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POLDIP2 encodes a protein that interacts with the DNA polymerase delta p50 subunit. Additionally we are shipping POLDIP2 Antibodies (60) and many more products for this protein.
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findings establish that PolDIP2 can regulate the translesion synthesis polymerase and primer extension activities of PrimPol
POLDIP2 plays a crucial role in Tau aggregation via the impairment of autophagy activity, providing insight into Tau aggregation in Tau pathology.
PDIP38 can respond to genotoxic or transcriptional stresses by undergoing translocation to the spliceosomes, where it is a required participant in the regulation of MDM2 (show MDM2 Proteins) alternative splicing.
DNA polymerase delta-interacting protein 2 is a processivity factor for DNA polymerase lambda (show POLL Proteins) during 8-oxo-7,8-dihydroguanine bypass.
We demonstrate that PDIP38 (Poldelta interacting protein of 38kDa (show RFC3 Proteins)) directly interacts with the TLS (show FUS Proteins) polymerase Poleta. PDIP38 is able to interact directly not only with Poleta but also with the specialized polymerases Rev1 (show REV1 Proteins) and Polzeta (via Rev7 (show MAD2L2 Proteins)).
suggest that the TNFAIP1 (show TNFAIP1 Proteins)/POLDIP2 complex sense-antisense architecture represents a clinically significant transcriptional structural-functional gene module associated with amplification of the genomic region on 17q11.2 in breast cancer.
PDIP38 might play a role in the pol delta (show POLD1 Proteins)-mediated viral DNA replication
PDIP38 is located in the mitochondrial matrix. TFAM (show TFAM Proteins) and mitochondrial single-stranded DNA binding protein (show RPA1 Proteins) (mtSSB) are co-immunoprecipitated with PDIP38
PDIP38 can shuttle between the cytoplasmic and the nuclear compartments and that its subcellular localization is regulated by CEACAM1 (show CEACAM1 Proteins)
Poldip2 associates with p22phox (show CYBA Proteins) to activate Nox4 (show NOX4 Proteins), leading to regulation of focal adhesion turnover and vascular smooth muscle cell migration, thus linking reactive oxygen species production and cytoskeletal remodeling.
the rate of collagen I degradation was increased in Poldip2(+/-) vs. Poldip2(+/+) MASMs. Conversely, activation of the PI3K/Akt (show AKT1 Proteins)/mTOR (show FRAP1 Proteins) signaling pathway, involved in regulation of protein synthesis, was significantly elevated in Poldip2(+/-) MASMs as was beta1-integrin expression.
Poldip2 is an essential protein in development, and underline its importance in cell viability and proliferation
Suggest Poldip2 promotes ischemia-induced collateral vessel formation via multiple mechanisms that likely involve reactive oxygen species-dependent activation of matrix metalloproteinase activity, as well as enhanced vascular cell growth and survival.
Poldip2 expression is necessary for maintainance vascular integrity and function.
miR (show MLXIP Proteins)-291a-5p directly inhibited the expression of PDIP38.
overexpression of Mitogenin I or mitochondrial single-stranded DNA-binding protein (show RPA1 Proteins) increased elongated or fragmented mitochondria in mouse C2C12 myoblast cells, respectively.
This gene encodes a protein that interacts with the DNA polymerase delta p50 subunit. The encoded protein also interacts with proliferating cell nuclear antigen. Some transcripts of this gene overlap in a tail-to-tail orientation with the gene for tumor necrosis factor, alpha-induced protein 1 (TNFAIP1).
38 kDa DNA polymerase delta interaction protein
, polymerase delta interacting protein 38
, polymerase delta-interacting protein 2
, mitogenin 1
, mitogenin I
, DNA-directed polymerase delta interacting protein 2
, DNA polymerase delta interacting protein 2
, polymerase (DNA-directed), delta interacting protein 2
, polymerase (DNA) delta interacting protein 2