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Strictinin is an orally active phenolic compound. Strictinin reduces xanthine oxidase activity, uric acid production, and the activation of ERK1/2, JNK, NF-κB, and NLRP3 inflammasome components in hepatocytes treated with Xanthine (HY-W017389). Strictinin decreases elevated serum uric acid levels and enhanced xanthine oxidase activity in mice treated with potassium oxonate. Strictinin acts as a ROR1 inhibitor and exhibits anticancer activity against highly aggressive non-androgen-dependent prostate cancer. Strictinin induces cancer cell apoptosis (apoptosis), arrests cell cycle, and inhibits cancer cell migration, invasion, and epithelial-mesenchymal transition. Strictinin modulates gut microbiota, inhibits bacterial growth and biofilm formation, accelerates small intestinal transit, and blocks viral entry and replication. Strictinin can be used in research related to hyperuricemia, androgen receptor-negative non-androgen-dependent prostate cancer, triple-negative breast cancer, bacterial infections, constipation, coronavirus infections, dental caries, and infections caused by influenza A, influenza B, and human parainfluenza virus type 1 .
Suraxavir marboxil (GP681; Cap-dependent endonuclease-IN-3) is a PA subunit cap-dependent endonuclease inhibitor with antiviral activity. Suraxavir marboxil inhibits PA subunit cap-dependent endonuclease activity and inhibits influenza A and/or influenza B viral replication. Suraxavir marboxil can be used alone or in combination with other anti-influenzal agents for the prevention of influenza A and/or influenza B viral infectious diseases. Suraxavir marboxil can be used for the research of influenza A and/or influenza B viral infectious diseases .
Noformicin has inhibitory effect on mumps virus and Newcastle disease virus in chicken embryo. Noformicin also extended the survival of mice infected with swine, influenza A (PR8) and influenza B (Lee) viruses .
S119-8 is a broad spectrum inhibitor of influenza A and B viruses, showing activity against multiple influenza B viruses and an oseltamivir-resistant influenza A virus, but does not inhibit a non-influenza virus, vesicular stomatitis nirus (VSV) .
Selenazofurin is an antiviral compound used against influenza A and influenza B viruses. Selenazofurin shows antiviral activity in cells against Measles, Para-3, Mumps, VV, HSV-2 with the ED50s of 3.7 μg/ml, 1.3 μg/ml, 8.0 μg/ml, 3.4 μg/ml, 4.3 μg/ml .
Ganoderic acid TR is a broad-spectrum inhibitor of influenza neuraminidase enzymes (NAs). Ganoderic acid TR has IC50 values of 10.9 and 4.6 μM for H5N1 and H1N1 NAs, respectively. Ganoderic acid TR is limited by cytotoxicity and shows only weak activity against Oseltamivir (HY-13317)-resistant H1N1 viruses and influenza B viruses .
Cap-dependent endonuclease-IN-8 is a potent inhibitor of cap-dependent endonuclease (CEN). Cap-dependent endonuclease-IN-8 inhibits replication of orthomyxoviruses (including influenza A, influenza B and influenza C) (extracted from patent CN111410661A, compound I-196) .
2-PADQZ is an antiviral compound with activity against influenza viruses. 2-PADQZ specifically binds to the influenza A virus RNA promoter and forms a binding site at the internal loop. 2-PADQZ has a significant inhibitory effect on H1N1 and H3N2 influenza A viruses and influenza B viruses .
Cap-dependent endonuclease-IN-7 is a potent inhibitor of cap-dependent endonuclease (CEN). Cap-dependent endonuclease-IN-7 Inhibits the synthesis of viral mRNA and eventually inhibits virus proliferation. Cap-dependent endonuclease-IN-7 has the potential for the research of viral infections (including influenza A, influenza B and influenza C) (extracted from patent WO2020177715A1, compound 5)
Cap-dependent endonuclease-IN-27 (Compound 8) is an orally active potent cap-dependent endonuclease (CEN) inhibitor. Cap-dependent endonuclease-IN-27, an antiviral agent, shows activity against influenza B virus. Cap-dependent endonuclease-IN-27 has inhibitory activity against IFV A/WSN/33 (H1N1) polymerase (EC50 = 12.26 nM) .
