Recombinant Human Melanocyte protein PMEL(PMEL),partial

Code CSB-YP021324HU
Size US$1298
Image
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

  • Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS Analysis result of CSB-YP021324HU could indicate that this peptide derived from Yeast-expressed Homo sapiens (Human) PMEL.

  • Based on the SEQUEST from database of Yeast host and target protein, the LC-MS/MS Analysis result of CSB-YP021324HU could indicate that this peptide derived from Yeast-expressed Homo sapiens (Human) PMEL.

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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names PMEL
Uniprot No. P40967
Research Area Metabolism
Alternative Names 95 kDa melanocyte specific secreted glycoprotein; 95 kDa melanocyte-specific secreted glycoprotein; D12S53E; gp100; M-beta; ME20; ME20 M/ME20 S; ME20-M; ME20-S; ME20M; ME20M/ME20S; ME20S; Melanocyte lineage specific antigen GP100 ; Melanocyte protein mel 17 ; Melanocyte protein Pmel 17; Melanocyte protein Pmel 17 precursor ; Melanocytes lineage-specific antigen GP100; Melanoma associated ME20 antigen; Melanoma gp100; Melanoma-associated ME20 antigen; Melanosomal matrix protein 17; Melanosomal matrix protein17; P1; p100; p26; PMEL 17; PMEL; PMEL_HUMAN; PMEL17; Premelanosome protein; Secreted melanoma-associated ME20 antigen; SI; SIL; SILV; Silver (mouse homolog) like; Silver homolog; Silver locus protein homolog; Silver, mouse, homolog of
Species Homo sapiens (Human)
Source Yeast
Expression Region 25-467aa
Target Protein Sequence KVPRNQDWLGVSRQLRTKAWNRQLYPEWTEAQRLDCWRGGQVSLKVSNDGPTLIGANASFSIALNFPGSQKVLPDGQVIWVNNTIINGSQVWGGQPVYPQETDDACIFPDGGPCPSGSWSQKRSFVYVWKTWGQYWQVLGGPVSGLSIGTGRAMLGTHTMEVTVYHRRGSRSYVPLAHSSSAFTITDQVPFSVSVSQLRALDGGNKHFLRNQPLTFALQLHDPSGYLAEADLSYTWDFGDSSGTLISRALVVTHTYLEPGPVTAQVVLQAAIPLTSCGSSPVPGTTDGHRPTAEAPNTTAGQVPTTEVVGTTPGQAPTAEPSGTTSVQVPTTEVISTAPVQMPTAESTGMTPEKVPVSEVMGTTLAEMSTPEATGMTPAEVSIVVLSGTTAAQVTTTEWVETTARELPIPEPEGPDASSIMSTESITGSLGPLLDGTATLRLV
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 49.0kDa
Protein Length Partial
Tag Info N-terminal 6xHis-tagged
Form Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA Please contact us to get it.

