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The antibody against POLE4 was raised in Rabbit using a synthetic peptide corresponding to a sequence within amino acids 1-100 of human POLE4 (NP_063949.2) as the immunogen. The polyclonal antibody exists as a isotype IgG, by affinity purification. This antibody has been validated on WB, ELISA.
The antibody against POLE4 was raised in Rabbit using a synthetic peptide corresponding to a sequence within amino acids 1-100 of human POLE4 (NP_063949.2) as the immunogen. The polyclonal antibody exists as a isotype IgG, by affinity purification. This antibody has been validated on WB, ELISA.
| Cat.No | ADA-08244A | Clonality | Polyclonal |
|---|---|---|---|
| Host Species | Rabbit | Target Name | POLE4 |
| Target Synonyms | POLE4; YHHQ1; p12; DNA polymerase epsilon subunit 4 | Form | Liquid |
| Species Reactivity | Mouse | Isotype | IgG |
| Storage Buffer | 50% Glycerol, PBS with 0.05% proclin300, pH7.3. | Purification Method | Affinity purification |
| Positive Samples | Mouse liver | Application | ELISA, WB |
| Immunogen Description | A synthetic peptide corresponding to a sequence within amino acids 1-100 of human POLE4 (NP_063949.2). | Target Species | Human |
|---|---|---|---|
| Immunogen Sequence | MAAAAAAGSGTPREEEGPAGEAAASQPQAPTSVPGARLSRLPLARVKALVKADPDVTLAGQEAIFILARAAELFVETIAKDAYCCAQQGKRKTLQRRDLD | Uniprot ID | Q9NR33 |
Uniprot Id
Q9NR33
Target Species
Human
Target Name
POLE4
Target Full Name
DNA polymerase epsilon subunit 4
Target Function
Accessory component of the DNA polymerase epsilon complex. Participates in DNA repair and in chromosomal DNA replication.
Target Subcellular Location
Nucleus.
Target Synonyms
DNA polymerase epsilon 4 accessory subunit; DNA polymerase epsilon p12 subunit; DNA polymerase epsilon subunit 4; DNA polymerase epsilon subunit p12; DNA polymerase II subunit 4; DPOE4_HUMAN; p12; POLE4; Polymerase (DNA directed) epsilon 4 (p12 subunit); Polymerase (DNA directed) epsilon 4; YHHQ1
Target Background
POLE4 is a histone-fold protein that interacts with other histone-fold proteins to bind DNA in a sequence-independent manner. These histone-fold protein dimers combine within larger enzymatic complexes for DNA transcription, replication, and packaging.[supplied by OMIM, Apr 2004]
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