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Epidermal growth factor (EGF) family is a group of growth factors with similar structural to EGF which is a potent mitogenic peptide. EGF family members include transforming growth factor-α (TGF-alpha), heparin-binding EGF-like growth factor (HB-EGF), amphiregulin, betacellulin, epiregulin, epigen, neuregulins 1-6. The biological effects of the EGF family members are mediated by the EGF receptor (EGFR/ErbB) tyrosine kinase family, which consists of four members: EGFR (ERBB1), ERBB2 (NEU/HER2 receptor), ERBB3, and ERBB4. EGF receptors are activated following the binding of ligands, and then activate signaling cascades that have many effects: cell proliferation, reduced apoptosis, and angiogenesis.
EGF Protein, a growth factor, is essential for cell growth, proliferation, and differentiation. It binds to the EGF receptor, activating signaling pathways that regulate cell survival and tissue repair. EGF Protein has therapeutic potential in promoting wound healing, tissue regeneration, and cancer treatment. Its role in cellular processes makes it a subject of interest in biomedical research. EGF Protein, Mouse (His) is the recombinant mouse-derived EGF protein, expressed by E. coli , with C-6*His labeled tag. The total length of EGF Protein, Mouse (His) is 53 a.a., with molecular weight of 9-14 kDa.
EGF proteins act as potent stimulators of growth in a variety of epidermal and epithelial tissues in both in vivo and in vitro settings, while promoting the proliferation of specific fibroblasts in cell culture. This multifaceted protein also acts as a magnesium stimulating hormone, driving magnesium reabsorption in the renal distal tubule through engagement of EGFR and activation of the magnesium channel TRPM6. GMP EGF Protein, Human is the recombinant human-derived EGF protein, expressed by E. coli , with tag free. The total length of GMP EGF Protein, Human is 53 a.a., with molecular weight of ~9.6 kDa.
NRG1-alpha protein acts as a direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors, concurrently recruiting ERBB1 and ERBB2 coreceptors, thereby inducing ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. The diverse functions of its multiple isoforms encompass the induction of growth and differentiation in various cell types, including epithelial, glial, neuronal, and skeletal muscle cells. NRG1-alpha is also involved in the expression of acetylcholine receptors during neuromuscular junction formation, the stimulation of lobuloalveolar budding and milk production in the mammary gland, and the induction of differentiation in mammary tumor cells. Furthermore, it stimulates Schwann cell proliferation and plays a role in myocardial development, specifically contributing to the trabeculation of the developing heart. Isoform 10 is implicated in motor and sensory neuron development. NRG1-alpha binds to ERBB4 and ERBB3, acting as a ligand for integrins and forming a ternary complex with integrins and ERBB3, a crucial step in NRG1-ERBB signaling. It induces the phosphorylation and activation of MAPK3/ERK1, MAPK1/ERK2, and AKT1. Additionally, NRG1-alpha participates in ligand-dependent ERBB4 endocytosis, essential for the activation of these kinases in neurons, and interacts with the LIM domain region of LIMK1. It also forms a ternary complex with ERBB3 and integrins ITGAV:ITGB3 or ITGA6:ITGB4 and interacts with NRDC and BACE1. NRG1-beta 1 Protein, Human (HEK293) is the recombinant human-derived NRG1-beta 1 protein, expressed by HEK293 , with tag free. The total length of NRG1-beta 1 Protein, Human (HEK293) is 245 a.a., with molecular weight of ~26.8 kDa.
Epiregulin Protein, a ligand for EGFR and ERBB4, crucially influences inflammation, wound healing, tissue repair, and oocyte maturation. It stimulates tyrosine phosphorylation of both receptors, regulating angiogenesis, vascular remodeling, and cell proliferation. Interactions with EGFR and ERBB4 contribute to intricate signaling pathways, essential for diverse physiological responses and cellular functions. Epiregulin Protein, Human (HEK293, Fc) is the recombinant human-derived Epiregulin protein, expressed by HEK293 , with N-hFc labeled tag. The total length of Epiregulin Protein, Human (HEK293, Fc) is 46 a.a., with molecular weight of ~35 kDa.