Target Data

Function Plays a central role in the biogenesis of melanosomes. Involved in the maturation of melanosomes from stage I to II. The transition from stage I melanosomes to stage II melanosomes involves an elongation of the vesicle, and the appearance within of distinct fibrillar structures. Release of the soluble form, ME20-S, could protect tumor cells from antibody mediated immunity.
Gene References into Functions
  1. To provide a source of dual-specific T cells for ACT, we generated a transgenic mouse strain expressing a CAR specific for Her2 in leukocytes under the control of the vav promoter .This CAR mouse strain was bred onto the pMEL transgenic mouse strain, expressing a TCR specific for the premelanosome protein, gp100 PMID: 27965307
  2. IMCgp100 (ImmTAC recognizing a peptide derived from the melanoma-specific protein, gp100, presented by HLA-A*0201) efficiently redirects and activates effector and memory cells from both CD8(+) and CD4(+) repertoires to kill melanoma cells. PMID: 28640942
  3. our work attempts to provide structural insights into the RPT domain structure and to elucidate its contribution to Pmel17 amyloid fibril formation. PMID: 26754844
  4. These findings help to clarify the mechanism of T-cell recognition of gp100 during melanoma responses and could direct the development of altered peptides for vaccination. PMID: 26917722
  5. Data suggest that the Kringle-like domain of PMEL facilitates post-endoplasmic reticulum processing of disulfide-bonded PMEL dimers and promotes formation of PMEL functional amyloid fibrillar structures within multivesicular endosomes. PMID: 26694611
  6. mutant N-terminally extended peptides exhibited significantly increased HLA-A*02:01 binding affinity and elicited CD8(+) T cell stimulation in vitro similar to the wtgp100209-217 epitope. PMID: 26507656
  7. Data indicate that repeat domain (RPT) derived from Pmel17 aggregation kinetics were influenced only by lysolipid-containing phospholipid vesicles. PMID: 25451784
  8. Melanosome-autonomous regulation of size and number: the OA1 receptor sustains PMEL expression. PMID: 24650003
  9. SIL-TAL1 rearrangement identifies a distinct subtype with inferior outcome which could allow for individual therapeutic stratification for T-ALL patients. PMID: 24040098
  10. the molecular basis for the distinct trafficking and morphogenetic properties of PMEL and GPNMB is the PKD domain PMID: 23452376
  11. Data indicat that the N-terminal region of PMEL/Pmel17 is essential for the formation of melanosomal fibrils. PMID: 23389629
  12. BACE2 cleaves the integral membrane form of PMEL within the juxtamembrane domain, releasing the PMEL luminal domain into endosomal precursors for the formation of amyloid fibrils and downstream melanosome morphogenesis. PMID: 23754390
  13. The recombinant Pmel 17 plasmids were right as we expected by DNA sequencing PMID: 23643172
  14. The most significant single-nucleotide polymorphism in the 12q13.2 locus is located immediately upstream of the promoter region of PMEL for vitiligo in Han Chinese. PMID: 22951725
  15. An antibody drug conjugate reactive with PMEL17 exhibits target-dependent tumor cell killing in vitro and in vivo. PMID: 22613716
  16. This is a review on two human amyloidogenic polypeptides, one associated with Parkinson's disease, alpha-synuclein (alpha-syn), and the other important for melanin synthesis, the repeat domain (RPT) from Pmel17.[Review] PMID: 21993592
  17. MART-1- and gp100-expressing and -non-expressing melanoma cells are equally proliferative in tumors and clonogenic in vitro. PMID: 21993558
  18. Pmel17 repeat domain fibril dissolution is pH dependent PMID: 22092386
  19. the DW and HoSi mutations alter PMEL TMD oligomerization and/or association with membranes, with consequent formation of aberrantly packed fibrils. PMEL mutations can model the conversion between physiological and pathological amyloid PMID: 21949659
  20. the multistep processing of Pmel17 begins with an early cleavage during secretion that primes the protein for later functional processing. PMID: 21247888
  21. Repeat domains of melanosome matrix protein Pmel17 orthologs form amyloid fibrils at the acidic melanosomal pH. PMID: 21148556
  22. Data suggest that intramelanosomal pH regulates Pmel17 amyloid formation and its subsequent dissolution in vivo. PMID: 21106765
  23. N-terminal region and the polycystic kidney disease-like domain is highly crucial for endoplasmic reticulum export, subcellular targeting, and fibril formation by Pmel17 and thus for establishing functional melanosomes. PMID: 20231267
  24. Data conclude that sPmel17 is released by regulated proteolytic ectodomain shedding. PMID: 19884326
  25. we identified the gp100/pMel17 melanosomal protein as the shared antigen recognized by three independent CD8+ CTL clones in HLA-A*6801-restricted fashion. PMID: 12135425
