Mouse Hsp25/Hsp27 Monoclonal Antibody | anti-HSPB2 antibody

Hsp25/Hsp27 Antibody: HRP

Cat. Num. AAA803007

• Gene Names: HSPB2; MKBP; HSP27; Hs.78846; LOH11CR1K
• Reactivity: Mouse, Rat, Bovine, Canine, Guinea pig, Hamster, Human. Recognizes Hsp25 and Hsp27, cross reacts with alpha B crystallin.
• Applications: Western Blot, Immunofluorescence, Immunocytochemistry, Immunoprecipitation, Immunohistochemistry
• Synonyms: Hsp25/Hsp27; Monoclonal Antibody; Hsp25/Hsp27 Antibody: HRP; HSPB2; Heat shock protein beta-2; HspB2; DMPK-binding protein; MKBP; anti-HSPB2 antibody

• Host: Mouse
• Reactivity: Mouse, Rat, Bovine, Canine, Guinea pig, Hamster, Human. Recognizes Hsp25 and Hsp27, cross reacts with alpha B crystallin.
• Clonality: Monoclonal
• Isotype: IgG
• Clone Number: 8A7
• Form/Format: Protein G Purified
• Concentration: 1mg/mL (varies by lot)
• Sequence Length: 182

• Applicable Applications for anti-HSPB2 antibody: Western Blot (WB), Immunofluorescence (IF), Immunocytochemistry (ICC), Immunoprecipitation (IP), Immunohistochemistry (IHC)
• Application Notes: WB 1:5000 (ECL), 1:200 (IF)
• Conjugate: HRP
• Storage Buffer: PBS, 50% glycerol, 0.09% sodium azide
• Preparation and Storage: -20 degree C

Immunohistochemistry (IHC)

(Immunohistochemistry analysis using Mouse Anti-Hsp27 Monoclonal Antibody, Clone 8A7. Tissue: embryo somites. Species: Rat. Primary Antibody: Mouse Anti-Hsp27 Monoclonal Antibody at 1:1000. Secondary Antibody: FITC Goat Anti-Mouse (green). Counterstain: Rhodamine-phalloidin labeled actin (red). Investigation at 11 days gestation. Courtesy of: Mike Welsh, Umich.)

Immunohistochemistry (IHC)

(Immunohistochemistry analysis using Mouse Anti-Hsp27 Monoclonal Antibody, Clone 8A7. Tissue: colon carcinoma. Species: Human. Fixation: Formalin. Primary Antibody: Mouse Anti-Hsp27 Monoclonal Antibody at 1:5000 for 12 hours at 4 degree C. Secondary Antibody: Biotin Goat Anti-Mouse at 1:2000 for 1 hour at RT. Counterstain: Mayer Hematoxylin (purple/blue) nuclear stain at 200 ul for 2 minutes at RT. Localization: Inflammatory cells. Magnification: 40x.)

Immunohistochemistry (IHC)

(Immunohistochemistry analysis using Mouse Anti-Hsp27 Monoclonal Antibody, Clone 8A7. Tissue: backskin. Species: Mouse. Fixation: Bouin's Fixative and paraffin-embedded. Primary Antibody: Mouse Anti-Hsp27 Monoclonal Antibody at 1:100 for 1 hour at RT. Secondary Antibody: FITC Goat Anti-Mouse (green) at 1:50 for 1 hour at RT. Localization: Epidermis.)

Western Blot (WB)

(Western Blot analysis of Rat Lung tissue lysates showing detection of Hsp27 protein using Mouse Anti-Hsp27 Monoclonal Antibody, Clone 8A7. Load: 15 ug. Block: 5% blocking solution. Primary Antibody: Mouse Anti-Hsp27 Monoclonal Antibody at 1:1000 for 2 hours at RT. Secondary Antibody: Goat Anti-Mouse: HRP for 1 hour at RT.)

Immunohistochemistry (IHC)

(Immunohistochemistry analysis using Mouse Anti-Hsp27 Monoclonal Antibody, Clone 8A7. Tissue: backskin. Species: Mouse. Fixation: Bouin's Fixative and paraffin-embedded. Primary Antibody: Mouse Anti-Hsp27 Monoclonal Antibody at 1:100 for 1 hour at RT. Secondary Antibody: FITC Goat Anti-Mouse (green) at 1:50 for 1 hour at RT. Localization: Epidermis.)

