immunohistochemistry (formalin-fixed, paraffin-embedded sections): 2-4 μg/mL using rat cerebellum microarray: suitable western blot: 0.5-1 μg/mL using cytosolic fraction of rat brain and whole cell extract of mouse fibroblast NIH3T3 cell line
Heat shock protein 110 (Hsp110) belongs to a family of large stress proteins referred to as the SSE family. This protein is a normal constituent of mammalian cells, ubiquitously expressed but at higher levels in the brain.
Specificity
Anti-Heat Shock Protein 110 (Hsp110) (HD-19) recognizes Hsp110 (110 kDa, may appear as a doublet band in some cell/tissue extracts).
Immunogen
synthetic peptide located at the C-terminus of mouse Hsp110 (amino acids 840-858), conjugated to KLH.
Application
Anti-Heat Shock Protein 110 (HD-19) antibody produced in rabbit may be used in immunoblotting and immunohistochemistry.
Biochem/physiol Actions
Heat shock protein 110 (Hsp110) is associated with the nucleoli of non-stressed and heat-stressed murine cells. Overexpression of Hsp110 gene has been shown to confer cellular heat resistance to prevent protein aggregation and to keep denatured protein in a folding-competent state. HSP110 plays a role in the pathophysiology of brain damage such as ischemia/reperfusion injuries and pathological conditions such as Alzheimer′s disease.
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Storage and Stability
For continuous use, store at 2-8 °C for up to one month. For prolonged storage, freeze in working aliquots at −20 °C. Repeated freezing and thawing is not recommended. Storage in frost-free freezers is also not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilutions should be discarded if not used within 12 hours.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Molecular and cellular biology, 30(19), 4626-4643 (2010-08-04)
Accumulation of tau into neurofibrillary tangles is a pathological consequence of Alzheimer's disease and other tauopathies. Failures of the quality control mechanisms by the heat shock proteins (Hsps) positively correlate with the appearance of such neurodegenerative diseases. However, in vivo
Hsp110 is one of the few, major heat shock proteins of mammalian cells and was one of the earliest heat shock proteins described. However, it has only recently been cloned and studied at the molecular level. It has been noted
The Journal of biological chemistry, 272(50), 31636-31640 (1998-02-12)
The 110-kDa heat shock protein (hsp110) has long been recognized as one of the primary heat shock proteins in mammalian cells. It belongs to a recently described protein family that is a significantly diverged subgroup of the hsp70 family and
Both the Grp170 and Hsp110 families represent relatively conserved and distinct sets of stress proteins, within a more diverse category that also includes the Hsp70s. All of these families are found in a wide variety of organisms from yeasts to
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