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Phospho-DAXX (Ser668) Polyclonal Antibody, RBITC Conjugated

Product Specifications

Background

Apoptosis, or programmed cell death, occurs during normal cellular differentiation and development of multicellular organisms. Apoptosis is induced by certain cytokines including TNF and Fas ligand of the TNF family through their death domain containing receptors, TNFR1 and Fas. Cell death signals are transduced by death domain (DD) containing adapter molecules and members of the ICE/CED3 protease family. A novel DD containing molecule was recently cloned from mouse, human and monkey and designated Daxx. Daxx is a death domain containing important intermediate in the Fas mediated apoptosis. Daxx binds specifically to the Fas death domain and enhances Fas induced apoptosis and activates the Jun N terminal kinase (JNK) pathway. It is widely expressed in fetal and adult human and mouse tissue, indicating its important function in Fas signaling pathways.

Synonyms

Daxx phospho S668; p-Daxx phospho S668; BING 2; BING2; DAP 6; DAP6; Death associated protein 6; Death domain associated protein 6; EAP 1; EAP1; ETS1 associated protein 1; Fas death domain associated protein; hDaxx; MGC126245; MGC126246; DAXX_HUMAN.

Gene ID

1616

Modification Site

Ser668

Cellular Locus

Cytoplasm, Nucleus

Host

Rabbit

Cross Reactivity

Human, Mouse

Target

Phospho-DAXX (Ser668)

Clonality

Polyclonal

Isotype

IgG

Conjugation

RBITC

Source

KLH conjugated synthetic phosphopeptide derived from human DAXX around the phosphorylation site of Ser668

Applications

WB, IF (IHC-P), IF (IHC-F), IF (ICC)

Purification

Purified by Protein A.

Excitation Emission

570nm/595nm

Concentration

1µg/µl

Dilution

WB (1:300-5000), IF (IHC-P) (1:50-200), IF (IHC-F) (1:50-200), IF (ICC) (1:50-200)

Buffer

Aqueous buffered solution containing 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Modification

Phosphorylation

Storage Conditions

Store at -20°C. Aliquot into multiple vials to avoid repeated freeze-thaw cycles.

Gene ID URL

1616

Curated Selection

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