Pab1p

Référence 045876-500ul

Conditionnement : 500ul

Marque : US Biological

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045876Pab1p

Specifications
Clone TypeMonoclonal
Hostmouse
Swiss ProtP04147
IsotypeIgG2a,k
GradeSupernatant
ApplicationsIC IF IHC IP WB
CrossreactivityYe
Shipping TempBlue Ice
Storage Temp-20°C

The Pab1p protein was discovered in Saccharomyces cerevisia since it is abundant and binds specifically to the polyA tails of mRNA molecules (1). It was characterized by Adam et al. who made antibodies to proteins which could be cross-linked to polyA sequences by UV irradiation, obtaining polyclonal antisera which revealed several immunoreactive bands. Screening a λgt11 expression library with these antisera led to the cloning and sequencing of the most abundant of these bands which was named Pab1p for polyadenylate binding protein, which proved to be the product of the single Pab1 gene. The systematic name in the Saccharomyces genome database is YER165w. It has a role in polyA length control in combination with Nab2p and may also be involved in mRNA stability and transcription (2). Pab1p is found in both the cytoplasm and nuclei of yeast cells (3) and has a deduced molecular weight of 64kDa, but runs on typical SDS-PAGE gels at about 67kDa (1). The yeast Pab1p protein sequence includes four RNA recognition motifs followed by a single C-terminal polyA binding domain. The closest human homolog of the yeast protein is polyadenylate-binding protein cytoplasmic 1-like (PABPC1L) which has the same domain structure, although is not well conserved in amino acid sequence. There are seven human genes encoding polyA binding proteins, four of which produce proteins with the same domain structure as yeast Pab1p and human PABPC1L (4). Recent studies suggest that Pab1p in yeast is centrally important in the stress triggered phase separation response, a newly recognized and studied phenomena in which stress can induces the formation of protein and RNA accumulations in cells (5).

Applications:
Suitable for use in Immunohistochemistry, Immunofluorescence/ Immunocytochemistry, Immunoprecipitation and Western Blot. Other applications not tested.

Recommended Dilutions:
Immunofluorescence (IC): 1:500
Western Blot: 1:1000-1:5000
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for 12 months after receipt. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

Applications
Product Type: Mab|Isotype: IgG2a,k|Clone No: 1G1|Host: mouse|Concentration: Not Determined |Form: Supplied as a liquid, 5mM sodium azide.|Purity: Sterile-filtered cell culture fluid from an Integra CL-350 biochamber|Immunogen: Yeast polyA binding protein preparations|Specificity: Recognizes Saccharomyces cerevisiae Pab1p. Reacts cleanly with the ~67kD Pab1p band on immunoblots of a yeast extracts and diffusely stains both the nuclei and cytoplasm of wild type yeast cells (2).||Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.
Immunogen
Yeast polyA binding protein preparations
Form
Supplied as a liquid, 5mM sodium azide.
Purity
Sterile-filtered cell culture fluid from an Integra CL-350 biochamber
Specificity
Recognizes Saccharomyces cerevisiae Pab1p. Reacts cleanly with the ~67kD Pab1p band on immunoblots of a yeast extracts and diffusely stains both the nuclei and cytoplasm of wild type yeast cells (2).
References
1. Adam SA, et al. mRNA polyadenylate-binding protein: gene isolation and sequencing and identification of a ribonucleoprotein consensus sequence. Mol. Cell Biol. 6:2932-43 (1986).|2. Hector RE, et al. Dual requirement for yeast hnRNP Nab2p in mRNA poly(A) tail length control and nuclear export. EMBO J. 21:1800-10 (2002).|3. Anderson JT, Wilson SM, Datar KV, Swanson MS. NAB2: a yeast nuclear polyadenylated RNA-binding protein essential for cell viability. Mol. Cell Biol. 13:2730-41 (1993).|4. Eliseeva, IA, Lyabin, DN, Ovchinnikov LP. Poly(A)-Binding Proteins: Structure, Domain Organization, and Activity Regulation. Biochem. (Mosc). 78:1377-91 (2013).|5. Ribackj JA, et al. Stress-Triggered Phase Separation Is an Adaptive,Evolutionarily Tuned Response. Cell 168:1028-40 (2017).