Mouse Hsp70/Hsc70 Monoclonal Antibody | anti-HSPA2 antibody

Hsp70/Hsc70 Antibody: PerCP

Cat. Num. AAA803387

• Gene Names: HSPA2; HSP70
• Reactivity: Human, Mouse, Rat, Sheep, Dog, Beluga, Bovine, Fish, Guinea pig, Scallop pig, Hamster, Rabbit, Chicken, Xenopus, Drosophila, Yeast
• Applications: Western Blot, Immunoprecipitation, Immunohistochemistry
• Synonyms: Hsp70/Hsc70; Monoclonal Antibody; Hsp70/Hsc70 Antibody: PerCP; HSC54; Hsc70; HSC71; Hsp70 1; Hsp701/Hsp70 2; Hsp70.1; Hsp71; Hsp72; Hsp73; HSPA1; HSPA10; HSPA1A; HSPA1B; LAP1; NIP71; anti-HSPA2 antibody

• Host: Mouse
• Reactivity: Human, Mouse, Rat, Sheep, Dog, Beluga, Bovine, Fish, Guinea pig, Scallop pig, Hamster, Rabbit, Chicken, Xenopus, Drosophila, Yeast
• Clonality: Monoclonal
• Isotype: IgG2a
• Clone Number: BB70
• Form/Format: Protein G Purified
• Concentration: 1mg/mL (varies by lot)
• Sequence Length: 634

• Applicable Applications for anti-HSPA2 antibody: Westen Blot (WB), Immunoprecipitation (IP), Immunohistochemistry (IHC), Protein-binding Assay
• Application Notes: 1ug/ml was sufficient for detection of hsp70/Hsc70 in 20ug of HeLa lysate.
• Conjugate: PerCP
• Storage Buffer: PBS pH7.2, 50% glycerol, 0.09% sodium azide
• Preparation and Storage: -20 degree C

Immunohistochemistry (IHC)

(Immunohistochemistry analysis using Mouse Anti-Hsp70 Monoclonal Antibody, Clone BB70. Tissue: inflamed colon. Species: Mouse. Fixation: Formalin. Primary Antibody: Mouse Anti-Hsp70 Monoclonal Antibody at 1:10000 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. Inflammatory cells. HSP70/HSC70 stained brown.)

Immunohistochemistry (IHC)

(Immunohistochemistry analysis using Mouse Anti-Hsp70 Monoclonal Antibody, Clone BB70. Tissue: colon carcinoma. Species: Human. Fixation: Formalin. Primary Antibody: Mouse Anti-Hsp70 Monoclonal Antibody at 1:10000 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. HSP70/HSC70 cells stained brown.)

Western Blot (WB)

(Western Blot analysis of Bovine MDBK cell lysates showing detection of Hsp70 protein using Mouse Anti-Hsp70 Monoclonal Antibody, Clone BB70. Primary Antibody: Mouse Anti-Hsp70 Monoclonal Antibody at 1:1000.)

Immunocytochemistry/Immunofluorescence (ICC/IF)

(Immunocytochemistry/Immunofluorescence analysis using Mouse Anti-Hsp70 Monoclonal Antibody, Clone BB70. Tissue: hepatocyte nuclei. Species: Rat. Primary Antibody: Mouse Anti-Hsp70 Monoclonal Antibody at 1:200. Liver sections were paraffin embedded. First pictures in series show two hours after exposure to stress, the second shows the control. Courtesy of: G. Matic, University of Belgrade, Serbia.)

Western Blot (WB)

(Western Blot analysis of Human Cervical cancer cell line (HeLa) lysate showing detection of Hsp70 protein using Mouse Anti-Hsp70 Monoclonal Antibody, Clone BB70. Primary Antibody: Mouse Anti-Hsp70 Monoclonal Antibody at 1:1000. Secondary Antibody: HRP Goat Anti-Rat.)

