Category: Antibodies

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  • Categories: ELISA Antibody Pairs
  • Brand: Abclonal
Reference: RM17744

Interleukin-4, is a cytokine that induces differentiation of naive helper T cells (Th0 cells to Th2 cells). In the presence of IL-4 and IL-13, cytokines that are produced in a Th-2 type response, particularly during allergy and parasitic infections, macrophages become differentially activated, And this cytokine is a ligand for interleukin 4 receptor. The interleukin 4 receptor also binds to IL13, which may contribute to many overlapping functions of this cytokine and IL13. STAT6, a signal transducer and activator of transcription, has been shown to play a central role in mediating the immune regulatory signal of this cytokine. Recently, researcher found that the cytokine IL-4 plays a key role in development of innate CD8+ T cells in the thymus of several gene-deficient mouse strains, including Itk, KLF2, CBP and Id3, without previous exposure to antigen.

Reference: RM17575

Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. Coronavirus N protein is required for coronavirus RNA synthesis, and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is a most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.

Reference: RM17576

Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. Coronavirus N protein is required for coronavirus RNA synthesis, and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is a most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.

Reference: RM17580

The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. The spike is essential for both host specificity and viral infectivity. The spike (S) glycoprotein of coronaviruses is known to be essential in the binding of the virus to the host cell at the advent of the infection process. It''s been reported that SARS-CoV-2 (COVID-19 coronavirus, 2019-nCoV) can infect the human respiratory epithelial cells through interaction with the human ACE2 receptor. S1 mainly contains a receptor binding domain (RBD), which is responsible for recognizing the cell surface receptor. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.

Reference: RM17589

Interleukin-2 (IL-2) is an interleukin, a type of cytokine immune system signaling molecule, which is a leukocytotrophic hormone that is instrumental in the body’s natural response to microbial infection and in discriminating between foreign (non-self) and self. IL-2 mediates its effects by binding to IL-2 receptors, which are expressed by lymphocytes, the cells that are responsible for immunity. Mature human IL-2 shares 56% and 66% aa sequence identity with mouse and rat IL-2, respectively. Human and mouse IL-2 exhibit crossspecies activity. The receptor for IL-2 consists of three subunits that are present on the cell surface in varying preformed complexes. IL-2 is also necessary during T cell development in the thymus for the maturation of a unique subset of T cells that are termed regulatory T cells (T-regs). After exiting from the thymus, T-Regs function to prevent other T cells from recognizing and reacting against “self antigens”, which could result in “autoimmunity”. T-Regs do so by preventing the responding cells from producing IL-2. Thus, IL-2 is required to discriminate between self and non-self, another one of the unique characteristics of the immune system.

Reference: RM17590

Interleukin-2 (IL-2) is an interleukin, a type of cytokine immune system signaling molecule, which is a leukocytotrophic hormone that is instrumental in the body’s natural response to microbial infection and in discriminating between foreign (non-self) and self. IL-2 mediates its effects by binding to IL-2 receptors, which are expressed by lymphocytes, the cells that are responsible for immunity. Mature human IL-2 shares 56% and 66% aa sequence identity with mouse and rat IL-2, respectively. Human and mouse IL-2 exhibit crossspecies activity. The receptor for IL-2 consists of three subunits that are present on the cell surface in varying preformed complexes. IL-2 is also necessary during T cell development in the thymus for the maturation of a unique subset of T cells that are termed regulatory T cells (T-regs). After exiting from the thymus, T-Regs function to prevent other T cells from recognizing and reacting against “self antigens“, which could result in “autoimmunity“. T-Regs do so by preventing the responding cells from producing IL-2. Thus, IL-2 is required to discriminate between self and non-self, another one of the unique characteristics of the immune system.