The HER2/CD340 protein is a dynamic tyrosine kinase that is essential in the neuregulin receptor complex and regulates microtubule dynamics. Upon activation, it triggers the MEMO1-RHOA-DIAPH1 pathway, inhibits GSK3B and promotes the association of APC and CLASP2 on the cell membrane to achieve microtubule stabilization. HER2/CD340 Protein, Human (Biotinylated, HEK293, Fc-Avi) is the recombinant human-derived HER2/CD340 protein, expressed by HEK293 , with C-Avi, C-hFc labeled tag. The total length of HER2/CD340 Protein, Human (Biotinylated, HEK293, Fc-Avi) is 630 a.a., with molecular weight of 120-140 kDa.
The Progranulin/PGRN protein is involved in a variety of cellular processes, including cell growth, inflammation, and neurodegeneration. It acts as a regulator of tissue repair and has been implicated in the pathogenesis of several diseases, including Alzheimer's disease and frontotemporal dementia. Progranulin/PGRN interacts with various receptors and signaling pathways to exert its effects on cellular function and disease progression. EGF Protein, Human (Solution, HEK293, N-hFc) is the recombinant human-derived EGF protein, expressed by HEK293 , with N-hFc labeled tag. The total length of EGF Protein, Human (Solution, HEK293, N-hFc) is 53 a.a., with molecular weight of ~37 kDa.
EGF Protein, a growth factor, is essential for cell growth, proliferation, and differentiation. It binds to the EGF receptor, activating signaling pathways that regulate cell survival and tissue repair. EGF Protein has therapeutic potential in promoting wound healing, tissue regeneration, and cancer treatment. Its role in cellular processes makes it a subject of interest in biomedical research. EGF Protein, Mouse (HEK293) is the recombinant mouse-derived EGF protein, expressed by HEK293 , with tag free. The total length of EGF Protein, Mouse (HEK293) is 53 a.a., with molecular weight of ~7 kDa.
The EGFR protein is a receptor tyrosine kinase that can bind to a variety of ligands, such as EGF, TGFA, AREG, epigen, BTC, epiregulin, and HBEGF, to initiate signaling cascades that mediate cellular responses. This involves receptor dimerization, autophosphorylation and recruitment of adapter proteins such as GRB2, activating downstream pathways such as RAS-RAF-MEK-ERK, PI3-kinase-AKT, PLCgamma-PKC and STAT. EGFR Protein, Human (sf9, His-GST) is the recombinant human-derived EGFR protein, expressed by Sf9 insect cells , with N-His, N-GST labeled tag. The total length of EGFR Protein, Human (sf9, His-GST) is 543 a.a., with molecular weight of ~89.1 kDa.
HER4 is an important tyrosine protein kinase receptor for members of the neuregulin and EGF families that directs heart, central nervous system, and mammary gland development. It is critical for myocardial differentiation, postnatal cardiomyocyte proliferation, neural crest cell migration, axon guidance, and mammary gland function. HER4 Protein, Human (HEK293, His-Fc) is the recombinant human-derived HER4 protein, expressed by HEK293 , with C-hFc, C-10*His labeled tag. The total length of HER4 Protein, Human (HEK293, His-Fc) is 626 a.a., with molecular weight of 125-135 kDa.
The HER2/CD340 protein is a dynamic tyrosine kinase that is essential in the neuregulin receptor complex and regulates microtubule dynamics. Upon activation, it triggers the MEMO1-RHOA-DIAPH1 pathway, inhibits GSK3B and promotes the association of APC and CLASP2 on the cell membrane to achieve microtubule stabilization. HER2/CD340 Protein, Human (HEK293) is the recombinant human-derived HER2/CD340 protein, expressed by HEK293 , with tag free. The total length of HER2/CD340 Protein, Human (HEK293) is 630 a.a., with molecular weight of 100-110 kDa.
