Anti-DPYS Antibody Picoband® 0,00647 Vervoeging

Dihydropyrimidinase is an enzyme that in humans is encoded by the DPYS gene. Dihydropyrimidinase catalyzes the conversion of 5,6-dihydrouracil to 3-ureidopropionate in pyrimidine metabolism. Dihydropyrimidinase is expressed at a high level in liver and kidney as a major 2.5-kb transcript and a minor 3.8-kb transcript. Defects in the DPYS gene are linked to dihydropyrimidinuria.

Peflin; PEF protein with a long N-terminal hydrophobic domain; Penta-EF hand domain-containing protein 1; PEF1; ABP32; UNQ1845; PRO3573

DPYS

1807

Q14117

Human, Mouse, Rat

No cross-reactivity with other proteins.

E.coli-derived human DPYS recombinant protein (Position: D100-P518) .

Pre-B-cells and B-cells but not terminally differentiated plasma cells.

Flow Cytometry

Epigenetics and Nuclear Signaling, Mediator Complex, Transcription

Immunogen affinity purified.

Liquid

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. Hamajima, N., Kouwaki, M., Vreken, P., Matsuda, K., Sumi, S., Imaeda, M., Ohba, S., Kidouchi, K., Nonaka, M., Sasaki, M., Tamaki, N., Endo, Y., De Abreu, R., Rotteveel, J., van Kuilenburg, A., van Gennip, A., Togari, H., Wada, Y. Dihydropyrimidinase deficiency: structural organization, chromosomal localization, and mutation analysis of the human dihydropyrimidinase gene. Am. J. Hum. Genet. 63: 717-726, 1998. 2. Hamajima, N., Matsuda, K., Sakata, S., Tamaki, N., Sasaki, M., Nonaka, M. A novel gene family defined by human dihydropyrimidinase and three related proteins with differential tissue distribution. Gene 180: 157-163, 1996. 3. Nakajima, Y., Meijer, J., Dobritzsch, D., Ito, T., Zhang, C., Wang, X., Watanabe, Y., Tashiro, K., Meinsma, R., Roelofsen, J., Zoetekouw, L, van Kuilenburg, A. B. P. Dihydropyrimidinase deficiency in four East Asian patients due to novel and rare DPYS mutations affecting protein structural integrity and catalytic activity. Molec. Genet. Metab. 122: 216-222, 2017.

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

6

Penta-EF-hand domain containing 1

Endoplasmic reticulum. Cytoplasm. Membrane. Peripheral membrane protein. COPII-coated vesicle membrane. Peripheral membrane protein.

Rabbit IgG

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