Reference: RM17599

The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. The spike is essential for both host specificity and viral infectivity. The spike (S) glycoprotein of coronaviruses is known to be essential in the binding of the virus to the host cell at the advent of the infection process. It''''s been reported that SARS-CoV-2 (COVID-19 coronavirus, 2019-nCoV) can infect the human respiratory epithelial cells through interaction with the human ACE2 receptor. S1 mainly contains a receptor binding domain (RBD), which is responsible for recognizing the cell surface receptor. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.

Reference: RM17601

Interleukin 6 (IL-6) is also known as HGF, BSF2,HSF, IFNB2 and IL-6, originally identified as a B cell differentiation factor, is a multifunctional cytokine that regulates immune responses, hematopoiesis, acute phase responses, and inflammatory reactions.It is secreted by T cells, macrophages , monocytes, fibroblasts,endothelial cells,et.al. to stimulate immune response to trauma, especially burns or other tissue damage leading to inflammation. Interleukin 6 has been shown to interact with interleukin-6 receptor and glycoprotein. IL-6 is relevant to many disease processes such as diabetes,atherosclerosis, depression,Alzheimer’s Disease,systemic,lupus erythematosus,prostate cancer and rheumatoid arthritis. Advanced/metastatic cancer patients have higher levels of IL-6 in their blood.Hence there is an interest in developing anti-IL-6 agents as therapy against many of these diseases.

Reference: RM17602

Interleukin 6 (IL-6) is also known as HGF, BSF2,HSF, IFNB2 and IL-6, originally identified as a B cell differentiation factor, is a multifunctional cytokine that regulates immune responses, hematopoiesis, acute phase responses, and inflammatory reactions.It is secreted by T cells, macrophages , monocytes, fibroblasts,endothelial cells,et.al. to stimulate immune response to trauma, especially burns or other tissue damage leading to inflammation. Interleukin 6 has been shown to interact with interleukin-6 receptor and glycoprotein. IL-6 is relevant to many disease processes such as diabetes,atherosclerosis, depression,Alzheimer’s Disease,systemic,lupus erythematosus,prostate cancer and rheumatoid arthritis. Advanced/metastatic cancer patients have higher levels of IL-6 in their blood.Hence there is an interest in developing anti-IL-6 agents as therapy against many of these diseases.

Reference: RM17612

The spike (S) glycoprotein of coronaviruses contains protrusions that will only bind to certain receptors on the host cell. The spike is essential for both host specificity and viral infectivity. The spike (S) glycoprotein of coronaviruses is known to be essential in the binding of the virus to the host cell at the advent of the infection process. It''s been reported that SARS-CoV-2 (COVID-19 coronavirus, 2019-nCoV) can infect the human respiratory epithelial cells through interaction with the human ACE2 receptor. S1 mainly contains a receptor binding domain (RBD), which is responsible for recognizing the cell surface receptor. The main functions for the Spike protein are summarized as: Mediate receptor binding and membrane fusion; Defines the range of the hosts and specificity of the virus; Main component to bind with the neutralizing antibody; Key target for vaccine design; Can be transmitted between different hosts through gene recombination or mutation of the receptor binding domain (RBD), leading to a higher mortality rate.

Reference: RM17614

Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. Coronavirus N protein is required for coronavirus RNA synthesis, and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is a most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.

Reference: RM17615

Coronaviruses are enveloped viruses with a positive-sense RNA genome and with a nucleocapsid of helical symmetry. Coronavirus nucleoproteins localize to the cytoplasm and the nucleolus, a subnuclear structure, in both virus-infected primary cells and in cells transfected with plasmids that express N protein. Coronavirus N protein is required for coronavirus RNA synthesis, and has RNA chaperone activity that may be involved in template switch. Nucleocapsid protein is a most abundant protein of coronavirus. During virion assembly, N protein binds to viral RNA and leads to formation of the helical nucleocapsid. Nucleocapsid protein is a highly immunogenic phosphoprotein also implicated in viral genome replication and in modulating cell signaling pathways. Because of the conservation of N protein sequence and its strong immunogenicity, the N protein of coronavirus is chosen as a diagnostic tool.