Recombinant Human Myelin proteolipid protein(PLP1)-VLPs

Code CSB-MP018202HU
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Product Details

Target Names PLP1
Uniprot No. P60201
Research Area Others
Alternative Names PLP1; PLP; Myelin proteolipid protein; Lipophilin
Species Homo sapiens (Human)
Source Mammalian cell
Expression Region 2-277aa
Target Protein Sequence GLLECCARCLVGAPFASLVATGLCFFGVALFCGCGHEALTGTEKLIETYFSKNYQDYEYLINVIHAFQYVIYGTASFFFLYGALLLAEGFYTTGAVRQIFGDYKTTICGKGLSATVTGGQKGRGSRGQHQAHSLERVCHCLGKWLGHPDKFVGITYALTVVWLLVFACSAVPVYIYFNTWTTCQSIAFPSKTSASIGSLCADARMYGVLPWNAFPGKVCGSNLLSICKTAEFQMTFHLFIAAFVGAAATLVSLLTFMIAATYNFAVLKLMGRGTKF
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Tag Info C-terminal 10xHis-tagged
If you have specified tag type, please tell us and we will check if it’s possible to develop.
Form Lyophilized powder
Note: We will default ship it in lyophilized form with normal bule ice packs. However, if you request to ship in liquid form, it needs to be shipped with dry ice, please communicate with us in advance and extra fees for dry ice and dry ice box will be charged.
Buffer Lyophilized from PBS, 6% Trehalose, pH 7.4
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°C/-80°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.
Note: 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 the protein at -20°C/-80°C upon receiving it, and ensure to avoid repeated freezing and thawing, otherwise, it will affect the protein activity.
Datasheet & COA Please contact us to get it.

