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POLA1 Antibody (N-Term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | P09884 |
| Other Accession | P33609, O89042 |
| Reactivity | Human |
| Predicted | Mouse, Rat |
| Host | Rabbit |
| Clonality | polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 165913 Da |
| Gene ID | 5422 |
|---|---|
| Other Names | DNA polymerase alpha catalytic subunit, 2.7.7.7, DNA polymerase alpha catalytic subunit p180, POLA1, POLA |
| Target/Specificity | This POLA1 antibody is generated from a rabbit immunized with a KLH conjugated synthetic peptide between 1-33 amino acids from the human region of human POLA1. |
| Dilution | WB~~1:2000 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | POLA1 Antibody (N-Term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | POLA1 |
|---|---|
| Synonyms | POLA |
| Function | Catalytic subunit of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex) which plays an essential role in the initiation of DNA synthesis. During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1, a regulatory subunit POLA2 and two primase subunits PRIM1 and PRIM2) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1. The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands. These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively. The reason this transfer occurs is because the polymerase alpha has limited processivity and lacks intrinsic 3' exonuclease activity for proofreading error, and therefore is not well suited for replicating long complexes. In the cytosol, responsible for a substantial proportion of the physiological concentration of cytosolic RNA:DNA hybrids, which are necessary to prevent spontaneous activation of type I interferon responses (PubMed:27019227). |
| Cellular Location | Nucleus. Cytoplasm, cytosol. Note=In the cytosol, colocalizes with RNA:DNA hybrids with a speckled pattern |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
Plays an essential role in the initiation of DNA replication. During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit POLA1/p180, a regulatory subunit POLA2/p70 and two primase subunits PRIM1/p49 and PRIM2/p58) is recruited to DNA at the replicative forks via direct interactions with MCM10 and WDHD1. The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands. These primers are initially extended by the polymerase alpha catalytic subunit and subsequently transferred to polymerase delta and polymerase epsilon for processive synthesis on the lagging and leading strand, respectively. The reason this transfer occurs is because the polymerase alpha has limited processivity and lacks intrinsic 3' exonuclease activity for proofreading error, and therefore is not well suited for replicating long complexes.
References
Wong S.W.,et al.EMBO J. 7:37-47(1988).
Pearson B.E.,et al.Mol. Cell. Biol. 11:2081-2095(1991).
Hsi K.-L.,et al.Nucleic Acids Res. 18:6231-6237(1990).
Smale S.T.,et al.Mol. Cell. Biol. 6:4077-4087(1986).
Lee S.S.,et al.Proc. Natl. Acad. Sci. U.S.A. 92:7882-7886(1995).
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