|Application ||WB, IHC-P, IF, E|
|Other Accession||NP_112182, 13569879|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||35 kDa|
|Application Notes||PHAP III antibody can be used for detection of PHAP III by Western blot at 1 µg/mL. A band at approximately 35 kDa can be detected. Antibody can also be used for immunohistochemistry starting at 2 µg/mL. For immunofluorescence start at 10 µg/mL.|
|Other Names||PHAP III Antibody: LANPL, LANP-L, Acidic leucine-rich nuclear phosphoprotein 32 family member E, LANP-like protein, acidic (leucine-rich) nuclear phosphoprotein 32 family, member E|
|Target/Specificity||ANP32E; PHAP III has no cross-reaction to PHAP I and PHAP I2a.|
|Reconstitution & Storage||PHAP III antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. As with all antibodies care should be taken to avoid repeated freeze thaw cycles. Antibodies should not be exposed to prolonged high temperatures.|
|Precautions||PHAP III Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Histone chaperone that specifically mediates the genome- wide removal of histone H2A.Z/H2AFZ from the nucleosome: removes H2A.Z/H2AFZ from its normal sites of deposition, especially from enhancer and insulator regions. Not involved in deposition of H2A.Z/H2AFZ in the nucleosome. May stabilize the evicted H2A.Z/H2AFZ-H2B dimer, thus shifting the equilibrium towards dissociation and the off-chromatin state (PubMed:24463511). Inhibits activity of protein phosphatase 2A (PP2A). Does not inhibit protein phosphatase 1. May play a role in cerebellar development and synaptogenesis.|
|Cellular Location||Cytoplasm. Nucleus|
|Tissue Location||Expressed in peripheral blood leukocytes, colon, small intestine, prostate, thymus, spleen, skeletal muscle, liver and kidney.|
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Provided below are standard protocols that you may find useful for product applications.
PHAP III Antibody: Apoptosis is related to many diseases and development. Caspase-9 plays a central role in cell death induced by a variety of apoptosis activators. Cytochrome c, after released from mitochondria, binds to Apaf-1, which forms an apoptosome that in turn binds to and activate procaspase-9. Activated caspase-9 cleaves and activates the effector caspases (caspase-3, -6 and -7), which are responsible for the proteolytic cleavage of many key proteins in apoptosis. The tumor suppressor putative HLA-DR-associated proteins (PHAPs) were recently identified as important regulators of mitochondrion apoptosis. PHAP appears to facilitate apoptosome-medicated caspase-9 activation and to stimulate the mitochondrial apoptotic pathway. PHAP was also shown to oppose both Ras- and Myc-medicated cell transformation.
Jiang X, Kim HE, Shu H, Zhao Y, Zhang H, Kofron J, Donnelly J, Burns D, Ng SC , Rosenberg S, Wang X. Distinctive roles of PHAP proteins and prothymosin-α in a death regulatory pathway. Science. 2003;299(5604):223-6.
Nicholson DW, Thornberry NA. Apoptosis. Life and death decisions. Science. 2003 10;299(5604):214-5.
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