HpARI (CCP1/2) (rec.) (His) MultiPack Reference: AG-40B-0201 HpARI is a protein secreted by the mouse parasite Heligmosomoides polygyrus. The mature protein HpARI, containing three predicted Complement Control Protein (CCP)-like modules (also known as Short Consensus Repeats (SCRs) or sushi-domains), suppresses type 2 (allergic) immune responses through interference in the interleukin-33 (IL-33) pathway. During cell damage, HpARI gains access to the nucleus of necrotic cells, where it binds directly to IL-33 and nuclear DNA, preventing secretion and binding of IL-33 to its receptor. A non-natural truncation consisting of the first 2 domains of HpARI (CCP1/2) retains IL-33 and DNA binding capacity. HpARI (CCP1/2) is able to stabilize IL-33, increasing its half-life and amplifying its effects. HpARI (CCP1/2) increases IL-33 activity by protecting it from oxidation and proteolytic degradation. HpARI (CCP1/2) (rec.) (His) is a new type of reagent to study IL-33-mediated pathology in vivo.
CD40L (mouse) (multimeric) (rec.) (Biotin) Reference: AG-40B-0020B The costimulatory molecule CD40, a member of the tumor necrosis factor (TNF) receptor superfamily, critically regulates B cell and T cell function in adaptive immunity and inflammation by interacting with CD40L (CD154). CD40L mediates a range of activities on B cells, including induction of activation-associated surface antigen, entry into cell cycle, isotype switching, immunoglobulin secretion and memory generation. CD40-CD40L interaction also plays important roles in monocyte activation and DC maturation. MultimericCD40L™ is a high activity construct in which two trimeric CD40 ligands are artificially linked via the collagen domain of ACRP30. This construct very effectively simulates the natural membrane-assisted aggregation of CD40L in vivo. It provides a simple and equally potent alternative to CD40L+enhancer combinations. MultimericCD40L™ has shown to suppress alum-induced IL-1beta release and caspase-1 activation in a dose-, CD40- and time dependent manner, without affecting BMDM (bone marrow-derived macrophages) viability. It also effectively suppressed the inflammasome function triggered by NLRP3 activators. The secretion of caspase-1 independent inflammatory mediators has been shown to be unaltered or even enhanced. MultimericCD40L™ enhances B cell proliferation.
SARS-CoV-2 Spike Protein S1 (RBD):Fc (human) (rec.) (B.1.1.7 Variant, Alpha) Reference: AG-40B-0202 SARS-CoV-2 shares 79.5% sequence identity with SARS-CoV and is 96.2% identical at the genome level to the bat coronavirus BatCoV RaTG133, suggesting it had originated in bats. The coronaviral genome encodes four major structural proteins: the Spike (S) protein, Nucleocapsid (N) protein, Membrane/Matrix (M) protein and the Envelope (E) protein. The SARS Envelope (E) protein contains a short palindromic transmembrane helical hairpin that seems to deform lipid bilayers, which may explain its role in viral budding and virion envelope morphogenesis. The SARS Membrane/Matrix (M) protein is one of the major structural viral proteins. It is an integral membrane protein involved in the budding of the viral particles and interacts with SARS Spike (S) protein and the Nucleocapsid (N) protein. The N protein contains two domains, both of them bind the virus RNA genome via different mechanisms. The CoV Spike (S) protein assembles as trimer and plays the most important role in viral attachment, fusion and entry. It is composed of a short intracellular tail, a transmembrane anchor and a large ectodomain that consists of a receptor binding S1 subunit (RBD domain) and a membrane-fusing S2 subunit. The S1 subunit contains a receptor binding domain (RBD), which binds to the cell surface receptor angiotensin-converting enzyme 2 (ACE2) present at the surface of epithelial cells. Recently, a more transmissible variant of SARS-CoV-2, called B.1.1.7 (Alpha), was detected in the south of England. This variant carries a mutation in the RBD at the position 501 (N501Y).
