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.
SARS-CoV-2 Spike Protein S1 (RBD):Fc (human) (rec.) (B.1.617 Variant, IND) Reference: AG-40B-0209 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.
SARS-CoV-2 Spike Protein S1 (RBD):Fc (human) (rec.) (B.1.617.2 Variant, Delta) Reference: AG-40B-0211 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.
SARS-CoV-2 Spike Protein S1 (RBD):Fc (human) (rec.) (B.1.617.2.1 Variant,... Reference: AG-40B-0212 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. Recently, a new variant derived from Delta (called Delta Plus and containing the mutations K417N, L452R & T478K) was detected in India and in several other countries. While studies are still underway, scientists say Delta Plus does not seem to be more transmissible than Delta.
Fc (human):FNDC4 (rec.) Reference: AG-40B-0213 Irisin is a recently described exercise-induced hormone secreted by skeletal muscle in mice and humans. Irisin activates beige fat cells (beige cells have a gene expression pattern distinct from either white or brown fat and are preferentially sensitive to the polypeptide hormone irisin). Irisin is cleaved from the type I membrane protein FNDC5 and improves systemic metabolism by increasing energy expenditure. FNDC4 is an ortholog of FNDC5 with 50% identity and 86% similarity compared to Irisin. FNDC4 as well as FNDC5 are extremely well conserved between species. The human FNDC4 gene is highly enriched in liver, brain tissue and adipocytes. FNDC4 is a factor with direct therapeutic potential in inflammatory bowel disease and possibly other inflammatory diseases. Recently, a new role of FNDC4 as a hepatokine has been published. Liver primarily controls the circulating levels of FNDC4 showing tight correlation with insulin sensitivity. In addition, a new orphan adhesion G protein-coupled receptor 116 (GPR116) has been identified as a receptor of FNDC4 in white adipose tissue (WAT), thereby establishing an endocrine FNDC4-GPR116 axis in the control of systemic glucose homeostasis. Moreover, the FNDC4-GPR116 axis is impaired in diabetic patients and therapeutic injections of recombinant Fc-FNDC4 into pre-diabetic mice corrected pre-diabetic hyperglycemia.
CD123 [IL-3Ralpha] (human)-muIg Fusion Protein (Biotin) Reference: ANC-545-030 Human CD123 (Interleukin-3 Receptor alpha) is a 70kDa type I transmembrane molecule, and is the low affinity receptor for the cytokine IL-3, which can stimulate proliferation or differentiation. When paired in a heterodimer with CD131 (IL-3Rbeta), it binds IL-3 with much higher affinity. CD123 is found on myeloid precusors, stem cells, a subset of T cells, some B cells, megakaryocytes, basophils, monocytes and epithelial cells. CD123 is present at high levels on many hematologic malignancies, and antibodies and CAR T cells against CD123 have been used successfully to combat acute myeloid leukemia (AML).
CD304 (human)-muIg Fusion Protein Reference: ANC-557-020 Human CD304 (neuropilin, NRP, NP1, BDCA-4) is a 140 kD type I glycoprotein expressed by a variety of tissue types,including Treg, follicular TH, neurons, dendritic cells and endothelial cells. Its ligands include VEGF165 and Semaphorin family members. It is a reliable marker for human BCP-ALL. Soluble CD304 has been used to slow progression of murine AML.