HSP27 Antibody (G3.1)

Hsp25 is the mouse homologue of the human Hsp27 protein, a member of the small heat shock protein family comprised of a diverse group of proteins from approx. 15 to >30kDa(1). The basic structure of most sHsps is a homologous and highly conserved amino acid sequence, with an alpha-crystallin-domain at the C-terminus and the WD/EPF domain at the less conserved N-terminus. This N-terminus is essential for the development of high molecular oligomers (2, 3). Hsp27-oligomers consist of stable dimers formed by as many as 8-40 Hsp27 protein monomers (4). The oligomerization status is connected with the chaperone activity: aggregates of large oligomers have high chaperone activity, whereas dimers have no chaperone activity (5). HSP27 is localized to the cytoplasm of unstressed cells but can redistribute to the nucleus in response to stress, where it may function to stabilize DNA and/or the nuclear membrane. It can be rapidly phosphorylated in response to physiological stimuli relevant to the cell type examined. Thus, hsp27 has been suggested to be an important intermediate in second messenger mediated signaling pathways (6). Other functions include chaperone activity (as mentioned above), thermotolerance in vivo, inhibition of apoptosis, and signal transduction. Specifically, in vitro, it acts as an ATP-independent chaperone by inhibiting protein aggregation and by stabilizing partially denatured proteins, which ensures refolding of the HSP70 complex. Hsp27 is also involved in the apoptotic signaling pathway because it interferes with the activation of cytochrome c/Apaf-1/dATP complex, thereby inhibiting the activation of procaspase-9. It is also hypothesized that hsp27 may serve some role in cross-bridge formation between actin and myosin (7). And finally, Hsp27 is also thought to be involved in the process of cell differentiation. The up-regulation of Hsp27 correlates with the rate of phosphorylation and with an increase of large oligomers. It is possible that Hsp27 may play a crucial role in termination of growth (8).

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

We have publications tested in 1 confirmed species: Mouse.

We have publications tested in 2 applications: B/N, WB.

Showing Publications 1 - 4 of 4.

Publications using NBP2-32972	Applications	Species
Schwab M, Thunborg K, Azimzadeh O et al. Abstract 5426: Down-regulation of cancer metabolism enhances radiosensitivity by impairing the heat shock response Cancer Research 2022-06-15
Schwab M, Dezfouli A, Khosravi M et al. The radiation- and chemo-sensitizing capacity of diclofenac can be predicted by a decreased lactate metabolism and stress response Research Square 2023-03-20 (WB)	WB
Schwab M, Multhoff G A Low Membrane Hsp70 Expression in Tumor Cells With Impaired Lactate Metabolism Mediates Radiosensitization by NVP-AUY922 Frontiers in oncology [PMID: 35463341] (WB, Mouse)	WB	Mouse
Schwab M, Thunborg K, Azimzadeh O et al. Targeting Cancer Metabolism Breaks Radioresistance by Impairing the Stress Response Cancers (Basel) 2021-07-27 [PMID: 34359663] (B/N, WB)	B/N, WB

Images	Ratings	Applications	Species	Date	Details
Enlarge	4 reviewed by: Byron Baron	WB	Human	12/24/2016	View Summary Application Western Blot Sample Tested SW480 (colon) Species Human Lot 3315-1P150413 Comments Comments Primary mouse anti HSP27 antibody diluted 1:1000 in TBS. Membrane incubation for 2 hours at RT. Secondary IRDye 800CW goat anti mouse antibody diluted 1:10000 in TBS. Membrane incubation for 1 hour at RT. Detection by Li-Cor Odyssey

Array NBP2-32972

• HSP27 Antibodies
• HSP27 Antibody Pair
• HSP27 ELISA Kits
• HSP27 Lysate
• HSP27 Proteins
• HSP27 ELISAs
• HSP27 Proteins and Enzyme