SARS-CoV-2 Spike Protein S1 (RBD):Fc (human) (rec.) (B.1.351 Variant, Beta) Reference: AG-40B-0203 SARS-CoV-2 shares 79.5% sequence identity with SARS-CoV and is 96.2% identical at the genome level to the bat coronavirus BatCoV RaTG133, suggesting it had originated in bats. The coronaviral genome encodes four major structural proteins: the Spike (S) protein, Nucleocapsid (N) protein, Membrane/Matrix (M) protein and the Envelope (E) protein. The SARS Envelope (E) protein contains a short palindromic transmembrane helical hairpin that seems to deform lipid bilayers, which may explain its role in viral budding and virion envelope morphogenesis. The SARS Membrane/Matrix (M) protein is one of the major structural viral proteins. It is an integral membrane protein involved in the budding of the viral particles and interacts with SARS Spike (S) protein and the Nucleocapsid (N) protein. The N protein contains two domains, both of them bind the virus RNA genome via different mechanisms. The CoV Spike (S) protein assembles as trimer and plays the most important role in viral attachment, fusion and entry. It is composed of a short intracellular tail, a transmembrane anchor and a large ectodomain that consists of a receptor binding S1 subunit (RBD domain) and a membrane-fusing S2 subunit. The S1 subunit contains a receptor binding domain (RBD), which binds to the cell surface receptor angiotensin-converting enzyme 2 (ACE2) present at the surface of epithelial cells. Recently, a new variant of SARS-CoV-2, called B.1.351 (Beta), was detected in South Africa. This variant carries three mutations in the RBD at the positions 417, 484 and 501 (K417N, E484K, N501Y) and is associated with a higher viral load, which may suggest potential for increased transmissibility.
SARS-CoV-2 Spike Protein S1 (RBD):Fc (human) (rec.) (P.1 Variant, Gamma) Reference: AG-40B-0204 SARS-CoV-2 shares 79.5% sequence identity with SARS-CoV and is 96.2% identical at the genome level to the bat coronavirus BatCoV RaTG133, suggesting it had originated in bats. The coronaviral genome encodes four major structural proteins: the Spike (S) protein, Nucleocapsid (N) protein, Membrane/Matrix (M) protein and the Envelope (E) protein. The SARS Envelope (E) protein contains a short palindromic transmembrane helical hairpin that seems to deform lipid bilayers, which may explain its role in viral budding and virion envelope morphogenesis. The SARS Membrane/Matrix (M) protein is one of the major structural viral proteins. It is an integral membrane protein involved in the budding of the viral particles and interacts with SARS Spike (S) protein and the Nucleocapsid (N) protein. The N protein contains two domains, both of them bind the virus RNA genome via different mechanisms. The CoV Spike (S) protein assembles as trimer and plays the most important role in viral attachment, fusion and entry. It is composed of a short intracellular tail, a transmembrane anchor and a large ectodomain that consists of a receptor binding S1 subunit (RBD domain) and a membrane-fusing S2 subunit. The S1 subunit contains a receptor binding domain (RBD), which binds to the cell surface receptor angiotensin-converting enzyme 2 (ACE2) present at the surface of epithelial cells. Recently, a new variant of SARS-CoV-2, called P.1 (Gamma) was detected in Brazil. This variant carries three mutations in the RBD at the positions 417, 484 and 501 (K417T, E484K, N501Y). The P.1 or Brazilian variant is a form of the SARS-CoV-2 coronavirus that appears to have evolved in Brazil and might have contributed to a surge in cases in the northern city of Manaus.
Streptavidin Reference: AG-35B-0014 Streptavidin is a non-glycosylated protein isolated from Streptomyces avidinii. It forms a homotetramer and strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin).
Streptavidin (HRP) Reference: AG-35B-0014E Streptavidin is a non-glycosylated protein isolated from Streptomyces avidinii. It forms a homotetramer and strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin). Streptavidin (HRP) is useful as a second step reagent for indirect enzymatic labeling, in conjunction with biotinylated primary antibodies. It is often used in ELISA, IHC or Western blotting applications together with relevant substrate systems.
Streptavidin (R-PE) Reference: AG-35B-0014R Streptavidin is a non-glycosylated protein isolated from Streptomyces avidinii. It forms a homotetramer and strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin). Streptavidin (R-PE) is typically used for flow cytometry, microarrays, ELISA and other applications that require either high sensitivity or simultaneous multicolor detection. Phycoerythrin is a member of a family of proteins called phycobiliproteins, which are derived from cyanobacteria and eukaryotic algae and exhibit extremely bright fluorescence and high quantum yields.