ATV03 is an anti-influenza virus agent with excellent anti-influenza A and B virus activity. ATV03 inhibits anti-influenza A (H3N2) and anti-influenza B with EC50 values of 0.78 nM and 2.02 nM, respectively. ATV03 exerts anti-influenza activity by inhibiting polymerase acidic protein (PA) and RNA-dependent RNA polymerase (RdRp), as well as disrupting nuclear protein .
BCX-1898, a cyclopentane derivative, is an orally active and selective influenza virus neuraminidase inhibitor. BCX-1898 has antiviral activity with EC50s of <0.01-21 μM on influenza A (H1N1, H3N2, and H5N1) and influenza B viruses replication in MDCK cells. BCX-1898 shows protection against the mouse influenza model .
Cap-dependent endonuclease-IN-10 is a potent inhibitor of cap-dependent endonuclease (CEN). Not only can Cap-dependent endonuclease-IN-10 inhibit influenza virus well, but also has lower cytotoxicity, better in vivo pharmacokinetic and in vivo pharmacodynamic properties, and better hepatic microsomal stability. Cap-dependent endonuclease-IN-10 has the potential for the research of viral infections (including influenza A, influenza B and influenza C) (extracted from patent WO2021129799A1, compound 1-1) .
Influenza virus-IN-10 is a dual-target antiviral agents for influenza that targets both PAC (KD = 8.9 μM) and NP (KD = 52.5 μM) simultaneously. Influenza virus-IN-10 exhibits an EC50 values of 1.64 μM) against influenza A virus (H1N1, A/WSN/33) and broad-spectrum activity against other influenza strains, including influenza B virus and multiple subtypes of influenza A .
Strictinin is an orally active phenolic compound. Strictinin reduces xanthine oxidase activity, uric acid production, and the activation of ERK1/2, JNK, NF-κB, and NLRP3 inflammasome components in hepatocytes treated with Xanthine (HY-W017389). Strictinin decreases elevated serum uric acid levels and enhanced xanthine oxidase activity in mice treated with potassium oxonate. Strictinin acts as a ROR1 inhibitor and exhibits anticancer activity against highly aggressive non-androgen-dependent prostate cancer. Strictinin induces cancer cell apoptosis (apoptosis), arrests cell cycle, and inhibits cancer cell migration, invasion, and epithelial-mesenchymal transition. Strictinin modulates gut microbiota, inhibits bacterial growth and biofilm formation, accelerates small intestinal transit, and blocks viral entry and replication. Strictinin can be used in research related to hyperuricemia, androgen receptor-negative non-androgen-dependent prostate cancer, triple-negative breast cancer, bacterial infections, constipation, coronavirus infections, dental caries, and infections caused by influenza A, influenza B, and human parainfluenza virus type 1 .
Noformicin has inhibitory effect on mumps virus and Newcastle disease virus in chicken embryo. Noformicin also extended the survival of mice infected with swine, influenza A (PR8) and influenza B (Lee) viruses .
Ganoderic acid TR is a broad-spectrum inhibitor of influenza neuraminidase enzymes (NAs). Ganoderic acid TR has IC50 values of 10.9 and 4.6 μM for H5N1 and H1N1 NAs, respectively. Ganoderic acid TR is limited by cytotoxicity and shows only weak activity against Oseltamivir (HY-13317)-resistant H1N1 viruses and influenza B viruses .
HA/Hemagglutinin Protein, Influenza B (EPI1868375, HEK293, His) is the recombinant virus-derived HA/Hemagglutinin protein, expressed by HEK293, with C-10*His tag.
NA/Neuraminidase Protein, Influenza B (EPI1868374, sf9, His) is the recombinant virus-derived NA/Neuraminidase protein, expressed by Sf9 insect cells, with C-His tag.