Immunohistochemistry (IHC)

(Immunohistochemistry analysis using Mouse Anti-Hsp70 Monoclonal Antibody, Clone BB70. Tissue: hepatocytes. Species: Rat. Fixation: Paraffin Embedded. Primary Antibody: Mouse Anti-Hsp70 Monoclonal Antibody at 1:200. Liver sections were paraffin embedded. First pictures in series show two hours after exposure to stress, the second shows the control. Courtesy of: G. Matic, University of Belgrade, Serbia.)

Related Product Information for anti-HSPA2 antibody

Background Info: Detects ~72 and ~73kDa proteins corresponding to the molecular mass of inducible Hsp and Hsc on SDS PAGE immunoblots.

Scientific Background: Hsp70 genes encode abundant heat-inducible 70-kDa hsps (hsp70s). In most eukaryotes hsp70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 5O% identity (2). The N-terminal two thirds of hsp70s are more conserved than the C-terminal third. Hsp70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides (3). When hsc70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44 kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half (4). The structure of this ATP binding domain displays multiple features of nucleotide binding proteins (5). All hsp70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the hsp70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein (6). The universal ability of hsp70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport.

Product Categories/Family for anti-HSPA2 antibody

Chaperones; Heat Shock; Trafficking

References

1. Zho J. (1998) Cell 94 : 471-480. 2. Boorstein W. R., Ziegelhoffer T. & Craig E. A. (1993) J. Mol. Evol.38 (1): 1-17. 3. Rothman J. (1989) Cell 59: 591 -601. 4. DeLuca-Flaherty et al. (1990) Cell 62: 875-887. 5. Bork P., Sander C. & Valencia A. (1992) Proc. Nut1 Acad. Sci. USA 89: 7290-7294. 6. Fink A.L. (1999) Physiol. Rev. 79: 425-449. 7. Smith D.F., et al, (1993) Mol. Cell. Biol. 13(2): 869- 876. 8. Prapapanich V., et al. (1996) Mol. Cell. Biol. 16(11): 6200-6207. 9. Fernandez-Funez et al., (2000) Nature 408(6808): 101- 106.
1. Rodina, A. et al. (2013). Identification of an Allosteric Pocket on Human Hsp70 Reveals a Mode of Inhibition of This Therapeutically Important Protein. Cell Chemistry & Biology. doi: 10.1016/j.chembiol.2013.10.008
2. Kang, Y. et al. (2014). Heat Shock Protein 70 Inhibitors. 1. 2,5'-Thiodipyrimidine and 5-(Phenylthio)pyrimidine Acrylamides as Irreversible Binders to an Allosteric Site on Heat Shock Protein 70. J Med Chem. doi.org/10.1021/jm401551n
3. Taldone, T. et al. (2014). Heat Shock Protein 70 Inhibitors. 2. 2,5'-Thiodipyrimidines, 5-(Phenylthio)pyrimidines, 2-(Pyridin-3-ylthio)pyrimidines, and 3-(Phenylthio)pyridines as Reversible Binders to an Allosteric Site on Heat Shock Protein 70. J Med Chem. doi.org/10.1021/jm401552y
4. Rodina, A. et al. (2014). Affinity Purification Probes of Potential Use To Investigate the
Endogenous Hsp70 Interactome in Cancer. ACS Chem Biol. doi.org/10.1021/cb500256u

NCBI and Uniprot Product Information

• NCBI GI #: 55742654
• NCBI GeneID: 423504
• NCBI Accession #: NP_001006686.1
• NCBI GenBank Nucleotide #: NM_001006685.1
• UniProt Accession #: P08106
• Molecular Weight: 69,751 Da
• NCBI Official Full Name: heat shock 70 kDa protein
• NCBI Official Synonym Full Names: heat shock 70kDa protein 2
• NCBI Official Symbol: HSPA2
• NCBI Official Synonym Symbols: HSP70
• NCBI Protein Information: heat shock 70 kDa protein; heat shock protein 70; dnaK-type molecular chaperone
• UniProt Protein Name: Heat shock 70 kDa protein
• Protein Family: Heat shock-related 70 kDa protein
• UniProt Gene Name: HSP70
• UniProt Synonym Gene Names: HSP70
• UniProt Entry Name: HSP70_CHICK