Background[1-3]
Phosphorylated protein tyrosine kinase 9 antibody is a type of polyclonal antibody that can specifically bind to phosphorylated protein tyrosine kinase 9. It is mainly used in immunological experiments to detect phosphorylated protein tyrosine kinase 9 in vitro.
Tyrosine kinases can be divided into three categories: ① Receptor tyrosine kinases, which are single-pass transmembrane proteins, and more than 50 species have been found in vertebrates; ② Cytoplasmic tyrosine kinases, such as the Src family, Tec family, ZAP70 family, JAK family, etc.; ③ Nuclear tyrosine kinases such as Abl and Wee.
The extracellular region of receptor tyrosine kinases (RPTKs) is a binding ligand domain. The ligands are soluble or membrane-bound polypeptide or protein hormones, including insulin and various growth factors. The intracellular segment is the catalytic site of tyrosine protein kinase, and the chain extender has an autophosphorylation site.
Ligands (such as EGF) bind to receptors extracellularly and cause conformational changes, leading to dimerization of the receptors to form homo- or heterodimers, in which each other phosphorylates each other intracellularly. A segment of tyrosine residues activates the tyrosine protein kinase activity of the receptor itself. Such ligands mainly include EGF, PDGF, FGF, etc.
Receptor tyrosine kinase exists as a monomer and is inactive when not bound to a signaling molecule; once a signaling molecule binds to the extracellular domain of the receptor, the two monomeric receptor molecules bind to the membrane On forming a dimer, the tails of the intracellular domains of the two receptors come into contact with each other, activating their protein kinase functions, resulting in phosphorylation of tyrosine residues in the tails. Phosphorylation causes the tail of the receptor’s intracellular domain to assemble into a signaling complex. The newly phosphorylated tyrosine site immediately becomes the binding site for intracellular signaling proteins. There may be 10 to 20 different intracellular signaling proteins that are activated after binding to the phosphorylated site on the receptor tail. Signaling complexes amplify information through several different signal transduction pathways and activate a series of biochemical reactions in cells; or they combine different information to cause a comprehensive response of cells (such as cell proliferation).
Apply[4][5]
Study on the molecular mechanism of selective splicing of Bcl-X in pancreatic cancer cells induced by tyrosine kinase Fyn
Pancreatic cancer is a malignant tumor with a high degree of malignancy, and its incidence rate is on the rise both at home and abroad. It currently ranks second among the causes of death from digestive tract cancer, and the 5-year survival rate is less than 4%. Early invasion and metastasis are important features of pancreatic cancer and key factors for poor prognosis.
It is currently believed that abnormal activation of signaling molecules plays an important role in tumor invasion and metastasis. Among them, the activation of the Src superfamily of non-receptor tyrosine kinases and related signaling molecules is particularly noteworthy. The Src superfamily of non-receptor tyrosine kinases is composed of Src, Fyn, Yes, Lyn and other members. This superfamily plays a very important role in cell proliferation, differentiation, mitosis, apoptosis and other processes.
Research shows that almost all solid tumors have high expression and overactivation of Src, which is closely related to the occurrence and development of tumors. Fyn, a member of the Src family, has been reported to have increased expression in brain tumors and head and neck tumors, suggesting that Fyn can also participate in tumor invasion and metastasis.
However, there are currently no studies on Fyn’s involvement in pancreatic cancer invasion and metastasis and its molecular mechanisms. During the process of tumor invasion and metastasis, tumor cells need to be detached from their original location and enter the blood circulation to reach the target organ. Only tumor cells with resistance to anoikis can grow in the target organ and eventually form metastases. Therefore, the regulation of apoptosis can directly affect the invasion and metastasis ability of tumor cells.
