| Name: | Mouse Monoclonal to Pab1p, yeast poly(a) tail binding protein |
| Immunogen: | Yeast polyA binding protein preparations |
| HGNC Name: | NA |
| UniProt: | P04147 |
| Molecular Weight: | 67kDa by SDS-PAGE |
| Host: | Mouse |
| Isotype: | IgG2a |
| Species Cross-Reactivity: | Saccharomyces cerevisiae |
| RRID: | AB_2572370 |
| Format: | Concentrated hybridoma cell culture media plus 5mM NaN3 |
| Applications: | WB, IF/ICC, IHC, IP |
| Recommended Dilutions: | WB: 1:1,000-1:5,000. IF/ICC 1:500. |
| Storage: | Store at 4°C for short term, for longer term at -20°C. Avoid freeze/thaw cycles. |
Mouse Monoclonal Antibody to Pab1p
Cat# MCA-1G1
$120.00 – $800.00
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).
The MCA-1G1 is a IgG2a class antibody with a κ (kappa) light chain which was raised against a preparation of yeast mRNA binding proteins. It reacts cleanly with the ~67kDa Pab1p band on immunoblots of a yeast extracts and diffusely stains both the nuclei and cytoplasm of wild type yeast cells (2). The antibody is supplied as a large aliquot of Integra CL-350 flask material, which is concentrated tissue culture supernatant.
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).
The MCA-1G1 is a IgG2a class antibody with a κ (kappa) light chain which was raised against a preparation of yeast mRNA binding proteins. It reacts cleanly with the ~67kDa Pab1p band on immunoblots ofayeast extracts and diffusely stains both the nuclei and cytoplasm of wild type yeast cells (2). The antibody is supplied as a large aliquot of Integra CL-350 flask material, which is concentrated tissue culture supernatant.
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).
This antibody has been widely used in peer reviewed publications, see here.
