PRPF8 Antibody, FITC conjugated

Code CSB-PA744036LC01HU
Size US$166
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Product Details

Full Product Name
Rabbit anti-Homo sapiens (Human) PRPF8 Polyclonal antibody
Uniprot No.
Target Names
PRPF8
Alternative Names
220 kDa U5 snRNP specific protein antibody; 220 kDa U5 snRNP-specific protein antibody; Apoptosis regulated protein 1 antibody; Apoptosis regulated protein 2 antibody; HPRP8 antibody; p220 antibody; Pre mRNA processing factor 8 antibody; Pre mRNA-processing factor 8; S. cerevisiae; homolog of antibody; Pre-mRNA-processing-splicing factor 8 antibody; Precursor mRNA processing protein antibody; PRP8 antibody; PRP8 homolog antibody; PRP8 pre mRNA processing factor 8 homolog antibody; PRP8_HUMAN antibody; PRPC8 antibody; Prpf8 antibody; Retinitis pigmentosa 13 (autosomal dominant) antibody; RP13 antibody; SNRNP220 antibody; Splicing factor Prp8 antibody; U5 snRNP specific protein antibody; U5 snRNP specific protein (220 kD); ortholog of S. cerevisiae Prp8p antibody
Raised in
Rabbit
Species Reactivity
Human
Immunogen
Recombinant Human Pre-mRNA-processing-splicing factor 8 protein (2037-2170AA)
Immunogen Species
Homo sapiens (Human)
Conjugate
FITC
Clonality
Polyclonal
Isotype
IgG
Purification Method
>95%, Protein G purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, pH 7.4
Form
Liquid
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

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Target Background

Function
Plays role in pre-mRNA splicing as core component of precatalytic, catalytic and postcatalytic spliceosomal complexes, both of the predominant U2-type spliceosome and the minor U12-type spliceosome. Functions as a scaffold that mediates the ordered assembly of spliceosomal proteins and snRNAs. Required for the assembly of the U4/U6-U5 tri-snRNP complex, a building block of the spliceosome. Functions as scaffold that positions spliceosomal U2, U5 and U6 snRNAs at splice sites on pre-mRNA substrates, so that splicing can occur. Interacts with both the 5' and the 3' splice site.
Gene References into Functions
  1. Multiple genes contributing to the retinal dystrophy genotypes within a family were discovered using retinal gene-targeted next-generation sequencing. Families with noted examples of phenotypic variation or apparent non-penetrant individuals may offer a clue to suspect complex inheritance. PMID: 28761320
  2. Frame-shift mutations and nonconservative amino acid changes in PRPF8 typically cause severe clinical phenotypes. The conservative missense variant p.PRPF8-Arg2310Lys that is not altering the global charge of the C-terminal tail, and variants located at the basis of the C-terminal tail show milder clinical phenotypes, in accordance with functional data on PRPF8/SNRNP200 interactions in yeast. PMID: 29087248
  3. HSP90/R2TP chaperone system promotes the assembly of a key module of U5 snRNP while assuring the quality control of PRPF8. The proteomics data further reveal new interactions between R2TP and the tuberous sclerosis complex, pointing to a potential link between growth signals and the assembly of key cellular machines. PMID: 28515276
  4. influenza A virus upregulates cellular PRPF8 gene expression through viral NS1 protein and influenza virus polymerase basic protein 1 to increase virus production. PMID: 28110426
  5. Our findings exemplify the regulatory potential of changes in the core spliceosome machinery, which may be relevant to slow-onset human genetic diseases linked to PRPF8 deficiency PMID: 26392272
  6. Most importantly between Prp8 and nucleotides at the exon-intron junction. PMID: 26385511
  7. A mutation in a splicing factor PRPF8 that causes retinitis pigmentosa has a transcriptome-wide effect on mRNA splicing. PMID: 24969741
  8. Data suggest Enterovirus 3DPol (RNA-dependent RNA polymerase) enters nucleus via nuclear localization signal, targets pre-mRNA processing factor 8 (Prp8) to block pre-mRNA splicing/mRNA synthesis, and shuts off cellular transcription/translation. PMID: 24968230
  9. In the cytoplasm, Prp8 forms a precursor complex with U5 snRNA PMID: 23727230
  10. these data show how a Ski2-like RNA helicase Brr2 can be reversibly inhibited by a protein cofactor Prp8 that directly competes with RNA substrate binding. PMID: 23704370
  11. This is the first report of marked intrafamilial variability associated with mutations in the PRPF8 gene, including incomplete penetrance. PRPF8 mutations should be suspected in patients with autosomal dominant retinitis pigmentosa. PMID: 22039234
  12. RP-PRPF defects affect the stoichiometry of spliceosomal small nuclear RNAs. Depleting PRPF8 in human cell lines alters alternative splicing. PMID: 21378395
  13. Data screened retinitis pigmentosa patients for PRPF8 mutations and identified three new missense mutations, including the first documented mutation outside exon 42 and the first de novo mutation. PMID: 20232351
  14. Mutations in PRPC8 is associated with autosomal dominant retinitis pigmentosa PMID: 11910553
  15. mutations revealed a novel insertion and deletion in the last exon of a splicing factor gene, PRPF8. PMID: 12601059
  16. Nine mutations, six of which are novel, in the pre-mRNA splicing-factor genes PRPF3, PRPF8, and PRPF31, causing adRP have been identified in the Spanish population. PMID: 12714658
  17. The gene for apoptosis regulated protein 2 (ARP2) overexpressed in apoptosis induced prostate cancer cell line LNCaP was cloned. PMID: 15786732
  18. The PRPF8 gene mutation is associated with a mild phenotype in which cone function is partially preserved. PMID: 17061239
  19. The expanded Prp8 Jab1/MPN domain represents a pseudoenzyme converted into a protein-protein interaction platform and that dysfunction of this platform underlies Retinitis pigmentosa. PMID: 17317632
  20. The severe form of autosomal dominant retinitis pigmentosa (adRP) was caused by the PRPF8 H2309R variant, whereas the IVS41-4G-->A variant was benign. PMID: 18695108
  21. Crystal structures of corresponding portions of yeast and human Prp8 that interact with functional regions of the pre-mRNA were determined, revealing a phylogenetically conserved RNase H fold, augmented by Prp8-specific elements. PMID: 18843295
  22. The aim of this study was to use lymphoblast cell lines derived from retinitis pigmentosa patients to determine whether mutations in two of these splicing factors, PRPF8 and PRPF31, cause measurable deficiencies in pre-mRNA splicing. PMID: 19096719

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Involvement in disease
Retinitis pigmentosa 13 (RP13)
Subcellular Location
Nucleus. Nucleus speckle.
Tissue Specificity
Widely expressed.
Database Links

HGNC: 17340

OMIM: 600059

KEGG: hsa:10594

STRING: 9606.ENSP00000304350

UniGene: Hs.181368

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