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.
Belongs to the DNA polymerase type-B family.
A 165 kDa form is probably produced by proteolytic cleavage at Lys-124.
ab176734 at 0.4 µg/ml detecting DNA polymerase alpha in HeLa whole cell lysate by WB following IP. ab176734 was used for IP at 3 µg/mg of lysate, 1 mg of lysate was used for IP and 20% of the IP was loaded.
Detection: Chemiluminescence with an exposure time of 10 seconds.