The hemagglutinin (HA) protein attaches viral particles to host cells by binding to sialic acid-containing receptors and induces viral particle internalization through clathrin-dependent endocytosis. HA also promotes an alternative clathrin- and caveolin-independent pathway for some virions. HA/Hemagglutinin Protein, Influenza B (ACN29380, sf9) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by Sf9 insect cells , with tag free.
The hemagglutinin (HA) protein attaches viral particles to host cells by binding to sialic acid-containing receptors and induces viral particle internalization through clathrin-dependent endocytosis. HA also promotes an alternative clathrin- and caveolin-independent pathway for some virions. HA/Hemagglutinin Protein, Influenza B (AAA43701, HEK293, His) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by HEK293 , with C-His labeled tag.
HA/Hemagglutinin proteins are Class I fusion proteins with multiple functions as attachment factors and membrane fusion proteins. HA/Hemagglutinin proteins can bind to cell surface receptors containing sialic acid, promote the attachment of virus particles to host cells, and play an important role in viral host range limitation and virulence. HA/Hemagglutinin Protein, Influenza B (EPI529345, sf9) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by Sf9 insect cells , with tag free.
The Angiopoietin-1 Protein is a secreted glycoprotein that is a key ligand in the vascular tyrosine kinase signaling pathway.ANGPT1 stimulates angiogenesis by activating PTK2/FAK and downstream kinase MAPK1/ERK2 and MAPK3/ERK1 signaling pathways.ANGPT1 affects the proliferation, migration and differentiation of skeletal muscle cells.HA/Hemagglutinin Protein, Influenza B (AGB07680, sf9) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by Sf9 insect cells , with tag free.
HA/Hemagglutinin proteins are Class I fusion proteins with multiple functions as attachment factors and membrane fusion proteins. HA/Hemagglutinin proteins can bind to cell surface receptors containing sialic acid, promote the attachment of virus particles to host cells, and play an important role in viral host range limitation and virulence. HA/Hemagglutinin Protein, Influenza B (EPI529345, sf9, His) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by Sf9 insect cells , with C-His labeled tag.
The Angiopoietin-1 Protein is a secreted glycoprotein that is a key ligand in the vascular tyrosine kinase signaling pathway. ANGPT1 stimulates angiogenesis by activating PTK2/FAK and downstream kinase MAPK1/ERK2 and MAPK3/ERK1 signaling pathways. ANGPT1 affects the proliferation, migration and differentiation of skeletal muscle cells. HA/Hemagglutinin Protein, Influenza B (AXB73995, HEK293, His) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by HEK293 , with C-His labeled tag.
Influenza virus nucleoprotein (NP) is a structural protein that coats viral negative-strand RNA. NP proteins protect viral RNA from degradation by cellular enzymes during the viral life cycle, fit the helical structure of RNP, regulate transcription and replication of viral RNA templates in a histone-like manner, and induce immunosuppression during infection. Nucleoprotein/NP Protein, Influenza B (EPI1649065, sf9, His) is the recombinant Virus-derived Nucleoprotein/NP protein, expressed by Sf9 insect cells , with C-His labeled tag.
NA/Neuraminidase Protein is a receptor-destroying enzyme that cleaves terminal sialic acids from cellular receptors, potentially facilitating viral invasion of the upper airways by targeting sialic acid moieties on airway epithelial cell mucin. NA plays a pivotal role in viral propagation by catalyzing the removal of terminal sialic acid residues from both viral and cellular glycoconjugates. Moreover, the sialidase activity in late endosome/lysosome traffic appears to enhance virus replication. NA/Neuraminidase Protein, Influenza B (AAA43749, HEK293, His) is the recombinant Virus-derived NA/Neuraminidase protein, expressed by HEK293 , with N-His labeled tag.
NA/Neuraminidase Protein, Influenza B (4CPL_A, HEK293) is the recombinant virus-derived NA/Neuraminidase, expressed by HEK293 , with tag Free labeled tag. ,
The Angiopoietin-1 Protein is a secreted glycoprotein that is a key ligand in the vascular tyrosine kinase signaling pathway. ANGPT1 stimulates angiogenesis by activating PTK2/FAK and downstream kinase MAPK1/ERK2 and MAPK3/ERK1 signaling pathways. ANGPT1 affects the proliferation, migration and differentiation of skeletal muscle cells. HA/Hemagglutinin Protein, Influenza B (EPI1394970, HEK293, His) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by HEK293 , with C-His labeled tag.