Related Product Information for anti-HSPB2 antibody

Background Info: Detects an 25kDa or 27kDa protein corresponding to the molecular mass of Hsp25/27 on SDS PAGE immunoblots.

Scientific Background: 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(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), 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 (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).

Product Categories/Family for anti-HSPB2 antibody

Chaperones; Heat Shock; Trafficking

References

1. Welch W.J. (1985) J Biol. Chem. 260: 3058-3062. 2.Kim K.K., Kim R., and Kim S. (1998) Nature 394(6693): 595-599. 3. Van Montfort R., Slingsby C., and Vierling E. (2001) Addv Protein Chem. 59: 105-56. 4. Ehrnsperger M., Graber S., Gaestel M. and Buchner J. (1997) EMBO J. 16: 221-229. 5. Ciocca D.R., Oesterreich S., Chamness G.C., McGuire W.L., and Fugua S.A. (1993) J Natl Cancer Inst. 85 (19): 1558-70. 6. Welsh M.J., Wu W., Parvinem M., and Gilmont R.R. (1996) Biol. Of Reprod. 55: 141-151. 7. Sarto C. Binnz P.A. and Mocarelli P. (2000) Electrophoresis. 21(6): 1218-26. 8. Arrigo A.P. (2005) J Cell Biochem. 94(2): 241-6. 9. Jia, Y. et al. (2001) J. Biol. Chem. 276(43):39911-39918.

NCBI and Uniprot Product Information

• NCBI GI #: 4504519
• NCBI GeneID: 3316
• NCBI Accession #: NP_001532.1
• NCBI GenBank Nucleotide #: NM_001541.3
• UniProt Accession #: P04792; Q6I9U7; Q16082
• Molecular Weight: 20,233 Da
• NCBI Official Full Name: heat shock protein beta-2
• NCBI Official Synonym Full Names: heat shock 27kDa protein 2
• NCBI Official Symbol: HSPB2
• NCBI Official Synonym Symbols: MKBP; HSP27; Hs.78846; LOH11CR1K
• NCBI Protein Information: heat shock protein beta-2; DMPK-binding protein; heat-shock protein beta-2
• UniProt Protein Name: Heat shock protein beta-2
• Protein Family: Heat shock protein
• UniProt Gene Name: HSPB2
• UniProt Synonym Gene Names: HspB2; MKBP
• UniProt Entry Name: HSPB2_HUMAN

NCBI Description

The protein encoded by this gene belongs to the superfamily of small heat-shock proteins containing a conservative alpha-crystallin domain at the C-terminal part of the molecule. The protein is expressed preferentially in the heart and skeletal muscle. This protein regulates Myotonic Dystrophy Protein Kinase, which plays an important role in maintenance of muscle structure and function. [provided by RefSeq, Dec 2012]

Uniprot Description

HSP27: a small heat shock protein that is regulated both transcriptionally and posttranslationally. Modulates actin polymerization and reorganization. Its expression level increases several-fold in response to stress and is phosphorylated by MAPKAP kinase 2. Cytoplasmic in interphase cells. Colocalizes with mitotic spindles in mitotic cells. Translocates to the nucleus during heat shock.

Protein type: Heat shock protein; Chaperone; Motility/polarity/chemotaxis

Chromosomal Location of Human Ortholog: 7q11.23

Cellular Component: proteasome complex; extracellular space; cytoskeleton; focal adhesion; cytoplasm; plasma membrane; spindle; nucleus; Z disc; cytosol

Molecular Function: identical protein binding; protein kinase C inhibitor activity; protein binding; ubiquitin binding; protein kinase C binding; protein kinase binding

Biological Process: positive regulation of tumor necrosis factor biosynthetic process; response to virus; positive regulation of blood vessel endothelial cell migration; response to unfolded protein; retinal homeostasis; positive regulation of interleukin-1 beta production; positive regulation of angiogenesis; negative regulation of protein kinase activity; gene expression; vascular endothelial growth factor receptor signaling pathway; cell motility; regulation of I-kappaB kinase/NF-kappaB cascade; regulation of translational initiation; negative regulation of apoptosis

Disease: Neuronopathy, Distal Hereditary Motor, Type Iib; Charcot-marie-tooth Disease, Axonal, Type 2f