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Recombinant Saccharomyces cerevisiae Pre-mRNA-splicing factor 8 (PRP8), partial

Recombinant Saccharomyces cerevisiae Pre-mRNA-splicing factor 8 (PRP8), partial

Code	CSB-YP333785SVG
MSDS	MSDS
Size	Pls inquire
Source	Yeast
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Code	CSB-EP333785SVG
MSDS	MSDS
Size	Pls inquire
Source	E.coli
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Code	CSB-EP333785SVG-B
MSDS	MSDS
Size	Pls inquire
Source	E.coli
Conjugate	Avi-tag Biotinylated E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code	CSB-BP333785SVG
MSDS	MSDS
Size	Pls inquire
Source	Baculovirus
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Code	CSB-MP333785SVG
MSDS	MSDS
Size	Pls inquire
Source	Mammalian cell
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Product Details
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Customer Reviews and Q&A
Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

PRP8

Uniprot No.

P33334

Alternative Names

PRP8; DBF3; DNA39; RNA8; SLT21; USA2; YHR165CPre-mRNA-splicing factor 8

Species

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Protein Length

Partial

Tag Info

Tag type will be determined during the manufacturing process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

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 before Lyophilization

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℃/-80℃. 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/-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: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet

Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function

Functions as a scaffold that mediates the ordered assembly of spliceosomal proteins and snRNAs. Required for association of BRR2 with the spliceosomal U5 snRNP, and the subsequent assembly of the U4/U6-U5 tri-snRNP complex. 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, as well as the branch region. Has a role in branch site-3' splice site selection. Associates with the branch site-3' splice 3'-exon region. Also has a role in cell cycle.

Gene References into Functions

error-prone/efficient RH alleles suppress a prp2 mutant deficient at promoting the first catalytic step of splicing, whereas hyperaccurate/inefficient RH alleles exhibit synthetic sickness. Together our data indicate that prp8 RH alleles link splicing fidelity with catalytic efficiency by biasing the relative stabilities of distinct spliceosome conformations. PMID: 28416677
Together, these data establish that PRP8 is a metalloprotein that promotes exon ligation within the spliceosome. PMID: 23686287
Prp8 interaction sites with Snu114 and Aar2 proteins PMID: 16373487
Our results define a new ubiquitin-binding domain of Prp8 and suggest functional links between ubiquitin and the pre-mRNA splicing machinery PMID: 16428608
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
Opposing classes of prp8 alleles modulate the transition between the catalytic steps of pre-mRNA splicing. PMID: 17486100
evidence for a cytoplasmic precursor U5 snRNP that lacks mature U5 snRNP component Brr2p & depends on nuclear localization signal in Prp8p for nuclear import; retinitis pigmentosa mutations in Prp8p result in nuclear accumulation of precursor U5 snRNP PMID: 17934474
possible mechanism of how Prp8 regulates spliceosome activation PMID: 18779563
Results suggest that domain IV of PRP8 forms a surface that interacts directly with the RNA structures at the catalytic core of the spliceosome. PMID: 18836455
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