Anti-hnRNP E2/PCBP2 Antibody Picoband® fluoro647 Vervoeging

Poly (rC) -binding protein 2 is a protein that in humans is encoded by the PCBP2 gene. The protein encoded by this gene appears to be multifunctional. Along with PCBP-1 and hnRNPK, it is one of the major cellular poly (rC) -binding proteins. The encoded protein contains three K-homologous (KH) domains which may be involved in RNA binding. Together with PCBP-1, this protein also functions as a translational coactivator of poliovirus RNA via a sequence-specific interaction with stem-loop IV of the IRES, promoting poliovirus RNA replication by binding to its 5'-terminal cloverleaf structure. It has also been implicated in translational control of the 15-lipoxygenase mRNA, human papillomavirus type 16 L2 mRNA, and hepatitis A virus RNA. The encoded protein is also suggested to play a part in formation of a sequence-specific alpha-globin mRNP complex which is associated with alpha-globin mRNA stability. This multiexon structural mRNA is thought to be retrotransposed to generate PCBP-1, an intronless gene with functions similar to that of PCBP2. This gene and PCBP-1 have paralogous genes (PCBP3 and PCBP4) which are thought to have arisen as a result of duplication events of entire genes. This gene also has two processed pseudogenes (PCBP2P1 and PCBP2P2) . Multiple transcript variants encoding different isoforms have been found for this gene.

Peptidyl-prolyl cis-trans isomerase D; PPIase D

PCBP2

5094

Q15366

Human, Mouse, Rat

No cross-reactivity with other proteins.

E.coli-derived human hnRNP E2/PCBP2 recombinant protein (Position: D136-K276) .

Widely expressed.

Flow Cytometry

Cardiovascular, Immunology

Immunogen affinity purified.

Liquid

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be involved in cytoplasmic dynein-dependent movement of the receptor from the cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA- binding activity. Involved in regulation of AHR signaling by promoting the formation of the AHR:ARNT dimer; the function is independent of HSP90 but requires the chaperone activity. Involved in regulation of UV radiation-induced apoptosis. Promotes cell viability in anaplastic lymphoma kinase-positive anaplastic large- cell lymphoma (ALK+ ALCL) cell lines. May be involved in hepatitis C virus (HCV) replication and release.

1. Bejerano, G., Lowe, C. B., Ahituv, N., King, B., Siepel, A., Salama, S. R., Rubin, E. M., Kent, W. J., Haussler, D. A distal enhancer and an ultraconserved exon are derived from a novel retroposon. Nature 441: 87-90, 2006. 2. Chkheidze, A. N., Liebhaber, S. A. A novel set of nuclear localization signals determine distributions of the alpha-CP RNA-binding proteins. Molec. Cell. Biol. 23: 8405-8415, 2003. 3. Eiring, A. M., Harb, J. G., Neviani, P., Garton, C., Oaks, J. J., Spizzo, R., Liu, S., Schwind, S., Santhanam, R., Hickey, C. J., Becker, H., Chandler, J. C., and 13 others. miR-328 functions as an RNA decoy to modulate hnRNP E2 regulation of mRNA translation in leukemic blasts. Cell 140: 652-665, 2010.

At -20 ̊C for one year from date of receipt. Avoid repeated freezing and thawing. Protect from light.

38779 MW

6

Peptidylprolyl isomerase D

Cytoplasm.

BAG family molecular chaperone regulator 1

Rabbit IgG

Each vial contains 50% glycerol, 0.9% NaCl, 0.2% Na2HPO4, 0.02% NaN3.