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Merck

WH0057804M1

Monoclonal Anti-POLD4 antibody produced in mouse

clone 2B11, ascites fluid

Synonym(s):

Anti-POLDS, Anti-p12, Anti-polymerase (DNA-directed), delta 4

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200 μL

₩856,254

₩856,254


Estimated to ship onFebruary 20, 2026Details

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About This Item

NACRES:
NA.41
UNSPSC Code:
12352203

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Product Name

Monoclonal Anti-POLD4 antibody produced in mouse, clone 2B11, ascites fluid

biological source

mouse

conjugate

unconjugated

antibody form

ascites fluid

antibody product type

primary antibodies

clone

2B11, monoclonal

species reactivity

human

technique(s)

indirect ELISA: suitable
western blot: 1:500-1:1000

isotype

IgG2bκ

GenBank accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Quality Level

Gene Information

human ... POLD4(57804)

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SAB4200054SAB1405011SAB1410988
species reactivity

human

species reactivity

human

species reactivity

human

species reactivity

human

clone

2B11, monoclonal

clone

PDK 7B4, monoclonal

clone

3D2, monoclonal

clone

polyclonal

conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

conjugate

unconjugated

Gene Information

human ... POLD4(57804)

Gene Information

human ... POLD2(5425)

Gene Information

human ... PLDN(26258)

Gene Information

human ... POLD2(5425)

antibody form

ascites fluid

antibody form

purified from hybridoma cell culture

antibody form

purified immunoglobulin

antibody form

purified immunoglobulin

biological source

mouse

biological source

rat

biological source

mouse

biological source

rabbit

Biochem/physiol Actions

DNA polymerase (Pol) δ plays a vital role in DNA replication, DNA repair processes and genetic recombination. POLD4 stabilizes the Pol δ holoenzyme. In addition, it also facilitates pol δ-PCNA complex stabilization. Proteolysis of POLD4 in response to DNA damage leads to the consequent conversion of the holoenzyme pol δ4 to the heterotrimer pol δ3. Pol δ3 acts as an antimutator polymerase and is supposed to enhance surveillance against mutagenesis. Downregulated expression of the gene is associated with the genomic instability in lung cancer.

General description

DNA polymerase δ 4 (POLD4), also known as p12, is the smallest subunit of DNA polymerase (Pol) δ. It is encoded by the gene mapped to human chromosome 11q13.2.
The DNA polymerase delta complex is involved in DNA replication and repair, and it consists of the proliferating cell nuclear antigen (PCNA; MIM 176740), the multisubunit replication factor C (see MIM 102579), and the 4 subunit polymerase complex: POLD1 (MIM 174761), POLD2 (MIM 600815), POLD3 (MIM 611415), and POLD4 (Liu and Warbrick, 2006 [PubMed 16934752]).

Immunogen

POLD4 (AAH01334, 1 a.a. ~ 34 a.a) full-length recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.

Sequence
MGRKRLITDSYPVVKRREGPAGHSKGELAPELGL

Physical form

Solution

Legal Information

GenBank is a registered trademark of United States Department of Health and Human Services

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Storage Class

10 - Combustible liquids

wgk

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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A novel DNA damage response: rapid degradation of the p12 subunit of dna polymerase delta.
Zhang S, et al.
The Journal of Biological Chemistry, 15330-40 null
PPP6R3?USP6 amplification: Novel oncogenic mechanism in malignant nodular fasciitis
Guo R, et al.
Genes Chromosomes Cancer, 640-9 null
Proteolysis of the Human DNA Polymerase Delta Smallest Subunit p12 by μ-Calpain in Calcium-Triggered Apoptotic HeLa Cells
Fan X, et al.
PLoS ONE null
Regulation of DNA Polymerase POLD4 Influences Genomic Instability in Lung Cancer
Huang QM, et al.
Cancer Research, 8407-16 null
Prashant Khandagale et al.
Life science alliance, 2(2) (2019-03-20)
Human DNA polymerase delta (Polδ), a holoenzyme consisting of p125, p50, p68, and p12 subunits, plays an essential role in DNA replication, repair, and recombination. Herein, using multiple physicochemical and cellular approaches, we found that the p12 protein forms a

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