STUB1 Antibody (C-term)
Affinity Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, FC, E |
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Primary Accession | Q9UNE7 |
Other Accession | Q9WUD1, Q5ZHY5, NP_005852.2 |
Reactivity | Human |
Predicted | Chicken, Mouse |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 34856 Da |
Antigen Region | 236-263 aa |
Gene ID | 10273 |
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Other Names | E3 ubiquitin-protein ligase CHIP, 632-, Antigen NY-CO-7, CLL-associated antigen KW-8, Carboxy terminus of Hsp70-interacting protein, STIP1 homology and U box-containing protein 1 {ECO:0000312|HGNC:HGNC:11427}, STUB1 (HGNC:11427) |
Target/Specificity | This STUB1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 236-263 amino acids from the C-terminal region of human STUB1. |
Dilution | WB~~1:1000 FC~~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 | STUB1 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | STUB1 {ECO:0000303|PubMed:23973223, ECO:0000312|HGNC:HGNC:11427} |
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Function | E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation (PubMed:10330192, PubMed:11146632, PubMed:11557750, PubMed:23990462). Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension (PubMed:10330192, PubMed:11146632, PubMed:11557750, PubMed:23990462). Ubiquitinates NOS1 in concert with Hsp70 and Hsp40 (PubMed:15466472). Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90 (PubMed:10330192, PubMed:11146632, PubMed:15466472). Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation (PubMed:11557750, PubMed:23990462). Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome (PubMed:19713937). Mediates polyubiquitination of CYP3A4 (PubMed:19103148). Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation (PubMed:19567782). Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation (PubMed:27708256). Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner (PubMed:23973223). Catalyzes monoubiquitination of SIRT6, preventing its degradation by the proteasome (PubMed:24043303). Likely mediates polyubiquitination and down-regulates plasma membrane expression of PD- L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity (PubMed:28813410). Negatively regulates TGF-beta signaling by modulating the basal level of SMAD3 via ubiquitin-mediated degradation (PubMed:24613385). May regulate myosin assembly in striated muscles together with UBE4B and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation (PubMed:17369820). Mediates ubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation (PubMed:29883609). |
Cellular Location | Cytoplasm. Nucleus. Note=Translocates to the nucleus in response to inflammatory signals in regulatory T-cells (Treg) |
Tissue Location | Expressed in differentiated myotubes (at protein level) (PubMed:17369820). Highly expressed in skeletal muscle, heart, pancreas, brain and placenta (PubMed:10330192, PubMed:11435423) Detected in kidney, liver and lung (PubMed:10330192, PubMed:11435423) |
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Provided below are standard protocols that you may find useful for product applications.
Background
STUB1, or CHIP, is a ubiquitin ligase/cochaperone that participates in protein quality control by targeting a broad range of chaperone protein substrates for degradation (Min et al., 2008 [PubMed 18411298]).
References
Stankiewicz, M., et al. FEBS J. 277(16):3353-3367(2010)
Naito, A.T., et al. Circ. Res. 106(11):1692-1702(2010)
Loffek, S., et al. Hum. Mutat. 31(4):466-476(2010)
Graf, C., et al. Biochemistry 49(10):2121-2129(2010)
Schulke, J.P., et al. PLoS ONE 5 (7), E11717 (2010) :
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