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the structure of human p49at 2.2A resolution with citrate in its inactive forms, is reported.
PRIM1 was detected preferentially at a higher level (>40-fold) in poorly differentiated tumor tissues (n = 46) compared with more highly differentiated tumors tissues (n = 10) (*p = 0.005).
PRIM1 inactivation sensitizes cancer cells to ATR and CHK1 inhibitors via S-phase stasis and Wee1-mediated, caspase 8-dependent apoptosis.
No mutations within PRIM1 were found in Chinese women with primary ovarian insufficiency.
Data suggest that PRIM1-p58,C-terminal domain stays bound to initiating NTP and 3prime-overhang DNA during whole cycle of RNA primer synthesis; meanwhile, PRIM1-p49 slides along DNA template toward 5prime-end with PRIM1-p58,N-terminal domain attached.
Data indicate that the conformational changes in primase are necessary to accomplish the initiation and then elongation of RNA synthesis.
Findings indicate that tethering of DNA primase Prim1 to the replisome by DNA polymerase alpha (pol alpha) is critical for the normal action of DNA replication forks in eukaryotic cells.
Mechanisms by which human DNA primase chooses to polymerize a nucleoside triphosphate
The replication of DNA in eukaryotic cells is carried out by a complex chromosomal replication apparatus, in which DNA polymerase alpha and primase are two key enzymatic components. Primase, which is a heterodimer of a small subunit and a large subunit, synthesizes small RNA primers for the Okazaki fragments made during discontinuous DNA replication. The protein encoded by this gene is the small, 49 kDa primase subunit.
DNA primase 49 kDa subunit
, DNA primase small subunit
, DNA primase small subunit, 49kDa
, DNA primase, p49 subunit
, DNA primase 1
, DNA primase subunit 48
, primase p49 subunit
, primase polypeptide 1, 49kDa
, primase, polypeptide 1, 49kDa