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HSC70 (HSP73) Antibody
HSC70 (HSP73) Antibody, Clone 1F2-H5
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC, ICC, IP, E, PLA, PBA, AM |
|---|---|
| Primary Accession | P11142 |
| Other Accession | NP_006588.1 |
| Host | Mouse |
| Isotype | IgG2a Kappa |
| Reactivity | Human, Mouse, Rat |
| Clonality | Monoclonal |
| Description | Mouse Anti-Human HSC70 (HSP73) Monoclonal IgG2a Kappa |
| Target/Specificity | Detects ~73kDa. Does not cross react with HSP70. |
| Other Names | HSC54 Antibody, HSC71 Antibody, HSC73 Antibody, HSP71 Antibody, HSP73 Antibody, HSPA10 Antibody, HSPA8 Antibody, LAP1 Antibody, NIP71 Antibody |
| Clone Names | 1F2-H5 |
| Immunogen | Full length human HSC70 |
| Purification | Protein G Purified |
| Storage | -20ºC |
| Storage Buffer | PBS pH7.4, 50% glycerol, 0.09% sodium azide |
| Shipping Temperature | Blue Ice or 4ºC |
| Certificate of Analysis | 1 µg/ml of SMC-151 was sufficient for detection of HSC70 in 10 µg of HeLa lysate by colorimetric immunoblot analysis using Goat anti-mouse IgG:HRP as the secondary antibody. |
| Cellular Localization | Cytoplasm | Melanosome |
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Provided below are standard protocols that you may find useful for product applications.
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 50% 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). When cells are subjected to metabolic stress (e.g., heat shock) a member of the HSP 70 family, HSP 70 (HSP72), is expressed; HSP 70 is highly related to HSC70 (>90% sequence identity). Constitutively expressed HSC70 rapidly forms a stable complex with the highly inducible HSP70 in cells following heat shock. The interaction of HSC70 with HSP 70 is regulated by ATP. These two heat shock proteins move together in the cell experiencing stress. Furthermore, research on HSC70 has implicates it with a role in facilitating the recovery of centrosomal structure and function after heat shock (6).
References
1. Brown C.L. et al. (1993) J.Cell Biol., 120 (5): 1101-1112.
2. Boorstein W.R., Ziegelhoffer T., and 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., and Valencia A. (1992) Proc. Nut1Acad. Sci. USA 89: 7290-7294.
6. Brown C.L. et al. (1996) J. Biol. Chem. 271(2): 833-840.
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