HSP27 Antibody (8A7) [Alexa Fluor® 647]

Alexa Fluor (R) products are provided under an intellectual property license from Life Technologies Corporation. The purchase of this product conveys to the buyer the non-transferable right to use the purchased product and components of the product only in research conducted by the buyer (whether the buyer is an academic or for-profit entity). The sale of this product is expressly conditioned on the buyer not using the product or its components, or any materials made using the product or its components, in any activity to generate revenue, which may include, but is not limited to use of the product or its components: (i) in manufacturing; (ii) to provide a service, information, or data in return for payment; (iii) for therapeutic, diagnostic or prophylactic purposes; or (iv) for resale, regardless of whether they are resold for use in research. For information on purchasing a license to this product for purposes other than as described above, contact Life Technologies Corporation, 5791 Van Allen Way, Carlsbad, CA 92008 USA or outlicensing@lifetech.com. This conjugate is made on demand. Actual recovery may vary from the stated volume of this product. The volume will be greater than or equal to the unit size stated on the datasheet.

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.

Array NB110-96431AF647

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