The Angiopoietin-1 Protein is a secreted glycoprotein that is a key ligand in the vascular tyrosine kinase signaling pathway. ANGPT1 stimulates angiogenesis by activating PTK2/FAK and downstream kinase MAPK1/ERK2 and MAPK3/ERK1 signaling pathways. ANGPT1 affects the proliferation, migration and differentiation of skeletal muscle cells. HA/Hemagglutinin Protein, Influenza B (AGX21754, HEK293, His) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by HEK293 , with C-His labeled tag.
The Angiopoietin-1 Protein is a secreted glycoprotein that is a key ligand in the vascular tyrosine kinase signaling pathway. ANGPT1 stimulates angiogenesis by activating PTK2/FAK and downstream kinase MAPK1/ERK2 and MAPK3/ERK1 signaling pathways. ANGPT1 affects the proliferation, migration and differentiation of skeletal muscle cells. HA/Hemagglutinin Protein, Influenza B (AGB07680, sf9, His) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by Sf9 insect cells , with C-His labeled tag.
The hemagglutinin (HA) protein attaches viral particles to host cells by binding to sialic acid-containing receptors and induces viral particle internalization through clathrin-dependent endocytosis. HA also promotes an alternative clathrin- and caveolin-independent pathway for some virions. HA/Hemagglutinin Protein, Influenza B (AFT64423, sf9, His) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by Sf9 insect cells , with C-His labeled tag.
The hemagglutinin (HA) protein attaches viral particles to host cells by binding to sialic acid-containing receptors and induces viral particle internalization through clathrin-dependent endocytosis. HA also promotes an alternative clathrin- and caveolin-independent pathway for some virions. HA/Hemagglutinin Protein, Influenza B (ACA33493, HEK293, Fc) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by HEK293 , with N-mFc labeled tag.
The hemagglutinin (HA) protein attaches viral particles to host cells by binding to sialic acid-containing receptors and induces viral particle internalization through clathrin-dependent endocytosis. HA also promotes an alternative clathrin- and caveolin-independent pathway for some virions. HA/Hemagglutinin Protein, Influenza B (ABL77299, HEK293, His) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by HEK293 , with C-His labeled tag.
The hemagglutinin (HA) protein attaches viral particles to host cells by binding to sialic acid-containing receptors and induces viral particle internalization through clathrin-dependent endocytosis. HA also promotes an alternative clathrin- and caveolin-independent pathway for some virions. HA/Hemagglutinin Protein, Influenza B (ABL77244, sf9, His) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by Sf9 insect cells , with C-His labeled tag.
Influenza virus nucleoprotein (NP) is a structural protein that coats viral negative-strand RNA. NP proteins protect viral RNA from degradation by cellular enzymes during the viral life cycle, fit the helical structure of RNP, regulate transcription and replication of viral RNA templates in a histone-like manner, and induce immunosuppression during infection. Nucleoprotein/NP Protein, Influenza B (EPI1368865, sf9, His) is the recombinant Virus-derived Nucleoprotein/NP protein, expressed by Sf9 insect cells , with C-His labeled tag.
Influenza virus nucleoprotein (NP) is a structural protein that coats viral negative-strand RNA.NP proteins protect viral RNA from degradation by cellular enzymes during the viral life cycle, fit the helical structure of RNP, regulate transcription and replication of viral RNA templates in a histone-like manner, and induce immunosuppression during infection.Nucleoprotein/NP Protein, Influenza B (ACF54251, sf9, His) is the recombinant Virus-derived Nucleoprotein/NP protein, expressed by Sf9 insect cells , with C-His labeled tag.
