Note: Application as IHC, only suitable for histochemical staining or fluorescence staining of paraffin-embedded sections. Application as ICC/IF, suitable for histochemical or fluorescent staining of frozen sections, as well as chemical and fluorescent staining at the cellular level.
注意:抗体应用为IHC的,抗体只适合于石蜡切片的组化染色或者荧光染色。
抗体应用为IF/ICC的,抗体适合于冰冻切片的组化染色或者荧光染色,以及细胞水平的化学染色和荧光染色。
ABMART实验方案下载
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.
GTPase KRas (EC 3.6.5.2) (K-Ras 2) (Ki-Ras) (c-K-ras) (c-Ki-ras) [Cleaved into: GTPase KRas, N-terminally processed] KRAS KRAS2 RASK2
Human,Mouse,Rat
WB,IF,ICC,FC
WB 1:500-1:1000IF 1:200ICC 1:100-1:400FC 1:500-1:1000
Predicted band size: 21 kDa
KRAS KRAS2 RASK2
p01116
Mouse
Monoclonal
Mouse IgG2b
Rat brain tissue lysate, Jurkat cell lysate, N2A cell lysate, PC-12 cell lysate, human kidney tissue lysate, Hela, NIH/3T3.
Protein A affinity purified.
PBS (pH7.4), 0.1% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Store at +4℃ after thawing. For long-term storage, please store it at -20℃. Avoid repeated freeze / thaw cycles.
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