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In vitro transcription of capped mRNA with modified nucleotides and Poly(A) tail
TSA (Tyramide Signal Amplification), used for signal amplification of ISH, IHC and IC etc.
Separation of phosphorylated and non-phosphorylated proteins without phospho-specific antibody
A convenient and sensitive way for cell proliferation assay and cytotoxicity assay
Protect the integrity of proteins from multiple proteases and phosphatases for different applications.
Vascular endothelial growth factor receptor 2 (VEGFR-2) belongs to the family of receptor tyrosine kinases (RTKs) and is almost exclusively restricted to endothelial cells. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. VEGFR-2 has seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 mediates mitogenic activity in endothelial cells, which leading to their proliferation. The binding of VEGF165 to VEGFR-2 is dependent on heparin.
Recombinant human VEGFR-2 is produced in baculovirus as a monomeric, glycosylated, polypeptide and having a total molecular mass of 116 kDa. The soluble receptor protein contains only the first 7 extracellular domains, which contain all the information necessary for ligand binding. The VEGFR-2 is purified by proprietary chromatographic techniques.