PHAX Antibody (C-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| IHC-P, WB, E |
---|---|
Primary Accession | Q9H814 |
Other Accession | Q63068, Q9JJT9, Q3MHI4, NP_115553.2 |
Reactivity | Human |
Predicted | Bovine, Mouse, Rat |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 44403 Da |
Antigen Region | 297-326 aa |
Gene ID | 51808 |
---|---|
Other Names | Phosphorylated adapter RNA export protein, RNA U small nuclear RNA export adapter protein, PHAX, RNUXA |
Target/Specificity | This PHAX antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 297-326 amino acids from the C-terminal region of human PHAX. |
Dilution | WB~~1:1000 IHC-P~~1:10~50 |
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 | PHAX Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | PHAX |
---|---|
Synonyms | RNUXA |
Function | A phosphoprotein adapter involved in the XPO1-mediated U snRNA export from the nucleus. Bridge components required for U snRNA export, the cap binding complex (CBC)-bound snRNA on the one hand and the GTPase Ran in its active GTP-bound form together with the export receptor XPO1 on the other. Its phosphorylation in the nucleus is required for U snRNA export complex assembly and export, while its dephosphorylation in the cytoplasm causes export complex disassembly. It is recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Its compartmentalized phosphorylation cycle may also contribute to the directionality of export. Binds strongly to m7G-capped U1 and U5 small nuclear RNAs (snRNAs) in a sequence-unspecific manner and phosphorylation-independent manner (By similarity). Also plays a role in the biogenesis of U3 small nucleolar RNA (snoRNA). Involved in the U3 snoRNA transport from nucleoplasm to Cajal bodies. Binds strongly to m7G-capped U3, U8 and U13 precursor snoRNAs and weakly to trimethylated (TMG)-capped U3, U8 and U13 snoRNAs. Binds also to telomerase RNA. |
Cellular Location | Nucleus, nucleoplasm. Nucleus, Cajal body. Cytoplasm. Note=Located in the nucleoplasm and Cajal bodies. Shuttles between the nucleus and the cytoplasm. Shuttles between the nucleoplasm and Cajal bodies. |
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Background
A phosphoprotein adapter involved in the XPO1-mediated U snRNA export from the nucleus. Bridge components required for U snRNA export, the cap binding complex (CBC)-bound snRNA on the one hand and the GTPase Ran in its active GTP-bound form together with the export receptor XPO1 on the other. Its phosphorylation in the nucleus is required for U snRNA export complex assembly and export, while its dephosphorylation in the cytoplasm causes export complex disassembly. It is recycled back to the nucleus via the importin alpha/beta heterodimeric import receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP-and GDP-bound forms of Ran between the cytoplasm and nucleus. Its compartmentalized phosphorylation cycle may also contribute to the directionality of export. Binds strongly to m7G-capped U1 and U5 small nuclear RNAs (snRNAs) in a sequence-unspecific manner and phosphorylation-independent manner (By similarity). Plays also a role in the biogenesis of U3 small nucleolar RNA (snoRNA). Involved in the U3 snoRNA transport from nucleoplasm to Cajal bodies. Binds strongly to m7G-capped U3, U8 and U13 precursor snoRNAs and weakly to trimethylated (TMG)-capped U3, U8 and U13 snoRNAs. Binds also to telomerase RNA.
References
Mourao, A., et al. RNA 16(6):1205-1216(2010)
Matsuoka, S., et al. Science 316(5828):1160-1166(2007)
Lemm, I., et al. Mol. Biol. Cell 17(7):3221-3231(2006)
Watkins, N.J., et al. Mol. Cell 16(5):789-798(2004)
Boulon, S., et al. Mol. Cell 16(5):777-787(2004)
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