NRG1-alpha protein acts as a direct ligand for ERBB3 and ERBB4 tyrosine kinase receptors, concurrently recruiting ERBB1 and ERBB2 coreceptors, thereby inducing ligand-stimulated tyrosine phosphorylation and activation of the ERBB receptors. The diverse functions of its multiple isoforms encompass the induction of growth and differentiation in various cell types, including epithelial, glial, neuronal, and skeletal muscle cells. NRG1-alpha is also involved in the expression of acetylcholine receptors during neuromuscular junction formation, the stimulation of lobuloalveolar budding and milk production in the mammary gland, and the induction of differentiation in mammary tumor cells. Furthermore, it stimulates Schwann cell proliferation and plays a role in myocardial development, specifically contributing to the trabeculation of the developing heart. Isoform 10 is implicated in motor and sensory neuron development. NRG1-alpha binds to ERBB4 and ERBB3, acting as a ligand for integrins and forming a ternary complex with integrins and ERBB3, a crucial step in NRG1-ERBB signaling. It induces the phosphorylation and activation of MAPK3/ERK1, MAPK1/ERK2, and AKT1. Additionally, NRG1-alpha participates in ligand-dependent ERBB4 endocytosis, essential for the activation of these kinases in neurons, and interacts with the LIM domain region of LIMK1. It also forms a ternary complex with ERBB3 and integrins ITGAV:ITGB3 or ITGA6:ITGB4 and interacts with NRDC and BACE1. NRG1-alpha Protein, Human (HEK293, His) is the recombinant human-derived NRG1-alpha protein, expressed by HEK293 , with C-His, C-6*His labeled tag. The total length of NRG1-alpha Protein, Human (HEK293, His) is 222 a.a., with molecular weight of 40-50 kDa.
The EGFR protein is a receptor tyrosine kinase that can bind to a variety of ligands, such as EGF, TGFA, AREG, epigen, BTC, epiregulin, and HBEGF, to initiate signaling cascades that mediate cellular responses. This involves receptor dimerization, autophosphorylation and recruitment of adapter proteins such as GRB2, activating downstream pathways such as RAS-RAF-MEK-ERK, PI3-kinase-AKT, PLCgamma-PKC and STAT. EGFR Protein, Human (Biotinylated, 621a.a, HEK293, His) is the recombinant human-derived EGFR protein, expressed by HEK293 , with C-His labeled tag. The total length of EGFR Protein, Human (Biotinylated, 621a.a, HEK293, His) is 621 a.a., with molecular weight of ~99.5 kDa.
EGFR Protein, a receptor tyrosine kinase, binds various ligands like EGF, TGFA, AREG, epigen, BTC, epiregulin, and HBEGF, initiating signaling cascades that mediate cellular responses. This involves receptor dimerization, autophosphorylation, and recruitment of adapter proteins like GRB2, activating downstream pathways such as RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC, and STATs. EGFR can also trigger NF-kappa-B signaling, phosphorylate proteins like RGS16, and interact with MUC1, influencing G protein-coupled receptor signaling. Moreover, it enhances cell migration through interactions with CCDC88A, promoting EGFR signaling and triggering cell migration. Additionally, EGFR impacts learning, memory, and pain signaling. EGFR Protein, Human (621a.a, HEK293, Fc) is the recombinant human-derived EGFR protein, expressed by HEK293, with C-hFc labeled tag. The total length of EGFR Protein, Human (621a.a, HEK293, Fc) is 621 a.a., with molecular weight of 110-160 kDa.
