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H2289

Sigma-Aldrich

Anti-Heat Shock Protein 27/25 antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-HSP27/25

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 25 kDa (mouse)
antigen 27 kDa (human)

species reactivity

human, canine, rat, mouse

technique(s)

indirect immunofluorescence: 4-8 μg/mL using MDCK cell line.
microarray: suitable
western blot: 0.5-1 μg/mL using whole extract of rat fibroblast Rat-1 cell line or Madin-Darby canine kidney (MDCK) cell line.
western blot: 1-2 μg/mL using mouse brain extract (S1 fraction) or human HeLa cell line

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... HSPB1(3315)
mouse ... Hspb1(15507)
rat ... Hspb1(24471)

General description

Heat shock protein 27 (HSP27), also known as mouse HSP25, is a highly conserved oligomeric protein. This protein is expressed constitutively in many cell types and tissues, such as the placenta, breast, skin, platelets, uterus and cervix. HSP27 is expressed in the cytoplasm and localizes to the nucleus upon stress stimuli. The HSPB1 or the HSP27 gene is mapped on the human chromosome at 7q11.23.

Specificity

Anti-Heat Shock Protein 27/25 (HSP27/25) recognizes HSP27 (27 kDa) (mouse HSP25).

Immunogen

synthetic peptide corresponding to amino acids 190-209 located at the C-terminus of mouse HSP27/25, conjugated to KLH. The sequence is identical in dog and Chinese hamster, highly conserved in rat HSP27 (85% identity), and to a lesser extent in human HSP27 (65%).

Application

Anti-Heat Shock Protein 27/25 antibody produced in rabbit may be used in western blotting and immunofluorescence.

Biochem/physiol Actions

Heat shock protein 27 (HSP27) accumulates in cells exposed to a short period of hyperthermia and contributes to the development of a transient state of thermotolerance. This protein is stimulated by various cytokines, growth factors, hormones, and chemicals. HSP27 shows rapid phosphorylation following exposure to stress stimuli. HSP27 acts as an actin-cap binding protein and can inhibit actin polymerization, thus modulating actin dynamics during stress. It also protects against apoptotic cell death triggered by a variety of stimuli including hyperthermia, oxidative stress, Fas ligand, and cytotoxic drugs. HSP27 interferes specifically with the mitochondrial pathway of caspase-induced cell death by acting as a negative regulator of cytochrome c-dependent activation of caspase-3.

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 extended storage, freeze in working aliquots. 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 dilu-tions 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.

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Storage Class Code

10 - Combustible liquids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

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D R Ciocca et al.
Journal of the National Cancer Institute, 85(19), 1558-1570 (1993-10-06)
Heat shock and other environmental and pathophysiologic stresses stimulate synthesis of heat shock proteins (Hsps). These proteins enable the cell to survive and recover from stressful conditions by as yet uncompletely understood mechanisms. Hsp27 is an important small Hsp (molecular
P Mehlen et al.
The Journal of biological chemistry, 272(50), 31657-31665 (1998-02-12)
Small stress proteins are developmentally regulated and linked to cell growth and differentiation. The early phase of murine embryonic stem (ES) cell differentiation, characterized by a gradual growth arrest, is accompanied with hsp27 transient accumulation. This differentiation process also correlated
P Pandey et al.
Oncogene, 19(16), 1975-1981 (2000-05-10)
The release of mitochondrial cytochrome c by genotoxic stress induces the formation of a cytosolic complex with Apaf-1 (mammalian CED4 homolog) and thereby the activation of procaspase-3 (cas-3) and procaspase-9 (cas-9). Here we demonstrate that heat-shock protein 27 (Hsp27) inhibits
Pragya Verma et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 34(5), 1599-1612 (2014-01-31)
Heat shock factor 1 (HSF1) protects neurons from death caused by the accumulation of misfolded proteins. It is believed that this protective effect is mediated by the transcriptional stimulation of genes encoding heat shock proteins (HSPs), a family of chaperones
Constantin d'Ydewalle et al.
Nature medicine, 17(8), 968-974 (2011-07-26)
Charcot-Marie-Tooth disease (CMT) is the most common inherited disorder of the peripheral nervous system. Mutations in the 27-kDa small heat-shock protein gene (HSPB1) cause axonal CMT or distal hereditary motor neuropathy (distal HMN). We developed and characterized transgenic mice expressing

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