SARS-CoV-2 Nucleocapsid Protein (rec.) (His) Reference: CHI-B233501 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 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. Sequence analysis of the SARS-CoV-2 S protein genome showed that it was only 75% identical with the SARS-CoV S protein. However, analysis of the receptor binding motif (RBM) in the S protein showed that most of the amino acid residues essential for receptor binding were conserved between SARS-CoV and SARS-CoV-2, suggesting that the 2 CoV strains use the same host receptor for cell entry, the receptor angiotensin-converting enzyme 2 (ACE2). The N protein contains two domains, both of them bind the virus RNA genome via different mechanisms.
SARS-CoV-2 Spike Protein S1 (RBD):Fc (human) (rec.) Reference: AG-40B-0194 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.
Tim-4 (mouse):Fc (human) (rec.) Reference: AG-40B-0180 Tim-4 (T cell immunoglobulin and mucin domain-containing protein 4) is a single-pass type I membrane protein which belongs to the immunoglobulin superfamily and TIM family. Tim-4 contains one Ig-like V-type (immunoglobulin-like) domain. It is expressed on dendritic cells and macrophages. TIM4 is expressed solely on antigen presenting cells (APCs) and is not found on T cells in contrast to TIM1 and TIM3. Tim-4 has a short intracellular domain and lacks an inward signaling motif. Tim-4 plays an important role in the proliferation of T helper type 2 (Th2) cells. Tim-4 binds to phosphatidylserine (PS) on the surface of apoptotic cells in a calcium-dependent manner and mediates phagocytosis of apoptotic cells.
ACE2 (human) (rec.) (Biotin) Reference: AG-40B-0192B Angiotensin-converting enzyme 2 (ACE2) is an ectoenzyme (carboxypeptidase) with an extracellular catalytic domain that predominantly localizes at the plasma membrane and is thereby able to hydrolyze circulating peptides. ACE2 has approximately 42% sequence identity with ACE, and its cytoplasmic and transmembrane domains show 48% homology to the protein collectrin that plays a critical role in the amino acid absorption of the kidney. ACE2 converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator. ACE2 is involved in the regulation of systemic blood pressure and has direct effects on cardiac functions. It is expressed predominantly in endothelial cells of the lung, gut, heart and kidney. ACE2 together with the protease TMPRSS2 acts as a functional receptor for SARS coronavirus as well as for the new highly pathogenic coronavirus, 2019-nCoV/SARS-CoV-2, which is cause for pneumonia COVID-19.
ACE2 (human) (rec.) (His) Reference: CHI-B232008 Angiotensin-converting enzyme 2 (ACE2) is an ectoenzyme (carboxypeptidase) with an extracellular catalytic domain that predominantly localizes at the plasma membrane and is thereby able to hydrolyze circulating peptides. ACE2 has approximately 42% sequence identity with ACE, and its cytoplasmic and transmembrane domains show 48% homology to the protein collectrin that plays a critical role in the amino acid absorption of the kidney. ACE2 converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator. ACE2 is involved in the regulation of systemic blood pressure and has direct effects on cardiac functions. It is expressed predominantly in endothelial cells of the lung, gut, heart and kidney. ACE2 together with the protease TMPRSS2 acts as a functional receptor for SARS coronavirus as well as for the new highly pathogenic coronavirus, 2019-nCoV/SARS-CoV-2, which is cause for pneumonia COVID-19. It has been shown that human recombinant soluble ACE2 can significantly block early stages of SARS-CoV-2 infections.
SARS-CoV-2 Spike Protein S1 (RBD) (rec.) (GST-His) Reference: CHI-B249001 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. Sequence analysis of the SARS-CoV-2 S protein genome showed that it was only 75% identical with the SARS-CoV S protein. However, analysis of the receptor binding motif (RBM) in the S protein showed that most of the amino acid residues essential for receptor binding were conserved between SARS-CoV and SARS-CoV-2, suggesting that the 2 CoV strains use the same host receptor for cell entry, the receptor angiotensin-converting enzyme 2 (ACE2).
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.