KRAS Mouse Monoclonal Antibody [A8E5] (HA601059)

UNIPROT #

P01116

PROTEIN NAME

KRAS

SYNONYMS

c Ki ras2 antibody;c Kirsten ras protein antibody;c-K-ras antibody;c-Ki-ras antibody;Cellular c Ki ras2 proto oncogene antibody;Cellular transforming proto oncogene antibody;CFC2 antibody;cK Ras antibody;GTPase KRas antibody;K RAS p21 protein antibody;K RAS2A antibody;K RAS2B antibody;K RAS4A antibody;K RAS4B antibody;K-Ras 2 antibody;KI RAS antibody;Ki-Ras antibody;KIRSTEN MURINE SARCOMA VIRUS 2 antibody;Kirsten rat sarcoma 2 viral (v Ki ras2) oncogene homolog antibody;Kirsten rat sarcoma viral oncogene homolog antibody;KRAS antibody;KRAS proto oncogene, GTPase antibody;KRAS1 antibody;KRAS2 antibody;N-terminally processed antibody;NS antibody;NS3 antibody;Oncogene KRAS2 antibody;p21ras antibody;PR310 c K ras oncogene antibody;PR310 cK ras oncogene antibody;RALD antibody;RASK_HUMAN antibody;RASK2 antibody;Transforming protein p21 antibody;v Ki ras2 Kirsten rat sarcoma 2 viral oncogene homolog antibody;v Ki ras2 Kirsten rat sarcoma viral oncogene homolog antibody

SUBCELLULAR LOCATION

Cell membrane. Cytoplasm.

FUNCTION

The K-Ras protein is a GTPase, a class of enzymes which convert the nucleotide guanosine triphosphate (GTP) into guanosine diphosphate (GDP). In this way the K-Ras protein acts like a switch that is turned on and off by the GTP and GDP molecules. To transmit signals, it must be turned on by attaching (binding) to a molecule of GTP. The K-Ras protein is turned off (inactivated) when it converts the GTP to GDP. When the protein is bound to GDP, it does not relay signals to the cell's nucleus. Several germline KRAS mutations have been found to be associated with Noonan syndrome and cardio-facio-cutaneous syndrome. Somatic KRAS mutations are found at high rates in leukemias, colorectal cancer, pancreatic cancer and lung cancer. KRAS mutations are more commonly observed in cecal cancers than colorectal cancers located in any other places from ascending colon to rectum. KRAS gene can also be amplified in colorectal cancer. Tumors or cell lines harboring this genetic lesion are not responsive to EGFR inhibitors. Although KRAS amplification is an infrequent event in colorectal cancer, it might be responsible for precluding response to anti-EGFR treatment in some patients. Amplification of wild-type Kras has also been observed in ovarian, gastric, uterine, and lung cancers. Driver mutations in KRAS underlie the pathogenesis of up to 20% of human cancers. Hence KRAS is an attractive drug target, however lack of obvious binding sites has hindered pharmaceutical development. One potential drug interaction site is where GTP/GDP binds. However, due to the extraordinarily high affinity of GTP/GDP for this site, it is unlikely that drug-like small molecule inhibitors could compete with GTP/GDP binding. Other than where GTP/GDP binds, there are no obvious high affinity binding sites for small molecules.