Foundational characteristics of cancer include proliferation, angiogenesis, migration, evasion of apoptosis, and cellular immortality. Find key markers for these cellular processes and antibodies to detect them.
The SUMOplot™ Analysis Program predicts and scores sumoylation sites in your protein. SUMOylation is a post-translational modification involved in various cellular processes, such as nuclear-cytosolic transport, transcriptional regulation, apoptosis, protein stability, response to stress, and progression through the cell cycle.
The Autophagy Receptor Motif Plotter predicts and scores autophagy receptor binding sites in your protein. Identifying proteins connected to this pathway is critical to understanding the role of autophagy in physiological as well as pathological processes such as development, differentiation, neurodegenerative diseases, stress, infection, and cancer.
HSP60 (Heat Shock Protein 60) (Mitochondrial Marker) Antibody - With BSA and Azide
Mouse Monoclonal Antibody [Clone HSPD1/780 ]
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC, IF, FC |
|---|---|
| Primary Accession | P10809 |
| Other Accession | 3329, 595053 |
| Reactivity | Human, Mouse, Rat, Rabbit, Hamster, Monkey, Pig, Chicken, Bovine, Sheep, Dog |
| Host | Mouse |
| Clonality | Monoclonal |
| Isotype | Mouse / IgG1, kappa |
| Clone Names | HSPD1/780 |
| Calculated MW | 60kDa |
| Gene ID | 3329 |
|---|---|
| Other Names | 60 kDa heat shock protein, mitochondrial, 60 kDa chaperonin, Chaperonin 60, CPN60, Heat shock protein 60, HSP-60, Hsp60, HuCHA60, Mitochondrial matrix protein P1, P60 lymphocyte protein, HSPD1, HSP60 |
| Storage | Store at 2 to 8°C.Antibody is stable for 24 months. |
| Precautions | HSP60 (Heat Shock Protein 60) (Mitochondrial Marker) Antibody - With BSA and Azide is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | HSPD1 |
|---|---|
| Synonyms | HSP60 |
| Function | Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (PubMed:11422376, PubMed:1346131). The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back- to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein (Probable). |
| Cellular Location | Mitochondrion matrix. |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
info@abcepta.com, and receive a free "I Love Antibodies" mug.
Provided below are standard protocols that you may find useful for product applications.
Background
Recognizes a 60kDa protein, identified as the heat shock protein 60 (hsp60). A wide variety of environmental and pathophysiological stressful conditions trigger the synthesis of a family of proteins known as heat shock proteins (hsp�s), more appropriately called as stress response proteins (srp�s). Hsp60 is a potential antigen in a number of autoimmune diseases. In human arthritis and in experimentally induced arthritis in animals, disease development coincides with the development of immune reactivity directed against not only bacterial hsp60, but also against its mammalian homolog.
References
Schlesinger, M.J., et al. 1982. Heat Shock: from Bacteria to Man. Cold Spring Harbor, N.Y.: Cold Spring Harbor Laboratory
If you have used an Abcepta product and would like to share how it has performed, please click on the "Submit Review" button and provide the requested information. Our staff will examine and post your review and contact you if needed.
If you have any additional inquiries please email technical services at tech@abcepta.com.
Ordering Information
Other Products
Shipping Information