  26. Data show that MITF appears to regulate the expression of the SILV and MLANA genes. PMID: 12819038
  27. Antigen-specific T lymphocyte reactivity to gp100 peptides was seen in 15 of 17 (88%) vitiligo patients, with many demonstrating very high reactivity at levels comparable with those observed with common recall antigens PMID: 12925214
  28. truncation of the repeat region within Pmel17 alters either fibrillogenic activity or the interaction of Pmel17 with melanin intermediates PMID: 14632201
  29. CD8 T lymphocytes recognized a nonameric peptide on melanoma cells that comprises two noncontiguous segments of melanocytic glycoprotein gp100(PMEL17); the production of this peptide involves the excision of four amino acids and splicing of the fragments PMID: 15001714
  30. PMEL17 is rapidly processed in the endoplasmic reticulum and glycosylated in the early Golgi PMID: 15096515
  31. Data suggest that MART-1 is indispensable for Pmel17 function and thus plays an important role in regulating mammalian pigmentation. PMID: 15695812
  32. Data show that the melanosomal protein Pmel17 is sorted into intralumenal vesicles by a mechanism that is dependent upon lumenal determinants and conserved in non-pigment cells. PMID: 16516837
  33. the RPT domain of PMEL17/GP100 is essential for its function in generating the fibrillar matrix of melanosomes and that the luminal domain is necessary for its correct processing and trafficking to those organelles PMID: 16682408
  34. Pmel17 is a critical component of melanogenesis. PMID: 16704461
  35. These data reveal a dual sorting defect in a natural mutant of Pmel17 and support a requirement of endocytic trafficking in Pmel17 fibril formation. PMID: 16760433
  36. addition of sialic acid affects the stability and sorting of Pmel17 and reduces pigmentation PMID: 17303571
  37. GTP-bound form of Rab7 promotes melanogenesis through the regulation of gp100 maturation in melanoma cells. PMID: 17625594
  38. Premelanosome amyloid-like fibrils are composed of only golgi-processed forms of Pmel17 that have been proteolytically processed in endosomes PMID: 17991747
  39. Measurement of Melan-A, gp100, MAGE-3, MIA and tyrosinase represents a prognostic factor and a method for early detection of metastasis and treatment response of melanoma patients. PMID: 18181974
  40. Tyrosinase-, gp100-, or TRP-2-specific CD8(+) T cells could not be identified in the peripheral blood of individuals with vitiligo. PMID: 18337837
  41. Nuclear to non-nuclear Pmel17/gp100 expression (HMB45 staining) is a discriminator between benign and malignant melanocytic lesions. PMID: 18552823
  42. MHC class II presentation of gp100 epitopes in melanoma cells requires the function of conventional endosomes and is influenced by melanosomes. PMID: 19017974
  43. release of the Pmel17 ectodomain, which is critical for melanin amyloidogenesis, is initiated by S2 cleavage at a juxtamembrane position PMID: 19047044
  44. the repeat domain of the melanosome fibril protein Pmel17 forms the amyloid core promoting melanin synthesis PMID: 19666488
  45. N-terminal domains elicit formation of functional Pmel17 amyloid fibrils. PMID: 19840945
  46. Details and validates the multiple sorting pathways used by the silver protein to reach melanosomes. It identifies the specific adaptor proteins involved and sheds light on the polarization of the melanocyte. PMID: 16492709
  47. Detailed analysis of the post-translational modifications and their effect over the processing and trafficking of the silv gene. PMID: 17303571
  48. The PMEL17 (SILV) protein catalyzes the polymerization of 5,6-dihydroxyindole-2-carboxylic acid to melanin. PMID: 8617263
  49. Pmel17 is proteolytically processed in a post-Golgi compartment and is enriched in multivesicular endosomes prior to incorporation in stage II melanosomes. PMID: 11694580
  50. A proteolytic fragment of Pmel17, generated by proprotein convertase cleavage, is the major biogenetic component of the underlying fibrillar matrix of melanosome precursors. PMID: 12732614

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Subcellular Location Endoplasmic reticulum membrane, Single-pass type I membrane protein, Golgi apparatus, Melanosome, Endosome, multivesicular body
Protein Families PMEL/NMB family
Tissue Specificity Preferentially expressed in melanomas. Some expression was found in dysplastic nevi. Not found in normal tissues nor in carcinomas. Normally expressed at low levels in quiescent adult melanocytes but overexpressed by proliferating neonatal melanocytes and
Database Links

HGNC: 10880

OMIM: 155550

KEGG: hsa:6490

STRING: 9606.ENSP00000402758

UniGene: Hs.95972

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