Anti-PDXP Antibody Picoband®, Cy3 Conjugate

Pyridoxal 5-prime-phosphate (PLP) is the active form of vitamin B6 that acts as a coenzyme in maintaining biochemical homeostasis. The preferred degradation route from PLP to 4-pyridoxic acid involves the dephosphorylation of PLP by PDXP.

Calcium-binding protein that acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium. Together with PDCD6, acts as calcium-dependent adapter for the BCR (KLHL12) complex, a complex involved in endoplasmic reticulum (ER)-Golgi transport by regulating the size of COPII coats. In response to cytosolic calcium increase, the heterodimer formed with PDCD6 interacts with, and bridges together the BCR (KLHL12) complex and SEC31 (SEC31A or SEC31B), promoting monoubiquitination of SEC31 and subsequent collagen export, which is required for neural crest specification. Its role in the heterodimer formed with PDCD6 is however unclear: some evidences show that PEF1 and PDCD6 work together and promote association between PDCD6 and SEC31 in presence of calcium. Other reports show that PEF1 dissociates from PDCD6 in presence of calcium, and may act as a negative regulator of PDCD6. Also acts as a negative regulator of ER-Golgi transport; possibly by inhibiting interaction between PDCD6 and SEC31.

1. Gohla, A., Birkenfeld, J., Bokoch, G. M. Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics. Nature Cell Biol. 7: 21-29, 2005. 2. Hartz, P. A. Personal Communication. Baltimore, Md. 02/27/2017. 3. Huang, T. Y., Michael, S., Xu, T., Sarkeshik, A., Moresco, J. J., Yates, J. R., III, Masliah, E., Bokoch, G. M., DerMardirossian, C. A novel Rac1 GAP splice variant relays poly-Ub accumulation signals to mediate Rac1 inactivation. Molec. Biol. Cell 24: 194-209, 2013.

At -20℃ for one year from date of receipt. After reconstitution, at 4℃ for one month. It can also be aliquotted and stored frozen at -20℃ for six months. Avoid repeated freezing and thawing.