SARS-CoV-2 Spike Protein S1 (RBD) (rec.) (His) (B.1.1.7 Variant, Alpha) Reference: AG-40B-0205 SARS-CoV-2 shares 79.5% sequence identity with SARS-CoV and is 96.2% identical at the genome level to the bat coronavirus BatCoV RaTG133, suggesting it had originated in bats. The coronaviral genome encodes four major structural proteins: the Spike (S) protein, Nucleocapsid (N) protein, Membrane/Matrix (M) protein and the Envelope (E) protein. The SARS Envelope (E) protein contains a short palindromic transmembrane helical hairpin that seems to deform lipid bilayers, which may explain its role in viral budding and virion envelope morphogenesis. The SARS Membrane/Matrix (M) protein is one of the major structural viral proteins. It is an integral membrane protein involved in the budding of the viral particles and interacts with SARS Spike (S) protein and the Nucleocapsid (N) protein. The N protein contains two domains, both of them bind the virus RNA genome via different mechanisms. The CoV Spike (S) protein assembles as trimer and plays the most important role in viral attachment, fusion and entry. It is composed of a short intracellular tail, a transmembrane anchor and a large ectodomain that consists of a receptor binding S1 subunit (RBD domain) and a membrane-fusing S2 subunit. The S1 subunit contains a receptor binding domain (RBD), which binds to the cell surface receptor angiotensin-converting enzyme 2 (ACE2) present at the surface of epithelial cells. Recently, a more transmissible variant of SARS-CoV-2, called B.1.1.7 (Alpha), was detected in the south of England. This variant carries a mutation in the RBD at the position 501 (N501Y). The SARS-CoV-2 Spike Protein S1 (RBD) (rec.) (His) (B.1.1.7 Variant, Alpha) can be used as antigen in Serological ELISA Kits to detect anti-SARS-CoV-2 Spike (RBD) antibodies in serum or plasma.
SARS-CoV-2 Spike Protein S1 (RBD) (rec.) (His) (B.1.351 Variant, Beta) Reference: AG-40B-0206 SARS-CoV-2 shares 79.5% sequence identity with SARS-CoV and is 96.2% identical at the genome level to the bat coronavirus BatCoV RaTG133, suggesting it had originated in bats. The coronaviral genome encodes four major structural proteins: the Spike (S) protein, Nucleocapsid (N) protein, Membrane/Matrix (M) protein and the Envelope (E) protein. The SARS Envelope (E) protein contains a short palindromic transmembrane helical hairpin that seems to deform lipid bilayers, which may explain its role in viral budding and virion envelope morphogenesis. The SARS Membrane/Matrix (M) protein is one of the major structural viral proteins. It is an integral membrane protein involved in the budding of the viral particles and interacts with SARS Spike (S) protein and the Nucleocapsid (N) protein. The N protein contains two domains, both of them bind the virus RNA genome via different mechanisms. The CoV Spike (S) protein assembles as trimer and plays the most important role in viral attachment, fusion and entry. It is composed of a short intracellular tail, a transmembrane anchor and a large ectodomain that consists of a receptor binding S1 subunit (RBD domain) and a membrane-fusing S2 subunit. The S1 subunit contains a receptor binding domain (RBD), which binds to the cell surface receptor angiotensin-converting enzyme 2 (ACE2) present at the surface of epithelial cells. Recently, a new variant of SARS-CoV-2, called B.1.351 (Beta), was detected in South Africa. This variant carries three mutations in the RBD at the positions 417, 484 and 501 (K417N, E484K, N501Y) and is associated with a higher viral load, which may suggest potential for increased transmissibility. The SARS-CoV-2 Spike Protein S1 (RBD) (rec.) (His) (B.1.351 Variant, Beta) can be used as antigen in Serological ELISA Kits to detect anti-SARS-CoV-2 Spike (RBD) antibodies in serum or plasma.
