Search results for heat shock protein

Heat Shock Protein 104 antibody, Genetex, GTX79161

Heat Shock Protein 90 antibody, Covalab, Ref 00026395

Heat Shock Protein 70 (HSP70) Antibody, Abbexa, abx234048

HSP70 Antibody is a Rabbit Polyclonal against HSP70.

Heat Shock Protein 42 (HSP42) Antibody, Abbexa, abx345960

Heat Shock Protein 42 (HSP42) Antibody is a Rabbit Polyclonal antibody for the detection of Saccharomyces cerevisiae (Baker's yeast) HSP42.

Heat Shock Protein 70 (HSP70) Antibody, Abbexa, abx000067

HSP70 Antibody is a Mouse Monoclonal antibody against HSP70. This intronless gene encodes a 70kDa heat shock protein which is a member of the heat shock protein 70 family. In conjuction with other heat shock proteins, this protein stabilizes existing proteins against aggregation and mediates the folding of newly translated proteins in the cytosol and in organelles. It is also involved in the ubiquitin-proteasome pathway through interaction with the AU-rich element RNA-binding protein 1. The gene is located in the major histocompatibility complex class III region, in a cluster with two closely related genes which encode similar proteins.

Heat Shock Protein 27 (HSP27) Antibody, Abbexa, abx011871

The protein encoded by this gene is induced by environmental stress and developmental changes. The encoded protein is involved in stress resistance and actin organization and translocates from the cytoplasm to the nucleus upon stress induction. Defects in this gene are a cause of Charcot-Marie-Tooth disease type 2F (CMT2F) and distal hereditary motor neuropathy (dHMN). (provided by RefSeq) Tissue specificity: Detected in all tissues tested: skeletal muscle, heart, aorta, large intestine, small intestine, stomach, esophagus, bladder, adrenal gland, thyroid, pancreas, testis, adipose tissue, kidney, liver, spleen, cerebral cortex, blood serum and cerebrospinal fluid. Highest levels are found in the heart and in tissues composed of striated and smooth muscle.

Heat Shock Protein 27 (HSP27) Antibody, Abbexa, abx033222

In response to adverse changes in their environment, cells from many organisms increase the expression of a class of proteins referred to as heat shock or stress proteins. HSBP1 exhibits rapid increased phosphorylation in response to various mitogens, tumor promoters (e.g. phorbol esters) and calcium ionophores, and high levels are associated with carcinoma of the breast and with endometrial adenocarcinomas. Heat shock of HeLa cell cultures, or treatment with arsenite, phorbol ester, or tumor necrosis factor, causes a rapid phosphorylation of preexisting HSBP1, with Ser82 as the major site and Ser78 the minor site of phosphorylation. HSBP1 may exert phosphorylation-activated functions linked with growth signaling pathways in unstressed cells. A homeostatic function at this level could protect cells from adverse effects of signal transduction systems which may be activated inappropriately during stress.

Heat Shock Protein 40 (HSP40) Antibody, Abbexa, abx027362

DnaJ (Hsp40) belongs to the DnaJ-class of molecular chaperones with a C-terminal Zn finger domain. HSP40 (DnaJ) together with DnaK and GrpE form a molecular chaperone that is involved in formation of protein complexes, protein folding, prevention of protein aggregation, and protein turnover and export. Several human neurodegenerative diseases involve the expansion of a polyglutamine within the disease proteins. Molecular chaperones such as HSP40 complexes can modulate polyglutamine pathogenesis In transgenic Drosophila disease models of Machado-Joseph disease and Huntington disease Hdj1, the Drosophila homolog to human HSP40, demonstrates substrate specificity for polyglutamine proteins suppression in combination with other molecular chapterones of neurotoxicity, and altered solubility of mutant polyglutamine proteins.

Heat Shock Protein 27 (HSP27) Antibody, Abbexa, abx033224

In response to adverse changes in their environment, cells from many organisms increase the expression of a class of proteins referred to as heat shock or stress proteins. HSBP1 exhibits rapid increased phosphorylation in response to various mitogens, tumor promoters (e.g. phorbol esters) and calcium ionophores, and high levels are associated with carcinoma of the breast and with endometrial adenocarcinomas. Heat shock of HeLa cell cultures, or treatment with arsenite, phorbol ester, or tumor necrosis factor, causes a rapid phosphorylation of preexisting HSBP1, with Ser82 as the major site and Ser78 the minor site of phosphorylation. HSBP1 may exert phosphorylation-activated functions linked with growth signaling pathways in unstressed cells. A homeostatic function at this level could protect cells from adverse effects of signal transduction systems which may be activated inappropriately during stress.

Heat Shock Protein 70 (HSP70) Antibody, Abbexa, abx137350

Heat Shock Protein 70 (HSP70) Antibody is a Mouse Monoclonal antibody against Heat Shock Protein 70 (HSP70).