NA/Neuraminidase Protein is a receptor-destroying enzyme that cleaves terminal sialic acids from cellular receptors, potentially facilitating viral invasion of the upper airways by targeting sialic acid moieties on airway epithelial cell mucin. NA plays a pivotal role in viral propagation by catalyzing the removal of terminal sialic acid residues from both viral and cellular glycoconjugates. Moreover, the sialidase activity in late endosome/lysosome traffic appears to enhance virus replication. NA/Neuraminidase Protein, Influenza B (EPI529344, sf9, His) is the recombinant Virus-derived NA/Neuraminidase protein, expressed by Sf9 insect cells , with N-His labeled tag.
The Angiopoietin-1 Protein is a secreted glycoprotein that is a key ligand in the vascular tyrosine kinase signaling pathway. ANGPT1 stimulates angiogenesis by activating PTK2/FAK and downstream kinase MAPK1/ERK2 and MAPK3/ERK1 signaling pathways. ANGPT1 affects the proliferation, migration and differentiation of skeletal muscle cells. HA/Hemagglutinin Protein, Influenza B (AGI64446, HEK293, His) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by HEK293 , with C-His labeled tag.
The hemagglutinin (HA) protein attaches viral particles to host cells by binding to sialic acid-containing receptors and induces viral particle internalization through clathrin-dependent endocytosis. HA also promotes an alternative clathrin- and caveolin-independent pathway for some virions. HA/Hemagglutinin Protein, Influenza B (ACN29380, sf9, His) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by Sf9 insect cells , with C-His labeled tag.
The hemagglutinin (HA) protein attaches viral particles to host cells by binding to sialic acid-containing receptors and induces viral particle internalization through clathrin-dependent endocytosis. HA also promotes an alternative clathrin- and caveolin-independent pathway for some virions. HA/Hemagglutinin Protein, Influenza B (ABL77244, HEK293, His) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by HEK293 , with C-His labeled tag.
The hemagglutinin (HA) protein attaches viral particles to host cells by binding to sialic acid-containing receptors and induces viral particle internalization through clathrin-dependent endocytosis. HA also promotes an alternative clathrin- and caveolin-independent pathway for some virions. HA/Hemagglutinin Protein, Influenza B (AFP83206, HEK293, His) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by HEK293 , with C-His labeled tag.
The hemagglutinin (HA) protein attaches viral particles to host cells by binding to sialic acid-containing receptors and induces viral particle internalization through clathrin-dependent endocytosis. HA also promotes an alternative clathrin- and caveolin-independent pathway for some virions. HA/Hemagglutinin Protein, Influenza B (ABF21279, HEK293, His) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by HEK293 , with C-His labeled tag.
HA/Hemagglutinin proteins are Class I fusion proteins with multiple functions as attachment factors and membrane fusion proteins. HA/Hemagglutinin proteins can bind to cell surface receptors containing sialic acid, promote the attachment of virus particles to host cells, and play an important role in viral host range limitation and virulence. HA1/Hemagglutinin Protein, Influenza B (EPI529345, HEK293, His) is the recombinant Virus-derived HA1/Hemagglutinin protein, expressed by HEK293 , with C-His labeled tag.
The hemagglutinin HA1 protein is essential for attachment of virions to host cells by binding to sialic acid-containing receptors, inducing virion internalization via clathrin-dependent or clathrin- and caveolin-independent pathways. As a class I viral fusion protein, HA1 determines host range restriction and virulence, mediating fusion between the virion membrane and the endosomal membrane. HA1/Hemagglutinin Protein, Influenza B (EPI483156, HEK293, His) is the recombinant Virus-derived HA1/Hemagglutinin protein, expressed by HEK293 , with C-His labeled tag.
The hemagglutinin HA1 protein is essential for attachment of virions to host cells by binding to sialic acid-containing receptors, inducing virion internalization via clathrin-dependent or clathrin- and caveolin-independent pathways. As a class I viral fusion protein, HA1 determines host range restriction and virulence, mediating fusion between the virion membrane and the endosomal membrane. HA1/Hemagglutinin Protein, Influenza B (EPI354025, HEK293, His) is the recombinant Virus-derived HA1/Hemagglutinin protein, expressed by HEK293 , with C-His labeled tag.
