Anti-CPT1A Antibody Picoband® Fluoro647 Conjugated

The mitochondrial oxidation of long-chain fatty acids is initiated by the sequential action of carnitine palmitoyltransferase I (which is located in the outer membrane and is detergent-labile) and carnitine palmitoyltransferase II (which is located in the inner membrane and is detergent-stable), together with a carnitine-acylcarnitine translocase. CPT I is the key enzyme in the carnitine-dependent transport across the mitochondrial inner membrane and its deficiency results in a decreased rate of fatty acid beta-oxidation. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.

Detected in T-47D, MDA-MB-175 and HBL-100 breast carcinoma cells, A-431 epidermoid carcinoma cells, SW48 and SNU-C2B colon carcinoma cells and Hs 294T melanoma cells (at protein level) . Expressed at low levels in most adult tissues and is highest in the brain, lung, placenta and kidney. Lower levels of expression are detected in melanocytes, heart, liver, skeletal muscle and pancreas. Abundant in breast carcinoma cell lines. In the colonic mucosa, expressed in epithelia but not in the connective tissue of the lamina propria. In the thyroid gland, expressed in the epithelium of the thyroid follicles. In pancreas, expressed in the islets of Langerhans cells, but not in the surrounding epithelial cells of the exocrine pancreas. In kidney, expressed in the epithelia of the distal tubules. Not expressed in connective tissue, endothelial cells, adipose tissue, muscle cells or cells of hematopoietic origin.

Angiogenesis, Cancer, Cancer Metabolism, Cardiovascular, Growth Factors, Growth Factors/Hormones, Hematopoietic Progenitors, Host-Virus Interaction, Interspecies Interaction, Invasion/Microenvironment, Metabolism, Metabolism Processes, Microbiology, Oncoproteins, Oncoproteins/Suppressors, Pathways and Processes, Protein Phosphorylation, Receptor Tyrosine Kinases, Response To Hypoxia, Signal Transduction, Stem Cells, Surface Molecules, Tyrosine Kinases

Potent inhibitor of the complement membrane attack complex (MAC) action. Acts by binding to the C8 and/or C9 complements of the assembling MAC, thereby preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore (By similarity) .

1. Andersen, M. K., Hansen, T. Genetics of metabolic traits in Greenlanders: lessons from an isolated population. J. Intern. Med. 284: 464-477, 2018. 2. Andersen, M. K., Jorsboe, E., Sandholt, C. H., Grarup, N., Jorgensen, M. E., Faergeman, N. J., Bjerregaard, P., Pedersen, O., Moltke, I., Hansen, T., Albrechtsen, A. Identification of novel genetic determinants of erythrocyte membrane fatty acid composition among Greenlanders. PLoS Genet. 12: e1006119, 2016. Note: Electronic Article. 3. Bergstrom, J. P., Reitz, R. C. Studies on carnitine palmitoyl transferase: the similar nature of CPTi (inner form) and CPTo (outer form) . Arch. Biochem. Biophys. 204: 71-78, 1980.