Product Details

Uniprot No.

Target Names

POLA1

Alternative Names

DKFZp686K1672 antibody; DNA polymerase alpha 1 catalytic subunit antibody; DNA polymerase alpha catalytic subunit antibody; DNA polymerase alpha catalytic subunit p180 antibody; DNA polymerase alpha p180 subunit antibody; DPOLA_HUMAN antibody; OTTHUMP00000023089 antibody; OTTHUMP00000023090 antibody; P180 antibody; p180 subunit antibody; POLA antibody; POLA1 antibody; Polymerase (DNA directed), alpha 1, catalytic subunit antibody; Polymerase (DNA-directed), alpha (70kD) antibody

Raised in

Rabbit

Species Reactivity

Human

Immunogen

Synthesized peptide derived from the N-terminal region of Human DNA pol α.

Immunogen Species

Homo sapiens (Human)

Conjugate

Non-conjugated

Isotype

IgG

Purification Method

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.

Concentration

It differs from different batches. Please contact us to confirm it.

Buffer

Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.

Form

Liquid

Tested Applications

WB, ELISA

Recommended Dilution

Application	Recommended Dilution
WB	1:500-1:2000
ELISA	1:20000

Protocols

Western Blotting(WB) Protocol
ELISA Protocol

Troubleshooting and FAQs

Antibody FAQs

Storage

Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.

Lead Time

Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

Citations

Customer Reviews and Q&A

■ Customer Reviews

Average Rating:

5.0 - 1 reviews

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Applications : Western blot analysis

Sample type: cell

Review: The expression of hub proteins (TNF, ESR1, MCL1, TBP, CD19, LCK, PCNA, CHEK1, and POLA1) in HeLa cells treated with N-CM and H-CM. The expression of hub proteins in HeLa cells treated with N-CM and H-CM for 24 h was analyzed with Western blotting.

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Target Background

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.

Gene References into Functions

High POLA1 expression is associated with bladder cancer. PMID: 28320388
Divalent ions attenuate DNA synthesis by human DNA polymerase alpha by changing the structure of the template/primer or by perturbing the polymerase reaction. PMID: 27235627
We propose that completely skewed XCI favoring the normal X chromosome resulted from death of cells with an active derivative X that was caused by a non-functional POLA1 gene. In summary, we conclude that functional monosomy of 6q27-qter and functional disomy of Xpter-p22.11 are responsible for the clinical phenotype of the patient PMID: 28371302
The first crystal structure of human Polalpha polymerase subunit in complex with a DNA:DNA helix shows that portion of the DNA:DNA helix in contact with the polymerase is not in a B-form but in a hybrid A-B form. The free energy cost of distorting DNA from B- to hybrid A-B form may augur the termination of primer synthesis. PMID: 27032819
Data indicate that X-linked reticulate pigmentary disorder (XLPDR) is caused by an intronic mutation that disrupts the expression of POLA1, which encodes the catalytic subunit of DNA polymerase-alpha. PMID: 27019227
Mutation in POLA1 is responsible for XLPDR (MIM: 312040) and demonstrates a role for this gene in interferon regulation PMID: 27019227
Inhibition of DNA polymerases a, delra and e by AFP promoter-driven artificial microRNAs may lead to effective growth arrest of AFP-positive HCC cells,as novel strategy for gene therapy PMID: 25924900
To understand the regulatory mechanisms and to reveal the details of DNA polymerase alpha organization, the study determined the crystal structure of p70 in complex with C terminus of the POLA catalytic subunit (p180C). PMID: 25847248
the N-terminal domain of the large subunit of primase (p58N) directly interacts with the C-terminal domain of the catalytic subunit of polalpha (p180C) PMID: 24962573
The Pol alpha-primase complex. PMID: 22918585
Pol epsilon and Pol alpha/delta seem to pursue their functions at least in part independently in late S phase PMID: 22887995
Findings indicate that tethering of primase to the replisome by DNA polymerase alpha (pol alpha) is critical for the normal action of DNA replication forks in eukaryotic cells. PMID: 22593576
Depletion of p180 in U2OS cells increases cell size. PMID: 22679391
Human cell DNA replication is mediated by a discrete multiprotein complex. The peak of DNA polymerase alpha activity co-purifies with the peak of in vitro SV40 DNA replication activity. PMID: 11968016
correlation between binding of CDP/Cux to the DNA pol alpha promoter and the stimulation of gene expression PMID: 12665598
Data show that human DNA polymerase alpha and the Klenow fragment of Escherichia coli DNA polymerase I (KF) incorporate all four nucleotide analogues opposite all four canonical bases up to 4000-fold more efficiently than incorrect natural bases. PMID: 12950174
Three-dimensional structures of the zinc finger motif in the carboxy terminus of the human DNA polymerase-alpha were determined in this study. PMID: 14499601
nonphosphorylated p68 inhibited the stimulation of pol-alpha activity by hyperphosphorylated retinoblastoma protein, suggesting that p68 might impede the association of ppRb with p180 PMID: 16935576
During dNTP polymerization, it uses a combination of negative (N-1 and N-3) and positive (N-1 and N-6) selectivity to differentiate between right and wrong dNTPs, while the shape of the base pair is essentially irrelevant. PMID: 17209555
These results argue that cells can tolerate low levels of p180 as long as Mcm10 is present to "recycle" it. PMID: 17699597
And-1/Ctf4 is therefore a new replication initiation factor that brings together the MCM2-7 helicase and the DNA pol alpha-primase complex. PMID: 17761813
Results show that depletion of DNA polymerase alpha and not Polepsilon or Poldelta by siRNA induces phosphorylation of Chk1 on Ser345, thus phenocopying antimetabolite exposure. PMID: 19177015
DNA and p180 binding to an Mcm10 construct that contains both the ID and CTD, provide the first mechanistic insight into how Mcm10 might use a handoff mechanism to load and stabilize pol alpha within the replication fork. PMID: 19608746

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Involvement in disease

Pigmentary disorder, reticulate, with systemic manifestations, X-linked (PDR)

Subcellular Location

Nucleus. Cytoplasm, cytosol.

Protein Families

DNA polymerase type-B family

Database Links

HGNC: 9173

OMIM: 301220

KEGG: hsa:5422

STRING: 9606.ENSP00000368349

UniGene: Hs.567319

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