HSPBP1 Antibody (N-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| IHC-P, WB, E |
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Primary Accession | Q9NZL4 |
Other Accession | Q6IMX7, Q99P31, Q4R588, NP_036399.3, NP_001123578.1 |
Reactivity | Human |
Predicted | Monkey, Mouse, Rat |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 39303 Da |
Antigen Region | 69-97 aa |
Gene ID | 23640 |
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Other Names | Hsp70-binding protein 1, HspBP1, Heat shock protein-binding protein 1, Hsp70-binding protein 2, HspBP2, Hsp70-interacting protein 1, Hsp70-interacting protein 2, HSPBP1, HSPBP |
Target/Specificity | This HSPBP1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 69-97 amino acids from the N-terminal region of human HSPBP1. |
Dilution | WB~~1:1000 IHC-P~~1:10~50 |
Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification. |
Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
Precautions | HSPBP1 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | HSPBP1 (HGNC:24989) |
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Synonyms | HSPBP |
Function | Inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and interfering with ATP binding. Interferes with ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of immature CFTR. |
Tissue Location | Ubiquitous.. |
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Provided below are standard protocols that you may find useful for product applications.
Background
HSPBP1 inhibits HSPA1A chaperone activity by changing the conformation of the ATP-binding domain of HSPA1A and interfering with ATP binding. Interferes with ubiquitination mediated by STUB1 and inhibits chaperone-assisted degradation of immature CFTR.
References
Graner, M.W., et al. Cancer Sci. 100(10):1870-1879(2009)
Evdonin, A., et al. Biol. Cell 101(6):351-360(2009)
Souza, A.P., et al. Cell Stress Chaperones 14(3):301-310(2009)
Howarth, J.L., et al. J. Neurochem. 108(4):945-951(2009)
Snyers, L., et al. Biochem. Biophys. Res. Commun. 368(3):767-771(2008)
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