Hsp25/Hsp27 Antibody from ROCKLAND IMMUNOCHEMICALS INC.
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| Antigenic Specificity | Hsp25/Hsp27 |
| Clone | 8A7 |
| Host Species | Mouse |
| Reactive Species | human, mouse, rat, bovine, dog, guinea pig, hamster, sheep |
| Isotype | IgG |
| Format | Protein G purified |
| Size | 100 µg |
| Concentration | 1 mg/mL |
| Applications | ELISA, Flow Cytometry, Immunohistochemistry, IF Microscopy, Immunoprecipitation, Western Blot |
| Reviews / Ratings | If you have used this antibody, please help fellow researchers by submitting reviews to pAbmAbs and antYbuddY. |
| Description | Anti-Hsp25/Hsp27 Antibody was purified by Protein G chromatography. A BLAST analysis was used to suggest cross-reactivity with Hsp25/27 from Mouse, Rat, Bovine, Canine, Guinea pig, and Hamster based on 100% homology with the immunizing sequence. Recognizes Hsp25 and Hsp27, cross reacts with alpha B crystallin. Cross-reactivity with Hsp25/Hsp27 from other sources has not been determined. Heat Shock research. 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 ~15 to >30kDa. The basic structure of most sHsps is a homologous and highly conserved amino acid sequence, with an α-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. Hsp27-oligomers consist of stable dimers formed by as many as 8-40 Hsp27 protein monomers. The oligomerization status is connected with the chaperone activity: aggregates of large oligomers have high chaperone activity, whereas dimers have no chaperone activity.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. Other functions include chaperone activity (as mentioned above), thermo-tolerance 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. 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. |
| Immunogen | Hsp25/Hsp27 Antibody was produced in mice by repeated immunizations raised against an internal region of hsp27 synthetic peptide. |
| Other Names | Heat shock protein beta-1, HspB1, Growth-related 25 kDa protein, Heat shock 25 kDa protein, HSP 25, Heat shock 27 kDa protein, HSP 27, p25, Hspb1, Hsp25, Hsp27 |
| Gene, Accession # | Hspb1, Gene ID: 15507, NCBI: NP_038588.2, UniProt: P14602 |
| Catalog # | 200-301-F55 |
| Price | $485 |
| Order / More Info | Hsp25/Hsp27 Antibody from ROCKLAND IMMUNOCHEMICALS INC. |
| Product Specific References | n/a |
ROCKLAND IMMUNOCHEMICALS INC.
ROCKLAND IMMUNOCHEMICALS INC.
PO Box 5199
Limerick PA 19468
P: 484-791-3823
P: 800.656.7625
F: 484.369.8654
orders@rockland.com
Technical Support: tech@rockland.com
https://www.rockland.com/
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