The hemagglutinin HA1 protein is essential for attachment of virions to host cells by binding to sialic acid-containing receptors, inducing virion internalization via clathrin-dependent or clathrin- and caveolin-independent pathways. As a class I viral fusion protein, HA1 determines host range restriction and virulence, mediating fusion between the virion membrane and the endosomal membrane. HA1/Hemagglutinin Protein, Influenza B (EPI346478, HEK293, His) is the recombinant Virus-derived HA1/Hemagglutinin protein, expressed by HEK293 , with C-His labeled tag.
The hemagglutinin (HA) protein attaches viral particles to host cells by binding to sialic acid-containing receptors and induces viral particle internalization through clathrin-dependent endocytosis.HA also promotes an alternative clathrin- and caveolin-independent pathway for some virions.HA1/Hemagglutinin Protein, Influenza B (AFT64423, HEK293, His) is the recombinant Virus-derived HA1/Hemagglutinin protein, expressed by HEK293 , with C-His labeled tag.
The hemagglutinin HA1 protein is essential for attachment of virions to host cells by binding to sialic acid-containing receptors, inducing virion internalization via clathrin-dependent or clathrin- and caveolin-independent pathways.As a class I viral fusion protein, HA1 determines host range restriction and virulence, mediating fusion between the virion membrane and the endosomal membrane.HA1/Hemagglutinin Protein, Influenza B (ACF54213, HEK293, His) is the recombinant Virus-derived HA1/Hemagglutinin protein, expressed by HEK293 , with C-His labeled tag.
The hemagglutinin HA1 protein is essential for attachment of virions to host cells by binding to sialic acid-containing receptors, inducing virion internalization via clathrin-dependent or clathrin- and caveolin-independent pathways.As a class I viral fusion protein, HA1 determines host range restriction and virulence, mediating fusion between the virion membrane and the endosomal membrane.HA1/Hemagglutinin Protein, Influenza B (ABL77255, HEK293, His) is the recombinant Virus-derived HA1/Hemagglutinin protein, expressed by HEK293 , with C-His labeled tag.
The hemagglutinin HA1 protein is essential for attachment of virions to host cells by binding to sialic acid-containing receptors, inducing virion internalization via clathrin-dependent or clathrin- and caveolin-independent pathways.As a class I viral fusion protein, HA1 determines host range restriction and virulence, mediating fusion between the virion membrane and the endosomal membrane.HA1/Hemagglutinin Protein, Influenza B (ABL77101, HEK293, His) is the recombinant Virus-derived HA1/Hemagglutinin protein, expressed by HEK293 , with C-His labeled tag.
Hemagglutinin (HA) is a class I viral fusion protein which is responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. HA binds to sialic acid-containing receptors on the cell surface to bring about the attachment of the virus particle to the cell. The attachment of HA induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. HA plays a major role in the determination of host range restriction and virulence. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide and forming fusion pore. Several HA trimers are required to form a competent fusion pore. HA/Hemagglutinin Protein, Influenza B (ACO05957, 556a.a, HEK293, His) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by HEK293 , with C-His labeled tag.
The hemagglutinin (HA) protein attaches viral particles to host cells by binding to sialic acid-containing receptors and induces viral particle internalization through clathrin-dependent endocytosis. HA also promotes an alternative clathrin- and caveolin-independent pathway for some virions. HA/Hemagglutinin Protein, Influenza B (ACA33493, 555a.a, HEK293, His) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by HEK293 , with C-His labeled tag.
The hemagglutinin HA1 protein is essential for attachment of virions to host cells by binding to sialic acid-containing receptors, inducing virion internalization via clathrin-dependent or clathrin- and caveolin-independent pathways.As a class I viral fusion protein, HA1 determines host range restriction and virulence, mediating fusion between the virion membrane and the endosomal membrane.HA1/Hemagglutinin Protein, Influenza B (ABF21280, HEK293, His) is the recombinant Virus-derived HA1/Hemagglutinin protein, expressed by HEK293 , with C-His labeled tag.
