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Phospho-DAXX (Ser495) Polyclonal Antibody, Biotin Conjugated

Product Specifications

Background

This gene encodes a multifunctional protein that resides in multiple locations in the nucleus and in the cytoplasm. It interacts with a wide variety of proteins, such as apoptosis antigen Fas, centromere protein C, and transcription factor erythroblastosis virus E26 oncogene homolog 1. In the nucleus, the encoded protein functions as a potent transcription repressor that binds to sumoylated transcription factors. Its repression can be relieved by the sequestration of this protein into promyelocytic leukemia nuclear bodies or nucleoli. This protein also associates with centromeres in G2 phase. In the cytoplasm, the encoded protein may function to regulate apoptosis. The subcellular localization and function of this protein are modulated by post-translational modifications, including sumoylation, phosphorylation and polyubiquitination. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Nov 2008]

Synonyms

DAP6; EAP1; BING2; Death domain-associated protein 6; Daxx; hDaxx; ETS1-associated protein 1; Fas death domain-associated protein

Gene ID

1616

Swiss Prot

Q9UER7

Modification Site

Ser495

Cellular Locus

Cytoplasm, Nucleus

Host

Rabbit

Cross Reactivity

Human

Target

Phospho-DAXX (Ser495)

Clonality

Polyclonal

Conjugation

Biotin

Source

KLH conjugated synthetic phosphopeptide derived from human DAXX around the phosphorylation site of Ser495

Applications

WB, ELISA, IHC-P, IHC-F

Purification

Purified by Protein A.

Concentration

1ug/ul

Dilution

WB (1:300-5000), ELISA (1:500-1000), IHC-P (1:200-400), IHC-F (1:100-500)

Buffer

Aqueous buffered solution containing 0.01M TBS (pH 7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Modification

Phosphorylation

Storage Conditions

Store at -20°C for 12 months.

Specificity

This phosphorylation site is homologous to that of Ser505 in Bovine.

Prediction Reactivity

Cow, Pig

Gene ID URL

1616

Isotype

IgG

Curated Selection

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