POLA1 ELISA Kit for Human(Homo sapiens) | EIAab.comPOLA1 ELISA Kit for Human(Homo sapiens)

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POLA1 (Gene name),

DNA polymerase alpha catalytic subunit (Protein name ), DPOLA_HUMAN from NCBI database.

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General Annotation

Antigen Annotation

Predicted Eptitope

Vaild Sequence

Related Databases

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Gene name:

POLA1(POLA);

Protein name:

DNA polymerase alpha catalytic subunit;

Alternative:

DNA polymerase alpha catalytic subunit p180;

Organism:

Human (Homo sapiens).

General Annotation

Sub Unit:

The DNA polymerase alpha complex is composed of four subunits: the catalytic subunit POLA1, the regulatory subunit POLA2, and the small and the large primase subunits PRIM1 and PRIM2 respectively. Interacts with PARP1; this interaction functions as part of the control of replication fork progression. Interacts with MCM10 and WDHD1; these interactions recruit the polymerase alpha complex to the pre-replicative complex bound to DNA. Interacts with RPA1; this interaction stabilizes the replicative complex and reduces the misincorporation rate of DNA polymerase alpha by acting as a fidelity clamp. Interacts with SV40 Large T antigen; this interaction allows viral DNA replication. Interacts with herpes simplex virus 1 (HHV-1) replication origin-binding protein UL9.

Function:

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.

Subcellular Location:

Nucleus

Protein Attributes:

Sequence length:

1462

Sequence:

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1400:

1450:

1462:

LSKLFAGCAV | KS

3D Structure:

N/A

Predicted Eptitope:

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Vaild Sequence:

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Related Databases

STRING:

9606.ENSP00000368349

MIM:

312040

SMR:

P09884

UniGene:

Hs.567319

Pfam:

PF12254

String:

P09884

KEGG:

hsa:5422

Uniprot:

P09884

FOR

ELISA Kit for Human DNA polymerase alpha catalytic subunit

CLIA Kit for Human DNA polymerase alpha catalytic subunit

Polyclonal Antibody for Human DNA polymerase alpha catalytic subunit

Monoclonal Antibody for Human DNA polymerase alpha catalytic subunit

Protein for Human DNA polymerase alpha catalytic subunit

R&D Technical Data

For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.

Precision

For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.

Recovery

For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.

Linearity

For more information, please refer to the manual,Or contact our technical support: tech@eiaab.com.

References

1.

"Human DNA polymerase alpha gene expression is cell proliferation dependent and its primary structure is similar to both prokaryotic and eukaryotic replicative DNA polymerases."
Wong S.W. , Wahl A.F. , Yuan P.-M. , Arai N. , Pearson B.E. , Arai K. , Korn D. , Hunkapiller M.W. , Wang T.S.-F.
EMBO J.7:37-47(1988) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA]
2.

NIEHS SNPs program
Submitted (2003-04) to the EMBL/GenBank/DDBJ databases

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]
3.

"Human DNA polymerase alpha gene: sequences controlling expression in cycling and serum-stimulated cells."
Pearson B.E. , Nasheuer H.-P. , Wang T.S.-F.
Mol. Cell. Biol.11:2081-2095(1991) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-8
4.

"Human DNA polymerase alpha catalytic polypeptide binds ConA and RCA and contains a specific labile site in the N-terminus."
Hsi K.-L. , Copeland W.C. , Wang T.S.-F.
Nucleic Acids Res.18:6231-6237(1990) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PROTEIN SEQUENCE OF 19-37 AND 1405-1426;PROTEOLYTIC PROCESSING AT LYS-124
5.

"T-antigen-DNA polymerase alpha complex implicated in simian virus 40 DNA replication."
Smale S.T. , Tjian R.
Mol. Cell. Biol.6:4077-4087(1986) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH SV40 LARGE T ANTIGEN
6.

"Interaction of herpes simplex virus 1 origin-binding protein with DNA polymerase alpha."
Lee S.S. , Dong Q. , Wang T.S. , Lehman I.R.
Proc. Natl. Acad. Sci. U.S.A.92:7882-7886(1995) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH HHV-1 UL9 PROTEIN
7.

"Role of protein-protein interactions in the function of replication protein A (RPA): RPA modulates the activity of DNA polymerase alpha by multiple mechanisms."
Braun K.A. , Lao Y. , He Z. , Ingles C.J. , Wold M.S.
Biochemistry36:8443-8454(1997) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH RPA1
8.

"Functional association of poly(ADP-ribose) polymerase with DNA polymerase alpha-primase complex: a link between DNA strand break detection and DNA replication."
Dantzer F. , Nasheuer H.P. , Vonesch J.L. , de Murcia G. , Menissier-de Murcia J.
Nucleic Acids Res.26:1891-1898(1998) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;INTERACTION WITH PARP1
9.

"A quantitative atlas of mitotic phosphorylation."
Dephoure N. , Zhou C. , Villen J. , Beausoleil S.A. , Bakalarski C.E. , Elledge S.J. , Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A.105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186; SER-190 AND SER-209;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
tissue: Cervix carcinoma.
10.

"Physical interactions between Mcm10, DNA, and DNA polymerase alpha."
Warren E.M. , Huang H. , Fanning E. , Chazin W.J. , Eichman B.F.
J. Biol. Chem.284:24662-24672(2009) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: INTERACTION WITH MCM10
11.

"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V. , Lundgren D.H. , Hwang S.-I. , Rezaul K. , Wu L. , Eng J.K. , Rodionov V. , Han D.K.
Sci. Signal.2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-174 AND SER-186;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
tissue: Leukemic T-cell.
12.

"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V. , Vermeulen M. , Santamaria A. , Kumar C. , Miller M.L. , Jensen L.J. , Gnad F. , Cox J. , Jensen T.S. , Nigg E.A. , Brunak S. , Mann M.
Sci. Signal.3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-174; SER-186; SER-190 AND SER-209;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
tissue: Cervix carcinoma.
13.

"Initial characterization of the human central proteome."
Burkard T.R. , Planyavsky M. , Kaupe I. , Breitwieser F.P. , Buerckstuemmer T. , Bennett K.L. , Superti-Furga G. , Colinge J.
BMC Syst. Biol.5:17-17(2011) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
14.

"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T. , Prokhorova T.A. , Akimov V. , Henningsen J. , Johansen P.T. , Kratchmarova I. , Kassem M. , Mann M. , Olsen J.V. , Blagoev B.
Sci. Signal.4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186 AND SER-209;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
15.

"Nuclear magnetic resonance structures of the zinc finger domain of human DNA polymerase-alpha."
Evanics F. , Maurmann L. , Yang W.W. , Bose R.N.
Biochim. Biophys. Acta1651:163-171(2003) [PubMed] [Europe PMC] [Abstract]

[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: STRUCTURE BY NMR OF 1345-1382

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