The hemagglutinin (HA) protein attaches viral particles to host cells by binding to sialic acid-containing receptors and induces viral particle internalization through clathrin-dependent endocytosis. HA also promotes an alternative clathrin- and caveolin-independent pathway for some virions. HA/Hemagglutinin Protein, Influenza B (A4D5Q0, sf9, His) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by Sf9 insect cells , with C-His labeled tag.
Hemagglutinin (HA) is a class I viral fusion protein which is responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. HA binds to sialic acid-containing receptors on the cell surface to bring about the attachment of the virus particle to the cell. The attachment of HA induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. HA plays a major role in the determination of host range restriction and virulence. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide and forming fusion pore. Several HA trimers are required to form a competent fusion pore. HA/Hemagglutinin Protein, Influenza B (ACO05957, 362a.a, HEK293, His) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by HEK293 , with C-His labeled tag.
The hemagglutinin (HA) protein attaches viral particles to host cells by binding to sialic acid-containing receptors and induces viral particle internalization through clathrin-dependent endocytosis. HA also promotes an alternative clathrin- and caveolin-independent pathway for some virions. HA/Hemagglutinin Protein, Influenza B (ACN29380, 556a.a, HEK293, His) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by HEK293 , with C-His labeled tag.
The hemagglutinin (HA) protein attaches viral particles to host cells by binding to sialic acid-containing receptors and induces viral particle internalization through clathrin-dependent endocytosis. HA also promotes an alternative clathrin- and caveolin-independent pathway for some virions. HA/Hemagglutinin Protein, Influenza B (ACA33493, 361a.a, HEK293, His) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by HEK293 , with C-His labeled tag.
Hemagglutinin (HA) is a class I viral fusion protein which is responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. HA binds to sialic acid-containing receptors on the cell surface to bring about the attachment of the virus particle to the cell. The attachment of HA induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. HA plays a major role in the determination of host range restriction and virulence. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide and forming fusion pore. Several HA trimers are required to form a competent fusion pore. HA/Hemagglutinin Protein, Influenza B (sf9, His) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by Sf9 insect cells , with C-His labeled tag.
The hemagglutinin (HA) protein attaches viral particles to host cells by binding to sialic acid-containing receptors and induces viral particle internalization through clathrin-dependent endocytosis. HA also promotes an alternative clathrin- and caveolin-independent pathway for some virions. HA/Hemagglutinin Protein, Influenza B (ACN29383, 362a.a, HEK293, His) is the recombinant Virus-derived HA/Hemagglutinin protein, expressed by HEK293 , with C-His labeled tag.
Nucleoprotein (NP) protects viral RNA and serves as a replication template. Nucleoprotein/NP Protein, Influenza B virus (His-SUMO) is the recombinant Virus-derived Nucleoprotein/NP protein, expressed by E. coli , with N-SUMO, N-6*His labeled tag.
Influenza B virus Nucleoprotein Antibody (YA4920) is a Mouse-derived and non-conjugated monoclonal antibody, targeting to Influenza B virus Nucleoprotein.
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Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
MedchemExpress Validation 03
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
MedchemExpress Validation 04
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
MedchemExpress Validation
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
MedchemExpress Validation
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
MedchemExpress Validation
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
MedchemExpress Validation
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
MedchemExpress Validation
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
MedchemExpress Validation
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
MedchemExpress Validation
Western blot analysis of extracts from THP-1(lane 2(20μg), Jurkat (lane 3(20μg) and NIH3T3(lane 4(20μg) using FOXO1A (HY-P80132) Rabbit mAb. Proteins were transferred
to a PVDF membrane and blocked with 5% non-fat milk in TBST for 2 hour at room temperature. The primary antibody (1/1000) and Loading control antibody (Beta Actin, HY-P80438, 1/10000) was
used in 5% non-fat milk in TBST at 4°C overnight. Goat Anti-Mouse/Rabbit IgG-HRP Secondary Antibody (1/10000) was used for 1 hour at room temperature.
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