| Synonym | PMEL17 | 
                
                    | Species | Human | 
                
                    | Protein Accession | Met186-Melanocyte Protein PMEL 17 (185-193) (hu product) | 
                
                    | Purity | Greater than 95% as determined by SDS-PAGE | 
                
                    | Endotoxin Level | Less than 1.0 EU per μg of the protein as determined by the LAL method | 
                
                    | Biological Activity | Not determined | 
                
                    | Expression System | E. coli | 
                
                    | Fusion Tag | None | 
                
                    | Predicted Molecular Mass | Approximately 9 kDa | 
                
                    | Formulation | Lyophilized from a 0.2 μm filtered solution of 20 mM Tris, 150 mM NaCl, pH 8.0 | 
                
                    | Reconstitution | We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the
                        bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a
                        concentration of 0.1-1.0 mg/mL. | 
                
                    | Storage & Stability | Store at -20°C. Please refer to product insert upon arrival for more detailed information. | 
            
            FAQ
            
                What is the importance of the Met186-Melanocyte Protein PMEL 17 (185-193) peptide in
                research?
The Met186-Melanocyte Protein PMEL 17 (185-193) peptide is a fascinating molecule that
                has gained significant attention in the realm of biomedical research, primarily due to its role in the
                functioning of melanocytes, the cells responsible for pigment production in the human body. This peptide
                is crucial in studying melanin synthesis, the process by which our bodies produce melanin, the pigment
                responsible for the color of skin, eyes, and hair. Melanin is more than just a cosmetic pigment; it
                plays a vital role in protecting skin cells from ultraviolet radiation damage. Understanding the
                mechanisms underlying melanin production and regulation can lead to breakthroughs in treating
                pigmentation disorders like vitiligo and melanoma, a severe form of skin cancer.
Researching this
                specific protein segment, Met186-Melanocyte Protein PMEL 17 (185-193), has opened avenues for
                understanding how various mutations or alterations in the protein can affect the pigmentation processes.
                Scientists are exploring its role in the aggregation of melanin precursors, which is a critical step in
                pigment formation. Identifying how changes in this peptide affect the pathway can provide insights into
                pathological states that lead to hyperpigmentation or hypopigmentation. Furthermore, this peptide can
                serve as a model for developing new strategies to influence melanin production, presenting potential
                therapeutic avenues not only for pigmentation disorders but also for designing novel sun-protection
                strategies by enhancing skin’s natural melanin synthesis.
Moreover, PMEL 17's role is not limited
                to pigmentation; it has implications in immune responses. PMEL 17 peptides can be recognized by the
                immune system, thus offering a potential target for immune-modulation therapies. This has particular
                relevance in cancer immunotherapy, where understanding how cancer cells might present these or similar
                peptides to evade immune responses can lead to the development of new treatment modalities. Innovatively
                utilizing peptides like Met186-Melanocyte Protein PMEL 17 (185-193) in research could thus contribute
                toward significant advancements in both dermatological and oncological therapeutic strategies. Hence,
                for researchers focusing on pigment biology or immunotherapy, this peptide offers a valuable tool for
                advancing our understanding and opening new investigative pathways.
How does the
                Met186-Melanocyte Protein PMEL 17 (185-193) operate within melanocytes?
Within melanocytes, the
                Met186-Melanocyte Protein PMEL 17 (185-193) peptide plays a pivotal role in the complex process of
                melanosome development and maturation. Melanosomes are organelles where melanin synthesis occurs, and
                their biogenesis is not only crucial for determining pigment production but also for understanding
                processes like cellular differentiation and developmental biology within these specialized
                cells.
PMEL, which spans a broader range beyond the 185-193 amino acid sequence, goes through
                multiple stages of processing and trafficking that are instrumental for its function. Made initially as
                an immature precursor, PMEL undergoes a complex cleavage process that results in several fragments. The
                segment Met186-Melanocyte Protein PMEL 17 (185-193) is part of this sophisticated maturation pathway
                within the lumen of the endoplasmic reticulum and Golgi apparatus before being transported to
                melanosomes. This peptide sequence is involved in creating a fibrillar matrix within melanosomes,
                crucial for melanin polymerization. The structural framework provided by PMEL is essential for the
                deposition of melanin, catalyzing the buildup of pigments in a controlled manner and ensuring the
                correct formation and stabilization of melanosomes.
Moreover, the mutation or dysregulation of
                PMEL and its peptide segments, such as Met186-Melanocyte Protein PMEL 17 (185-193), can lead to
                significant implications for melanin synthesis, impacting skin coloration and contributing to disorders
                like oculocutaneous albinism or melanosome-related dysfunctions. The study of how this peptide interacts
                with other biological molecules offers deeper insights into the cellular architecture of pigment cells
                and highlights the importance of protein trafficking and proteolysis as central avenues of research in
                understanding pigmentation.
