Search results for HSP27

Anti-HSPB1/HSP27 Antibody (R1J73), AntibodySystem, RHC10501
Host
Reactivity
Applications
IF, IHC, IP, WB
Conjugation

Anti-Hsp27 (phospho S15) antibody, Abcam, AB5581
Host
Rabbit
Reactivity
Human
Applications
ICC/IF, WB, IP
Conjugation

Anti-Hsp27 (phospho S86) antibody, Abcam, AB17938
Host
Rabbit
Reactivity
Mouse, Human
Applications
ICC, WB
Conjugation

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.
Host
Rabbit
Reactivity
Human
Applications
ELISA, WB, IHC
Conjugation
Unconjugated

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.
Host
Rabbit
Reactivity
Human
Applications
ELISA, WB, IHC
Conjugation
Unconjugated

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.
Host
Mouse
Reactivity
Human, Rat
Applications
ELISA, WB, IHC, IF/ICC, FCM
Conjugation
Unconjugated

Anti-Mouse HSPB1/HSP27 Polyclonal Antibody, AntibodySystem, PMC10501
Host
Reactivity
Applications
ELISA, IHC, WB
Conjugation

Heat Shock Protein 27 (HSP27) Antibody, Abbexa, abx234044
HSP27 Antibody is a Rabbit Polyclonal against HSP27.
Host
Rabbit
Reactivity
Human, Mouse, Rat
Applications
ELISA, WB, IHC, IF/ICC
Conjugation
Unconjugated

Heat Shock Protein 27 (HSP27) Antibody, Abbexa, abx033221
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.
Host
Rabbit
Reactivity
Human
Applications
ELISA, WB
Conjugation
Unconjugated

Heat Shock Protein 27 (HSP27) Antibody, Abbexa, abx444888
HSP27 Antibody is a Mouse Monoclonal antibody against HSP27.
Host
Mouse
Reactivity
Human
Applications
ELISA, WB, IHC, IF/ICC, IP
Conjugation
Unconjugated
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