Anti-OCT1/Slc22a1 Antibody Picoband® Fluoro647 Conjugated

Solute carrier family 22 (organic cation transporter), member 1, also called SLC22A1 or OCT1 is a protein that in humans is encoded by the SLC22A1 gene. This gene is mapped to 6q25.3. Polyspecific organic cation transporters in the liver, kidney, intestine, and other organs are critical for elimination of many endogenous small organic cations as well as a wide array of drugs and environmental toxins. This gene transports the polyamines spermine and spermidine. It also transports pramipexole across the basolateral membrane of the proximal tubular epithelial cells. This gene regulated by various intracellular signaling pathways including inhibition by protein kinase A activation, and endogenously activation by the calmodulin complex, the calmodulin-dependent kinase II and LCK tyrosine kinase.

A synthetic peptide corresponding to a sequence in the middle region of mouse OCT1/Slc22a1, which shares 66.7% and 94.4% amino acid (aa) sequence identity with human and rat SLC22A1, respectively.

Domain Families, Epigenetics and Nuclear Signaling, Protein Phosphorylation, Receptor Tyrosine Kinases, Signal Transduction, Transcription, Transcription Factors, Tyrosine Kinases, Zinc Finger

Calcium-activated, phospholipid- and diacylglycerol (DAG) -dependent serine/threonine-protein kinase involved in various cellular processes such as regulation of the B-cell receptor (BCR) signalosome, oxidative stress-induced apoptosis, androgen receptor-dependent transcription regulation, insulin signaling and endothelial cells proliferation. Plays a key role in B-cell activation by regulating BCR-induced NF-kappa-B activation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by phosphorylation of CARD11/CARMA1 at 'Ser-559', 'Ser-644' and 'Ser-652'. Phosphorylation induces CARD11/CARMA1 association with lipid rafts and recruitment of the BCL10-MALT1 complex as well as MAP3K7/TAK1, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. Plays a role in the negative feedback regulation of the BCR signaling, by down-modulating BTK function via phosphorylation of BTK at 'Ser-180', which results in the alteration of BTK plasma membrane localization and in turn inhibition of BTK activity. Involved in apoptosis following oxidative damage: in case of oxidative conditions, specifically phosphorylates 'Ser-36' of isoform p66Shc of SHC1, leading to mitochondrial accumulation of p66Shc, where p66Shc acts as a reactive oxygen species producer. Acts as a coactivator of androgen receptor (ANDR) -dependent transcription, by being recruited to ANDR target genes and specifically mediating phosphorylation of 'Thr-6' of histone H3 (H3T6ph), a specific tag for epigenetic transcriptional activation that prevents demethylation of histone H3 'Lys-4' (H3K4me) by LSD1/KDM1A. In insulin signaling, may function downstream of IRS1 in muscle cells and mediate insulin-dependent DNA synthesis through the RAF1-MAPK/ERK signaling cascade. May participate in the regulation of glucose transport in adipocytes by negatively modulating the insulin-stimulated translocation of the glucose transporter SLC2A4/GLUT4. Under high glucose in pancreatic beta-cells, is probably involved in the inhibition of the insulin gene transcription, via regulation of MYC expression. In endothelial cells, activation of PRKCB induces increased phosphorylation of RB1, increased VEGFA-induced cell proliferation, and inhibits PI3K/AKT-dependent nitric oxide synthase (NOS3/eNOS) regulation by insulin, which causes endothelial dysfunction. Also involved in triglyceride homeostasis (By similarity) . Phosphorylates ATF2 which promotes cooperation between ATF2 and JUN, activating transcription.

1. Leabman, M. K., Huang, C. C., DeYoung, J., Carlson, E. J., Taylor, T. R., de la Cruz, M., Johns, S. J., Stryke, D., Kawamoto, M., Urban, T. J., Kroetz, D. L., Ferrin, T. E. Clark, A. G.; Risch, N.; Herskowitz, I.; Giacomini, K. M.; {Pharmacogenetics of Membrane Transporters Investigators}: Natural variation in human membrane transporter genes reveals evolutionary and functional constraints. Proc. Nat. Acad. Sci. 100: 5896-5901, 2003. 2. Shu, Y., Sheardown, S. A., Brown, C., Owen, R. P., Zhang, S., Castro, R. A., Ianculescu, A. G., Yue, L., Lo, J. C., Burchard, E. G., Brett, C. M., Giacomini, K. M. Effect of genetic variation in the organic cation transporter 1 (OCT1) on metformin action. J. Clin. Invest. 117: 1422-1431, 2007.