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ANP32A Antibody (C-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| IHC-P, WB, E |
|---|---|
| Primary Accession | P39687 |
| Other Accession | P51122 |
| Reactivity | Human |
| Predicted | Bovine |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 28585 Da |
| Antigen Region | 211-239 aa |
| Gene ID | 8125 |
|---|---|
| Other Names | Acidic leucine-rich nuclear phosphoprotein 32 family member A, Acidic nuclear phosphoprotein pp32, pp32, Leucine-rich acidic nuclear protein, LANP, Mapmodulin, Potent heat-stable protein phosphatase 2A inhibitor I1PP2A, Putative HLA-DR-associated protein I, PHAPI, ANP32A, C15orf1, LANP, MAPM, PHAP1 |
| Target/Specificity | This ANP32A antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 211-239 amino acids from the C-terminal region of human ANP32A. |
| Dilution | WB~~1:1000 IHC-P~~1:50~100 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | ANP32A Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | ANP32A |
|---|---|
| Synonyms | C15orf1, LANP, MAPM, PHAP1 |
| Function | Multifunctional protein that is involved in the regulation of many processes including tumor suppression, apoptosis, cell cycle progression or transcription (PubMed:16341127, PubMed:11360199, PubMed:18439902, PubMed:10400610). Promotes apoptosis by favouring the activation of caspase-9/CASP9 and allowing apoptosome formation (PubMed:18439902). In addition, plays a role in the modulation of histone acetylation and transcription as part of the INHAT (inhibitor of histone acetyltransferases) complex. Inhibits the histone- acetyltranferase activity of EP300/CREBBP (CREB-binding protein) and EP300/CREBBP-associated factor by histone masking (PubMed:11830591). Preferentially binds to unmodified histone H3 and sterically inhibiting its acetylation and phosphorylation leading to cell growth inhibition (PubMed:16341127). Participates in other biochemical processes such as regulation of mRNA nuclear-to-cytoplasmic translocation and stability by its association with ELAVL1 (Hu-antigen R) (PubMed:18180367). Plays a role in E4F1-mediated transcriptional repression as well as inhibition of protein phosphatase 2A (PubMed:15642345, PubMed:17557114). |
| Cellular Location | Nucleus. Cytoplasm Endoplasmic reticulum. Note=Translocates to the cytoplasm during the process of neuritogenesis (By similarity). Shuttles between nucleus and cytoplasm. {ECO:0000250, ECO:0000269|PubMed:18180367} |
| Tissue Location | Expressed in all tissues tested. Highly expressed in kidney and skeletal muscle, moderate levels of expression in brain, placenta and pancreas, and weakly expressed in lung. Found in all regions of the brain examined (amygdala, caudate nucleus, corpus callosum, hippocampus and thalamus), with highest levels in amygdala |
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Provided below are standard protocols that you may find useful for product applications.
Background
Implicated in a number of cellular processes, including proliferation, differentiation, caspase-dependent and caspase-independent apoptosis, suppression of transformation (tumor suppressor), inhibition of protein phosphatase 2A, regulation of mRNA trafficking and stability in association with ELAVL1, and inhibition of acetyltransferases as part of the INHAT (inhibitor of histone acetyltransferases) complex. ANP32A plays a role in E4F1-mediated transcriptional repression.
References
Valdes, A.M., et al. Arthritis Rheum. 60(7):2046-2054(2009)
Pan, W., et al. J. Biol. Chem. 284(11):6946-6954(2009)
de Chiara, C., et al. FEBS J. 275(10):2548-2560(2008)
Kim, H.E., et al. Mol. Cell 30(2):239-247(2008)
Matilla, A., et al. Cerebellum 4(1):7-18(2005)
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