The EGFR protein is a receptor tyrosine kinase that can bind to a variety of ligands, such as EGF, TGFA, AREG, epigen, BTC, epiregulin, and HBEGF, to initiate signaling cascades that mediate cellular responses. This involves receptor dimerization, autophosphorylation and recruitment of adapter proteins such as GRB2, activating downstream pathways such as RAS-RAF-MEK-ERK, PI3-kinase-AKT, PLCgamma-PKC and STAT. EGFR Protein, Human (Biotinylated, HEK293, His-Avi) is the recombinant human-derived EGFR protein, expressed by HEK293 , with C-Avi, C-His labeled tag. The total length of EGFR Protein, Human (Biotinylated, HEK293, His-Avi) is 621 a.a., with molecular weight of 80-110 kDa.
The HER2/CD340 protein is a dynamic tyrosine kinase that is essential in the neuregulin receptor complex and regulates microtubule dynamics. Upon activation, it triggers the MEMO1-RHOA-DIAPH1 pathway, inhibits GSK3B and promotes the association of APC and CLASP2 on the cell membrane to achieve microtubule stabilization. HER2/CD340 Protein, Human (Biotinylated, HEK293, His-Avi) is the recombinant human-derived HER2/CD340 protein, expressed by HEK293 , with C-Avi, C-His labeled tag. The total length of HER2/CD340 Protein, Human (Biotinylated, HEK293, His-Avi) is 630 a.a., with molecular weight of 80-100 kDa.
HER2/CD340 Protein, a dynamic tyrosine kinase, is crucial in neuregulin-receptor complexes and regulates microtubule dynamics. Upon activation, it triggers the MEMO1-RHOA-DIAPH1 pathway, inhibiting GSK3B and facilitating APC and CLASP2 association at the cell membrane for microtubule stabilization. In the nucleus, HER2/CD340 Protein activates PTGS2/COX-2 and rRNA genes, contributing to transcriptional regulation and protein synthesis. Its multifaceted activities emphasize its central role in cellular processes, spanning receptor signaling, microtubule dynamics, and transcriptional control. HER2/CD340 Protein, Human (S310Y, HEK293, His) is the recombinant human-derived HER2/CD340 protein, expressed by HEK293 , with C-10*His labeled tag and S310Y mutation. The total length of HER2/CD340 Protein, Human (S310Y, HEK293, His) is 630 a.a., with molecular weight of 80-100 kDa.
HER2/CD340 Protein, a dynamic tyrosine kinase, is crucial in neuregulin-receptor complexes and regulates microtubule dynamics. Upon activation, it triggers the MEMO1-RHOA-DIAPH1 pathway, inhibiting GSK3B and facilitating APC and CLASP2 association at the cell membrane for microtubule stabilization. In the nucleus, HER2/CD340 Protein activates PTGS2/COX-2 and rRNA genes, contributing to transcriptional regulation and protein synthesis. Its multifaceted activities emphasize its central role in cellular processes, spanning receptor signaling, microtubule dynamics, and transcriptional control. Her2/CD340 Protein, Human (Biotinylated, HEK293, His) is the recombinant human-derived Her2/CD340 protein, expressed by HEK293, with C-His labeled tag. The total length of Her2/CD340 Protein, Human (Biotinylated, HEK293, His) is 630 a.a., with molecular weight of 80-110 kDa.
EGF protein does not possess the conserved residue(s) necessary for propagating feature annotation. Animal-Free EGF Protein, Human (His) is the recombinant human-derived animal-FreeEGF protein, expressed by E. coli , with C-His labeled tag. The total length of Animal-Free EGF Protein, Human (His) is 53 a.a., with molecular weight of ~7.16 kDa.
TGF α/TGFA protein is a mitogenic polypeptide that binds to EGFR and acts synergistically with TGF β to promote anchorage-dependent cell proliferation. Its interaction with MAGI3, SDCBP, and the SNTA1 PDZ domain, especially with SDCBP, is critical for efficient cell surface targeting. Animal-Free TGF alpha/TGFA Protein, Human (His) is the recombinant human-derived animal-FreeTGF alpha/TGFA protein, expressed by E. coli , with C-His labeled tag. The total length of Animal-Free TGF alpha/TGFA Protein, Human (His) is 50 a.a., with molecular weight of ~6.49 kDa.