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PMEL encodes a melanocyte-specific type I transmembrane glycoprotein.
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To provide a source of dual-specific T cells for ACT, we generated a transgenic mouse strain expressing a CAR specific for Her2 (show ERBB2 Proteins) in leukocytes under the control of the vav (show VAV1 Proteins) promoter .This CAR mouse strain was bred onto the pMEL transgenic mouse strain, expressing a TCR specific for the premelanosome protein, gp100
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 (show CD8A Proteins)(+) and CD4 (show CD4 Proteins)(+) repertoires to kill melanoma cells.
our work attempts to provide structural insights into the RPT domain structure and to elucidate its contribution to Pmel17 amyloid fibril formation.
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.
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.
mutant N-terminally extended peptides exhibited significantly increased HLA-A*02:01 binding affinity and elicited CD8 (show CD8A Proteins)(+) T cell stimulation in vitro similar to the wtgp100209-217 epitope.
Data indicate that repeat domain (RPT) derived from Pmel17 aggregation kinetics were influenced only by lysolipid-containing phospholipid vesicles.
Melanosome-autonomous regulation of size and number: the OA1 (show GPR143 Proteins) receptor sustains PMEL expression.
SIL-TAL1 (show TAL1 Proteins) rearrangement identifies a distinct subtype with inferior outcome which could allow for individual therapeutic stratification for T-ALL patients.
the molecular basis for the distinct trafficking and morphogenetic properties of PMEL and GPNMB is the PKD (show PRKD1 Proteins) domain
Six solid colors occur in Highland cattle: black, dun, silver dun and red, yellow, and white. These six coat colors are explained by a non-epistatic interaction of the genotypes at the MC1R (show MSHR Proteins) and PMEL genes.
no convincing recombination events were found between the SILV c.64A>G mutation and the Dc locus
the complex expression pattern of the bovine SILV gene in pigmented and non-pigmented tissues
These findings indicated that overexpression of miR (show MLXIP Proteins)-136 inhibits melanoma cell epithelial-mesenchymal transition, proliferation, migration, invasion, and promotes apoptosis by targetting PMEL through down-regulation of the Wnt (show WNT2 Proteins) signaling pathway.
Prophylactic and therapeutic vaccinations of mice with MCMV-gp100KGP effectively protected mice from highly aggressive lung B16-F10 (show F10 Proteins) melanoma, and the protection was mediated by gp100-specific CD8 (show CD8A Proteins)(+) T cells
the BACE1 (show BACE Proteins) homologue BACE2 (show BACE2 Proteins) processes PMEL to generate functional amyloids
A long-peptide vaccine formulation of 20-mer (show ERH Proteins) synthetic peptide elicits gp100-specific CD8 (show CD8A Proteins) T cells from the endogenous repertoire.
Despite a mild effect on visible pigmentation, inactivation of Pmel led to a substantial reduction in eumelanin content in hair, which demonstrates that PMEL has a critical role for maintaining efficient epidermal pigmentation.
Pmel17 gene expression is Microphthalmia-associated transcription factor (show MITF Proteins)-dependent in the mouse embryo.
These data reveal a dual sorting defect in a natural mutant of Pmel17 and support a requirement of endocytic trafficking in Pmel17 fibril formation.
This gene encodes a melanocyte-specific type I transmembrane glycoprotein. The encoded protein is enriched in melanosomes, which are the melanin-producing organelles in melanocytes, and plays an essential role in the structural organization of premelanosomes. This protein is involved in generating internal matrix fibers that define the transition from Stage I to Stage II melanosomes. This protein undergoes a complex pattern of prosttranslational processing and modification that is essential to the proper functioning of the protein. A secreted form of this protein that is released by proteolytic ectodomain shedding may be used as a melanoma-specific serum marker. Alternate splicing results in multiple transcript variants.
melanocyte protein PMEL
, melanocyte protein Pmel 17
, melanocyte protein mel 17
, melanocytes lineage-specific antigen GP100
, melanoma-associated ME20 antigen
, melanosomal matrix protein17
, silver locus protein homolog
, silver, mouse, homolog of
, silver homolog
, retinal pigment epithelial-specific protein
, melanocyte protein pmel 17
, silver locus protein
, 115 kDa melanosomal matrix protein
, PMEL17 protein