Category: Proteins & Peptides

Active filters

Reference: GTX88408-PEP

The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 2S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the proteasome B-type family, also known as the T1B family, that is a 2S core beta subunit. Proteolytic processing is required to generate a mature subunit. Expression of this gene is induced by gamma interferon, and this gene product replaces catalytic subunit 2 (proteasome beta 7 subunit) in the immunoproteasome. [provided by RefSeq, Jul 28]

Reference: GFM59-100

Interleukin-17A (IL-17A), also known as CTLA-8, is a member of the IL-17 family of proteins. IL-17A is a proinflammatory cytokine that is secreted by activated CD4+ and CD8+ T lymphocytes. IL-17A acts through its receptor, IL-17R, to promote increased cytokine and chemokine secretion. In turn, the cytokines and chemokines mediate the immunoregulatory function of IL-17A by promoting the proliferation, maturation, and chemoattraction of neutrophils to inflammatory sites. Elevated levels of IL-17A are associated with rheumatoid arthritis, airway inflammation, allograft rejection, inflammatory bowel disease, psoriasis, cancer, and multiple sclerosis. Human, mouse, and rat IL-17A show activity on mouse cells.

Reference: GTX88409-PEP

G protein-coupled receptors (GPCRs, or GPRs), such as GPR81, contain 7 transmembrane domains and transduce extracellular signals through heterotrimeric G proteins.[supplied by OMIM, Feb 25]

Reference: GFM59-1000

Interleukin-17A (IL-17A), also known as CTLA-8, is a member of the IL-17 family of proteins. IL-17A is a proinflammatory cytokine that is secreted by activated CD4+ and CD8+ T lymphocytes. IL-17A acts through its receptor, IL-17R, to promote increased cytokine and chemokine secretion. In turn, the cytokines and chemokines mediate the immunoregulatory function of IL-17A by promoting the proliferation, maturation, and chemoattraction of neutrophils to inflammatory sites. Elevated levels of IL-17A are associated with rheumatoid arthritis, airway inflammation, allograft rejection, inflammatory bowel disease, psoriasis, cancer, and multiple sclerosis. Human, mouse, and rat IL-17A show activity on mouse cells.

Reference: GTX88410-PEP

The proteasome is a multicatalytic proteinase complex with a highly ordered ring-shaped 2S core structure. The core structure is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes a member of the proteasome B-type family, also known as the T1B family, that is a 2S core beta subunit. This gene is located in the class II region of the MHC (major histocompatibility complex). Expression of this gene is induced by gamma interferon and this gene product replaces catalytic subunit 3 (proteasome beta 5 subunit) in the immunoproteasome. Proteolytic processing is required to generate a mature subunit. Two alternative t

Reference: GFM59AF-5

Interleukin-17A (IL-17A), also known as CTLA-8, is a member of the IL-17 family of proteins. IL-17A is a proinflammatory cytokine that is secreted by activated CD4+ and CD8+ T lymphocytes. IL-17A acts through its receptor, IL-17R, to promote increased cytokine and chemokine secretion. In turn, the cytokines and chemokines mediate the immunoregulatory function of IL-17A by promoting the proliferation, maturation, and chemoattraction of neutrophils to inflammatory sites. Elevated levels of IL-17A are associated with rheumatoid arthritis, airway inflammation, allograft rejection, inflammatory bowel disease, psoriasis, cancer, and multiple sclerosis. Human, mouse, and rat IL-17A show activity on mouse cells.

Reference: GFM59AF-25

Interleukin-17A (IL-17A), also known as CTLA-8, is a member of the IL-17 family of proteins. IL-17A is a proinflammatory cytokine that is secreted by activated CD4+ and CD8+ T lymphocytes. IL-17A acts through its receptor, IL-17R, to promote increased cytokine and chemokine secretion. In turn, the cytokines and chemokines mediate the immunoregulatory function of IL-17A by promoting the proliferation, maturation, and chemoattraction of neutrophils to inflammatory sites. Elevated levels of IL-17A are associated with rheumatoid arthritis, airway inflammation, allograft rejection, inflammatory bowel disease, psoriasis, cancer, and multiple sclerosis. Human, mouse, and rat IL-17A show activity on mouse cells.

Reference: GFM59AF-100

Interleukin-17A (IL-17A), also known as CTLA-8, is a member of the IL-17 family of proteins. IL-17A is a proinflammatory cytokine that is secreted by activated CD4+ and CD8+ T lymphocytes. IL-17A acts through its receptor, IL-17R, to promote increased cytokine and chemokine secretion. In turn, the cytokines and chemokines mediate the immunoregulatory function of IL-17A by promoting the proliferation, maturation, and chemoattraction of neutrophils to inflammatory sites. Elevated levels of IL-17A are associated with rheumatoid arthritis, airway inflammation, allograft rejection, inflammatory bowel disease, psoriasis, cancer, and multiple sclerosis. Human, mouse, and rat IL-17A show activity on mouse cells.

Reference: GTX88413-PEP

The product of this gene belongs to the serine/threonine protein kinases family, and to the Ca(2+)/calmodulin-dependent protein kinases subfamily. Calcium signaling is crucial for several aspects of plasticity at glutamatergic synapses. This calcium calmodulin-dependent protein kinase is composed of four different chains: alpha, beta, gamma, and delta. The alpha chain encoded by this gene is required for hippocampal long-term potentiation (LTP) and spatial learning. In addition to its calcium-calmodulin (CaM)-dependent activity, this protein can undergo autophosphorylation, resulting in CaM-independent activity. Two transcript variants encoding distinct isoforms have been identified for this gene. [provided by RefSeq, Nov 28]

Reference: GFM59AF-1000

Interleukin-17A (IL-17A), also known as CTLA-8, is a member of the IL-17 family of proteins. IL-17A is a proinflammatory cytokine that is secreted by activated CD4+ and CD8+ T lymphocytes. IL-17A acts through its receptor, IL-17R, to promote increased cytokine and chemokine secretion. In turn, the cytokines and chemokines mediate the immunoregulatory function of IL-17A by promoting the proliferation, maturation, and chemoattraction of neutrophils to inflammatory sites. Elevated levels of IL-17A are associated with rheumatoid arthritis, airway inflammation, allograft rejection, inflammatory bowel disease, psoriasis, cancer, and multiple sclerosis. Human, mouse, and rat IL-17A show activity on mouse cells.