HSP27 (HSPB1) Antibody (S15) Blocking peptide
€363.00
In stock
SKU
AC-BP7199b
Background:
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.
Other Names:
Heat shock protein beta-1, HspB1, 28 kDa heat shock protein, Estrogen-regulated 24 kDa protein, Heat shock 27 kDa protein, HSP 27, Stress-responsive protein 27, SRP27, HSPB1, HSP27, HSP28
Target/Specificity:
The synthetic peptide sequence used to generate the antibody AP7199b was selected from the S15 region of human HSPB1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Gene Name: HSPB1
Gene ID: 3315
Primary Accession: P04792
Format: Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
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.
Other Names:
Heat shock protein beta-1, HspB1, 28 kDa heat shock protein, Estrogen-regulated 24 kDa protein, Heat shock 27 kDa protein, HSP 27, Stress-responsive protein 27, SRP27, HSPB1, HSP27, HSP28
Target/Specificity:
The synthetic peptide sequence used to generate the antibody AP7199b was selected from the S15 region of human HSPB1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.
Gene Name: HSPB1
Gene ID: 3315
Primary Accession: P04792
Format: Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed.
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