Anti-ErbB 2/ERBB2 Antibody Picoband™
384.81 €
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product details
Catalog number: 519 - A00010-2
Product Category: Business & Industrial > Science & Laboratory
Gentaur
Size: 100ug/vial
5153-002mg
erbB-2 Antibody
erbB-2 Antibody: The ErbB family consists of four closely related tyrosine kinase receptors that act as potent mediators of normal cell growth and development. Aberrant expression or function of one or more of these receptors can play a major role in the development and evolution of cancer. ErbB-2, also known as HER2, has been implicated in the evolution of both breast and gastric cancers, and is evident in other cancer types such as ovarian and salivary gland tumors. ErbB-2 possesses an active tyrosine kinase domain, but no direct ligand has been identified yet. ErbB-2 is the preferred binding partner to the other members of the ErbB family and is thought to act primarily through the Ras-MAPK, PI3k-PKB/Akt, and PLC-PKC signaling pathways. Numerous anti-cancer strategies have been employed against erbB-2, such as antibody-based therapies to prevent ligand binding or receptor activation through dimerization, antibody-dependent cell mediated cytotoxicity, in addition to direct kinase inhibition to prevent molecular activation/downstream signaling.
443.66 €
BT-MCA0504-50ul
ErbB-3 Monoclonal Antibody
This gene encodes a member of the epidermal growth factor receptor (EGFR) family of receptor tyrosine kinases. This membrane-bound protein has a neuregulin binding domain but not an active kinase domain. It therefore can bind this ligand but not convey the signal into the cell through protein phosphorylation. However, it does form heterodimers with other EGF receptor family members which do have kinase activity. Heterodimerization leads to the activation of pathways which lead to cell proliferation or differentiation. Amplification of this gene and/or overexpression of its protein have been reported in numerous cancers, including prostate, bladder, and breast tumors. Alternate transcriptional splice variants encoding different isoforms have been characterized. One isoform lacks the intermembrane region and is secreted outside the cell. This form acts to modulate the activity of the m
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BT-AP03039-100ul
ErbB-3 Polyclonal Antibody
ERBB3 encodes a member of the epidermal growth factor receptor (EGFR) family of receptor tyrosine kinases. This membrane-bound protein has a neuregulin binding domain but not an active kinase domain. It therefore can bind this ligand but not convey the signal into the cell through protein phosphorylation. However, it does form heterodimers with other EGF receptor family members which do have kinase activity. Heterodimerization leads to the activation of pathways which lead to cell proliferation or differentiation. Amplification of this gene and/or overexpression of its protein have been reported in numerous cancers, including prostate, bladder, and breast tumors. Alternate transcriptional splice variants encoding different isoforms have been characterized. One isoform lacks the intermembrane region and is secreted outside the cell. This form acts to modulate the activity of the membrane-bound form. Additional splice variants have also been reported, but they have not been thoroughly characterized.
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BT-AP03039-20ul
ErbB-3 Polyclonal Antibody
ERBB3 encodes a member of the epidermal growth factor receptor (EGFR) family of receptor tyrosine kinases. This membrane-bound protein has a neuregulin binding domain but not an active kinase domain. It therefore can bind this ligand but not convey the signal into the cell through protein phosphorylation. However, it does form heterodimers with other EGF receptor family members which do have kinase activity. Heterodimerization leads to the activation of pathways which lead to cell proliferation or differentiation. Amplification of this gene and/or overexpression of its protein have been reported in numerous cancers, including prostate, bladder, and breast tumors. Alternate transcriptional splice variants encoding different isoforms have been characterized. One isoform lacks the intermembrane region and is secreted outside the cell. This form acts to modulate the activity of the membrane-bound form. Additional splice variants have also been reported, but they have not been thoroughly characterized.