In summary, the Met186 portion of PMEL 17 is more than just a passive
                component within the melanosome formation; it is an active participant in the assembly of the key
                structural framework that supports pigmentation. Understanding its precise functions, pathways, and
                interactions remains a critical focus for researchers aiming to manipulate or rectify pigment-related
                issues in medical science.
What potential medical applications stem from understanding the
                Met186-Melanocyte Protein PMEL 17 (185-193) peptide?
Understanding the role and functionality of
                the Met186-Melanocyte Protein PMEL 17 (185-193) peptide opens several promising avenues for therapeutic
                applications, particularly in dermatology and oncology. The peptide's involvement in melanin synthesis
                and immune recognition makes it a prime target for novel treatments of various conditions.
In
                dermatology, the potential applications of this peptide lie predominantly in the treatment of
                pigmentation disorders such as vitiligo, hyperpigmentation, and albinism. By elucidating the molecular
                mechanics of PMEL 17 within melanosomes, researchers can develop drugs or interventions that alter
                melanin production. For instance, in vitiligo, where pigment-producing melanocytes are attacked and
                destroyed, understanding PMEL's role could lead to approaches that enhance the regeneration or
                protection of these cells, offering patients more effective and long-lasting solutions for
                repigmentation.
Another significant field of application is in the realm of oncological research.
                The immune properties of PMEL 17 make it particularly useful in developing cancer immunotherapies.
                Cancer cells, especially in melanoma, often exploit self-proteins to escape immune detection. By
                manipulating PMEL 17 peptide's presentation on tumor cells, it might be possible to improve immune
                system recognition and response to cancer cells. Therapies could be designed to boost a body's natural
                immune response against tumor cells presenting PMEL fragments, making it a compelling target for
                vaccine-based treatments or immune checkpoint therapies.
Furthermore, understanding
                Met186-Melanocyte Protein PMEL 17 (185-193) can aid in designing protective strategies against UV
                radiation by enhancing melanin synthesis, offering a natural method for boosting the skin's defense
                mechanism against harmful sun exposure. These insights into melanin's natural protective qualities can
                lead to new methods for skin cancer prevention or reducing UV-induced damage, appealing both to the
                medical community and as consumer products in the skincare industry.
In conclusion, the study of
                the Met186 segment of PMEL 17 provides more than just an understanding of pigmentation biology; it lays
                the groundwork for novel therapeutic strategies that can significantly impact the treatment and
                management of skin disorders, cancer therapies, and protective dermatological applications, making it an
                essential focus for continued research and development in medical science.
Can you explain the
                biochemical interactions involving Met186-Melanocyte Protein PMEL 17 (185-193) and its
                implications?
Biochemically, the Met186-Melanocyte Protein PMEL 17 (185-193) peptide is an
                integral part of the intricate network of interactions involved in melanosome maturation and melanin
                synthesis. PMEL protein requires precise cleavage into smaller fragments, like Met186-Melanocyte
                Protein, to form the fibrillar matrix within melanosomes, providing a scaffold for melanin
                polymerization. 
One of the critical biochemical interactions of PMEL involves its role in
                amyloid formation, which, in the context of melanosomes, is non-pathogenic and crucial for its function.
                Unlike other amyloids, which are typically associated with pathological states such as Alzheimer's
                disease, PMEL fibrils help structure the melanosome interior. This unique arrangement allows the storage
                and stabilization of melanin intermediates, catalyzing their polymerization into mature melanin
                efficiently. These amyloid fibrils are resistant to proteolytic digestion and provide the framework
                around which melanin precursors aggregate, efficiently converting them into stable pigment,
                demonstrating a beneficial aspect of amyloid biology.
Moreover, this peptide segment interacts
                with a host of other proteins involved in melanosome biogenesis and transport processes within the cell.
                Interactions with membrane-bound transporters and enzymes, such as tyrosinase and related proteins, are
                essential for the distribution of melanin-producing complexes to the forming melanosomes. These
                interactions are crucial for ensuring that melanin is synthesized only in the correct cell compartments,
                safeguarding cellular structures from potential oxidative stress caused by melanin precursors and
                intermediates.
In terms of implications, understanding these biochemical interactions gives
                insight into how variations or disruptions in these pathways could lead to melanin-related disorders,
                such as hypo- or hyperpigmentation. By leveraging this understanding, scientists can design
                interventions that target specific interactions and modulate melanin production, potentially correcting
                abnormal pigmentation processes. Additionally, further exploring these interactions provides research
                models for studying similar protein interactions in neurodegenerative diseases, wherein amyloid fibril
                formation leads to pathological conditions rather than beneficial biological processes, underscoring the
                diverse implications of Met186-Melanocyte Protein PMEL 17 (185-193) in health and disease.