SARS-CoV-2 Spike Protein S1 (RBD) (rec.) (His) (P.1 Variant, Gamma) Reference: AG-40B-0207 SARS-CoV-2 shares 79.5% sequence identity with SARS-CoV and is 96.2% identical at the genome level to the bat coronavirus BatCoV RaTG133, suggesting it had originated in bats. The coronaviral genome encodes four major structural proteins: the Spike (S) protein, Nucleocapsid (N) protein, Membrane/Matrix (M) protein and the Envelope (E) protein. The SARS Envelope (E) protein contains a short palindromic transmembrane helical hairpin that seems to deform lipid bilayers, which may explain its role in viral budding and virion envelope morphogenesis. The SARS Membrane/Matrix (M) protein is one of the major structural viral proteins. It is an integral membrane protein involved in the budding of the viral particles and interacts with SARS Spike (S) protein and the Nucleocapsid (N) protein. The N protein contains two domains, both of them bind the virus RNA genome via different mechanisms. The CoV Spike (S) protein assembles as trimer and plays the most important role in viral attachment, fusion and entry. It is composed of a short intracellular tail, a transmembrane anchor and a large ectodomain that consists of a receptor binding S1 subunit (RBD domain) and a membrane-fusing S2 subunit. The S1 subunit contains a receptor binding domain (RBD), which binds to the cell surface receptor angiotensin-converting enzyme 2 (ACE2) present at the surface of epithelial cells. Recently, a new variant of SARS-CoV-2, called P.1 (Gamma) was detected in Brazil. This variant carries three mutations in the RBD at the positions 417, 484 and 501 (K417T, E484K, N501Y). The P.1 or Brazilian variant is a form of the SARS-CoV-2 coronavirus that appears to have evolved in Brazil and might have contributed to a surge in cases in the northern city of Manaus. The SARS-CoV-2 Spike Protein S1 (RBD) (rec.) (His) (P.1 Variant, Gamma) can be used as antigen in Serological ELISA Kits to detect anti-SARS-CoV-2 Spike (RBD) antibodies in serum or plasma.
SARS-CoV-2 Spike Protein S1 (RBD) (rec.) (His) (B.1.617 Variant, IND) Reference: AG-40B-0208 SARS-CoV-2 shares 79.5% sequence identity with SARS-CoV and is 96.2% identical at the genome level to the bat coronavirus BatCoV RaTG133, suggesting it had originated in bats. The coronaviral genome encodes four major structural proteins: the Spike (S) protein, Nucleocapsid (N) protein, Membrane/Matrix (M) protein and the Envelope (E) protein. The SARS Envelope (E) protein contains a short palindromic transmembrane helical hairpin that seems to deform lipid bilayers, which may explain its role in viral budding and virion envelope morphogenesis. The SARS Membrane/Matrix (M) protein is one of the major structural viral proteins. It is an integral membrane protein involved in the budding of the viral particles and interacts with SARS Spike (S) protein and the Nucleocapsid (N) protein. The N protein contains two domains, both of them bind the virus RNA genome via different mechanisms. The CoV Spike (S) protein assembles as trimer and plays the most important role in viral attachment, fusion and entry. It is composed of a short intracellular tail, a transmembrane anchor and a large ectodomain that consists of a receptor binding S1 subunit (RBD domain) and a membrane-fusing S2 subunit. The S1 subunit contains a receptor binding domain (RBD), which binds to the cell surface receptor angiotensin-converting enzyme 2 (ACE2) present at the surface of epithelial cells. Recently, a new variant of SARS-CoV-2, called B.1.617 was detected in India. Three sublineages have been found, B.1.617.1 (variant Kappa) and B.1.617.3 containing 4 mutations in the Spike protein with a double mutations in the Receptor Binding Region (L452R, E484Q) and B.1.617.2 (variant Delta) that is different since it contains the mutation T478K instead of E484Q. These variants (especially the B.1.617.1 & B.1.617.2) of the SARS-CoV-2 coronavirus have evolved as fast-growing variants outspacing other variants. The SARS-CoV-2 Spike Protein S1 (RBD) (rec.) (His) (B.1.617.1 Variant, Kappa) can be used as antigen in Serological ELISA Kits to detect anti-SARS-CoV-2 Spike (RBD) antibodies in serum or plasma.