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Target Background

Function
This is the major myelin protein from the central nervous system. It plays an important role in the formation or maintenance of the multilamellar structure of myelin.
Gene References into Functions
  1. three single nucleotide polymorphisms in PLP1 that were associated with interhemispheric integration via the corpus callosum in a previous study also are relevant for functional hemispheric asymmetries. PMID: 29435918
  2. This study demonstrated that the plp and alpha-synuclein transgenic mouse model of multiple system atrophy showed the Progressive striatonigral degeneration. PMID: 29298733
  3. Pelizaeus-Merzbacher disease (PMD) is an X-linked disorder caused by mutations in the PLP1 gene, which encodes the proteolipid protein of myelinating oligodendroglia. PMID: 29478609
  4. Proteolipid protein 1 and contactin 1 gene variation modulates interhemispheric integration PMID: 27864734
  5. Using whole exome sequencing, a novel pathogenic PLP1 missense mutation c.251C > A (p.Ala84Asp) was detected in a Moroccan family, allowing a diagnosis of Pelizaeus-Merzbacher Disease. PMID: 29486744
  6. down-regulated in cord blood by prenatal smoking PMID: 28130959
  7. Authors investigated the disease progression in mouse models carrying PLP1 point mutations previously found in patients displaying clinical features of multiple sclerosis. These mouse models show loss-of-function of PLP1 associated with neuroinflammation. PMID: 28173160
  8. Review focusing on sequences in hPLP1 intron 1 DNA deemed important for hPLP1 gene activity as well as a couple of "human-specific" supplementary exons within the first intron which are utilized to generate novel splice variants, and the potential role that these sequences may play in PLP1-linked disorders. PMID: 28735559
  9. it seems that the epitopes of some microorganisms mimicking PLP such as PLP58-74 might have a potential role in the initiation of Multiple Sclerosis. PMID: 27917626
  10. Human induced pluripotent stem cells-derived oligodendrocytes from 12 individuals with Pelizaeus-Merzbacher and identified individual and shared defects in PLP1 mRNA expression and splicing, oligodendrocyte progenitor development, and oligodendrocyte morphology and capacity for myelination. PMID: 28366443
  11. report a novel mutation of the PLP1 gene in two siblings with Pelizaeus-Merzbacher disease associated with a rare and protean neuroimaging finding of optic nerve enlargement PMID: 27793435
  12. Identification and functional study of novel PLP1 mutations in Chinese patients with Pelizaeus-Merzbacher disease. We identified PLP1 mutations in seven male patients with PMD. PMID: 25491635
  13. In major depressive disorder there was a significantly reduced expression of PLP1 mRNA. PMID: 25930075
  14. Study investigated 17 unrelated Pelizaeus-Merzbacher disease subjects with copy number gains at the PLP1 locus including triplication and quadruplication of specific genomic intervals-16/17 were found to have a duplication-inverted triplication-duplication rearrangement product. PMID: 25749076
  15. Myelin proteolipid protein is critical to regulating oligodendrocyte progenitor cell migration. PMID: 26311781
  16. PLP1 splicing mutations may result in a wide variety of disease phenotypes through a combination of multiple molecular pathogenic mechanisms. PMID: 23771846
  17. this study provides new insight into the genotype-phenotype correlations of patients with PLP1 splice-site mutations. PMID: 23711321
  18. Insertion of an extra copy of Xq22.2 into 1p36 results in functional duplication of the PLP1 gene in a girl with classical Pelizaeus-Merzbacher disease. PMID: 26329556
  19. Data strongly suggest that a secondary structure within intron 3 is important for controlling regulation of the PLP1 alternative splice and that patient mutations can cause Pelizaeus-Merzbacher disease by disrupting this structure. PMID: 24890387
  20. Mutations found in the PLP1 gene are the cause of PMD in around 20% of the patients in this series. PMID: 23347225
  21. Data suggest transmembrane segment of PLP contains multiple helix-helix interaction motifs that play role in ability of PLP to form dimers/oligomers; alteration of local hydrophobicity affects both helix-helix interaction and segment alpha-helicity. PMID: 24857611
  22. show that the presence of the c.436C>G mutation served to introduce regulatory motifs that appear to be responsible for the perturbed splicing pattern that led to loss of the major PLP transcript PMID: 24019930
  23. Our clinical and molecular findings showed that the phenotypic spectrum resulting from PLP1 mutations seems to be broader in patients with the PLP1 gene duplication compared to patients with both nonsense and missense mutation. PMID: 24519770
  24. report a novel PLP1 missense mutation (c.88G>C) in a family from Argentina. This mutation is in a highly conserved transmembrane domain of PLP1 and the mutant protein was found to be retained in the endoplasmic reticulum when expressed in vitro PMID: 24103481
  25. data show that complex duplications involving PLP1 are not uncommon, can be detected at the level of genome resolution afforded by clinical aCGH and duplication and inversion can be produced in the same event. PMID: 21623770
  26. The PLP1 gene has a more complex role in human brain development, exceeding its structural function in myelin formation. PMID: 22511562
  27. PLP1 mutants inhibit Golgi apparatus to endoplasmic reticulum trafficking and have a role in pathogenesis of Pelizaeus-Merzbacher disease PMID: 23344956
  28. In transfected cells, oligodendrocytes & brain, PLP exists as a monomer or a disulfide-linked dimer via Cys108. Isoform DM20 is usually a monomer. Mutants causing Pelizaeus-Merzbacher disease form disulfide-linked, high-MW aggregates. PMID: 22902553
  29. the underlying effect of the partial PLP1 duplication identified in this study was different from other PLP1 alterations including a typical duplication and a missense mutation. PMID: 22695888
  30. expression of PLP1 in oligodendrocytes markedly inhibits their differentiation, and that this inhibitory effect is effectively improved by inhibition of extracellular signal-regulated kinase activity. PMID: 22750001
  31. A novel PLP1 mutation was found in a family presenting with X-linked recessive Hereditary Spastic Paraplegia. PMID: 22343157
  32. Inflammation in mammals with increased Plp1 gene dosage may also contribute to axonal degeneration described in patients and transgenic rodents with PLP1 increased gene dosage. PMID: 20885931
  33. Data suggest that a defective disulfide bond in proteolipid protein 1 could be important in the pathogenesis of Pelizaeus-Merzbacher disease. PMID: 21177054
  34. study of patients with PLP1-related disorders; PLP1 gene duplications were identified in 24 of unrelated patients whereas a variety of intragenic PLP1 mutations were found in the remaining 14 patients; of the 14 different intragenic lesions, 11 were novel PMID: 21679407
  35. Results prove for the first time the interaction of PLP and MAL2 in oligodendrocytic cells, supporting the transcytotic model of PLP transport previously suggested. PMID: 21573057
  36. Central nervous system myelination is compromised by overexpression of proteolipid protein PLP/DM20 in a transgenic mouse model of Pelizaeus-Merzbacher disease. PMID: 20629189
  37. G Run-mediated recognition of proteolipid protein and DM20 5' splice sites by U1 small nuclear RNA is regulated by context and proximity to the splice site. PMID: 21127064
  38. A patient with Pelizaeus-Merzbacher disease has duplication of all 7 exons of the PLP1 gene. This duplication was inherited from the patient's mother, who is an unaffected carrier of the mutation. PMID: 21082496
  39. PLP1 gene mutations cause hereditary spastic paraplegia. PMID: 19955111
  40. These results suggest for the first time that PLP may have functions in humans not only in oligodendrocytes but also in neurons and could be implicated in axono-glial communication PMID: 20036320
  41. his study presented new mutation and variable sizes of duplications in patient with Pelizaeus-Merzbacher disease. PMID: 19328639
  42. report on a family of two young boys and their mother who share the same unusual 4-bp deletion of the PLP1 gene: c51_54 del TTCC, causing truncation of the PLP1 in exon 2. The brain MRI appearances in this unique deletion, using MR imaging, are described. PMID: 20186781
  43. A242V PLP1 mutant, which causes severe Pelizaeus-Merzbacher disease, was more stable and accumulated at the endoplasmic-reticulum. PMID: 19825935
  44. PLP1 deletions are likely caused by nonhomologous end joining PMID: 12297985
  45. A PLP splicing abnormality is associated with an unusual presentation of PMD. PMID: 12325077
  46. a study of the mutations in Pelizaeus Merzbacher disease. PMID: 12491939
  47. Decreased expression of a number of myelin-related genes, including myelin basic protein (MBP), proteolipid protein (PLP), and myelin-associated oligodendrocyte basic protein (MOBP) was noted in nucleus accumbens of cocaine abusers PMID: 15009677
  48. A Korean boy diagnosed with SPG2 caused by a mutation that results in a Pro215Leu substitution in the second extracellular domain. PMID: 15450775
  49. Mutations are associated with Pelizaeus-Merzbacher disease and spastic paraplegia type 2. (review) PMID: 15627202
  50. the genetic polymorphisms within PLP1 in male are likely to confer an increased susceptibility to schizophrenia in the Chinese population. PMID: 15694262

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Involvement in disease Leukodystrophy, hypomyelinating, 1 (HLD1); Spastic paraplegia 2, X-linked (SPG2)
Subcellular Location Cell membrane; Multi-pass membrane protein. Myelin membrane.
Protein Families Myelin proteolipid protein family
Database Links

HGNC: 9086

OMIM: 300401

KEGG: hsa:5354

STRING: 9606.ENSP00000305152

UniGene: Hs.1787

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