Adiponectin (rat) (rec.) Reference: AG-40A-0004Y ACRP30 was identified as a novel adipocyte-specific synthesized and secreted protein with structural resemblance to complement factor C1q. Like adipsin, ACRP30 secretion is induced ~10-fold during adipocyte differentiation. Plasma levels are reduced in obese humans and low levels are associated with insulin-resistance. Treatment of db/db mice with TZD increased ACRP30 levels.
Vaspin (mouse) (rec.) Reference: AG-40A-0094Y Vaspin (Visceral adipose tissue-derived serpin; Serpin A12), a serine protease inhibitor (serpin), is an insulin-sensitizing adipocytokine that has been isolated from both visceral and subcutaneous white adipose tissue. Vaspin modulates insulin action by specifically inhibiting its target protease KLK7 in white adipose tissues. Based on recent findings, vaspin is suggested to regulate immune responses and inflammation and is correlated with various metabolic parameters. Vaspin may represent a novel biomarker for obesity and impaired insulin sensitivity and might serve as a new therapeutic target of metabolic syndrome.
SARS-CoV-2 Spike Protein S1 (RBD) (rec.) (His) Reference: AG-40B-0195 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. The SARS-CoV-2 Spike Protein S1 (RBD) (rec.) (His) is used as antigen in the Serological ELISA Kit to detect anti-SARS-CoV-2 Spike (RBD) antibodies in serum or plasma (see SARS-CoV-2 (Spike RBD) IgG Serological ELISA Kit; AG-45B-0020).
Acyl-CoA-binding Protein (human) (rec.) (His) Reference: AG-40B-0197 Acyl-coenzyme A (CoA)-binding protein (ACBP) is an ubiquitously expressed 86 aa polypeptide that binds medium- and long-chain acyl-CoA esters with very high affinity. It plays a role as an intracellular carrier of acyl-CoA esters and regulates lipid metabolism in the cytoplasm of most cell types. In addition to its function within the cells as acyl-coenzyme A (CoA)-binding protein, ACBP also functions as secreted protein called Diazepam-Binding Inhibitor (DBI) that can interact with the benzodiazepine-binding site of the gamma-aminobutyric acid (GABA) type A receptor, GABAAR, and modulate its activity. ACBP is secreted upon induction of autophagy (energy deficiency) in different organisms including mouse and human. ACBP levels correlate with human body mass index (BMI). Increasing ACBP levels in mice triggers lipogenesis, food intake and weight gain and neutralization of ACBP increases lipolysis, reduces food intake post-starvation and causes weight loss in mice. Obese patients exhibit elevated plasma levels of ACBP, while a reduction in the ACBP mRNA and ACBP plasma protein levels is observed in these patients after an important weight loss. ACBP might be useful for the prevention or treatment of obesity and metabolic syndrome diseases.
SARS-CoV-2 Spike Protein (D614G) (Stable Trimer) (rec.) (His) Reference: AG-40B-6003 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 original Wuhan strain of the virus has become quickly replaced by its more transmissible variant, mainly determined by a single amino acid point mutation D614G. 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. It has been demonstrated that certain mutations and the inclusion of trimerization motif can stabilize recombinant Spike protein trimers. The recombinant protein SARS-CoV-2 Spike Protein (D614G) (Stable Trimer) (rec.) (His) could be useful for structural biology research, vaccine development, serological diagnostic kit development or neutralizing antibody screening.
SARS-CoV-2 Spike Protein S1 (RBD) (rec.) (His) (Biotin) Reference: AG-40B-0195B 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. The SARS-CoV-2 Spike Protein S1 (RBD) (rec.) (His) is used as antigen in the Serological ELISA Kit to detect anti-SARS-CoV-2 Spike (RBD) antibodies in serum or plasma (see SARS-CoV-2 (Spike RBD) IgG Serological ELISA Kit; AG-45B-0020). This biotinylated version of SARS-CoV-2 Spike Protein S1 (RBD) (rec.) (His) forms a tetramer in the presence of streptavidin and this tetramer can be used to activate B cell memory to SARS-CoV-2 Spike protein.
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).