ErbB-2 Human Recombinant
Tyrosine Kinase ErbB-2 Human Recombinant, Sf9
ErbB2 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 638 amino acids (23-652) and having a molecular mass of 70.4kDa (Molecular size on SDS-PAGE will appear at approximately 70-100kDa). ErbB2 is fused to 8 amino acid IgG His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Tyrosine Kinase ErbB-3 Human Recombinant
Tyrosine Kinase ErbB-3 Human Recombinant, sf9
Tyrosine Kinase ErbB-3 Mouse Recombinant
Tyrosine Kinase ErbB-4 Human Recombinant
ErbB4 Human Recombinant produced in HEK293 Cells is a single, glycosylated polypeptide chain containing 863 amino acids (26-649 a.a) and having a molecular mass of 96.6 kDa.
ErbB4 is fused to a 239 amino acid hIgG-His-Tag at C-terminus & purified by proprietary chromatographic techniques.
Tyrosyl-DNA Phosphodiesterase 1 Human Recombinant, Sf9
TDP1 Human Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 617 amino acids (1-608) and having a molecular mass of 69.5kDa. TDP1 is fused to 6 amino acid His-Tag at C-terminus and purified by proprietary chromatographic techniques.
TYRO3 Protein Tyrosine Kinase Mouse Recombinant
TYRO3 Mouse produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 628 amino acids (31-419 aa) and having a molecular mass of 68.9kDa.
TYRO3 is fused to a 239 amino acid hIgG-His-Tag at C-terminus and purified by proprietary chromatographic techniques.
Tyrosine kinases are enzymes that transfer a phosphate group from ATP to the tyrosine residues of specific proteins inside a cell. This process, known as phosphorylation, acts as an “on” or “off” switch in many cellular functions . Tyrosine kinases are classified into two main types:
Tyrosine kinases play crucial roles in cellular communication, growth, and differentiation. They are expressed in various tissues and have distinct expression patterns . For example, RTKs are often found on the cell surface, while NRTKs are located within the cell . Their tissue distribution is widespread, affecting numerous cellular processes.
Tyrosine kinases interact with other molecules and cells through binding partners and downstream signaling cascades . For instance, RTKs bind to extracellular signaling molecules, causing dimerization and activation of their kinase domains . This leads to autophosphorylation and the activation of downstream signaling proteins .
The expression and activity of tyrosine kinases are tightly regulated through various mechanisms, including transcriptional regulation and post-translational modifications . For example, ligand binding to RTKs triggers dimerization and autophosphorylation, which activates the kinase domains . Additionally, protein tyrosine phosphatases remove phosphate groups, turning off the signaling pathways .
Tyrosine kinases have numerous applications in biomedical research, diagnostic tools, and therapeutic strategies . They are targets for cancer treatment, with tyrosine kinase inhibitors (TKIs) being used to block the activity of specific kinases involved in tumor growth . Additionally, they serve as biomarkers for various diseases and are used in diagnostic assays .