melanoma-associated pathways in experimental systems where gp100 expression provides important biological insight.
Optimal dilution of the PMEL17 antibody should be determined by the researcher.
A portion of amino acids 376-502 from the human protein was used as the immunogen for the PMEL17 antibody.
Store the PMEL17 antibody at 2-8oC (with azide) or aliquot and store at -20oC or colder (without azide).
gp100 antibody, Premelanosome protein antibody, Pmel17 antibody, Melanosome structural protein antibody
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