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.
FKBP51 Antibody
FKBP51 Antibody, Clone Hi51B
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, ICC |
|---|---|
| Primary Accession | Q13451 |
| Other Accession | NP_001139247.1 |
| Host | Mouse |
| Isotype | IgG |
| Reactivity | Human, Mouse, Rat, Rabbit, Hamster, Dog |
| Clonality | Monoclonal |
| Description | Mouse Anti-Human FKBP51 Monoclonal IgG |
| Target/Specificity | Detects ~51kDa. |
| Other Names | AIG6 Antibody, FK506 binding protein 5 Antibody, FKBP5 Antibody, FKBP54 Antibody, HSP90 binding immunophilin Antibody, p54 Antibody, Pplase Antibody, Ptg10 Antibody, Rotamase Antibody, T cekk FK506 binding protein Antibody |
| Clone Names | Hi51B |
| Immunogen | Synthetic peptide corresponding to the residues of human FKBP51 |
| Purification | Protein G Purified |
| Storage | -20ºC |
| Storage Buffer | PBS, 50% glycerol, 0.09% sodium azide |
| Shipping Temperature | Blue Ice or 4ºC |
| Certificate of Analysis | A 1:2000 dilution was sufficient for detection of FKBP51 in ~50 µg total protein using WB analysis. |
| Cellular Localization | Cytoplasm | Nucleus |
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
HSP90 is crucial to cellular signaling by its regulation of the folding, activity, and stability of a wide range of client proteins. These client protein complexes may also contain one or more cochaperones (1). One class of HSP90-binding cochaperone is composed of proteins with a characteristic tetratricopeptide repeat (TPR) domain that forms an HSP90 binding site. Among the TPR cochaperones of HSP90 are Hop/Sti1, protein phosphatase PP5, and members of both the FK506- and cyclosporin A-binding families of immunophilins (2). FK506-binding protein 51 (FKBP51) and FKBP52 are large molecular weight immunophilins that are part of the mature glucocorticoid receptor (GR) heterocomplex (3). The N terminal domain of each protein binds FK506 and has peptidyl-prolyl isomerase (PPIase) activity that converts prolyl peptide bonds within target proteins from cis- to trans- proline. The C-terminal domains contain the TPR repeats involved in protein-protein interactions with the HSP90 (4). Although FKBP52 and FKBP51 share ~75% sequence similarity, they affect hormone binding by glucocorticoid receptor in opposing manners and have different HSP90-binding characteristics (3). FK506 binding protein 51 kDa (FKBP51 or otherwise referred to as FKBP54) has been identified as a progestininducible gene. This protein is predominantly expressed in murine T cells but in humans, it is abundantly expressed in numerous tissues at levels many times higher than FKBP12. The FKBP51 gene is known to be induced by glucocorticoids (5).
References
1. Cheung-Flynn J., Roberts P.J., Riggs D.L., and Smith D.F.(2003) J. Biol. Chem. 278(19): 17388-17394.
2. Davies T.H., Ning Y.N., and Sanchez E.R. (2002) J Biol. Chem. 277 (7): 4597-4600.
3. Wu B. et al. (2004) Proc. Natl. Acad. Sci. USA. 101(22): 8348-8353.
4. Denny W.B., Prapapanich V., Smith D.F., and Scammell J.G. (2005) Endocrinology 146(7): 3194-3201.
5. Hubler T.R. et al. (2003) Endocrinology 144(6): 2380- 2387.
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
