SDS-PAGE
STUB1 (CHIP) recombinant protein
STUB1 (CHIP) recombinant protein
SDS-PAGE
SDS-PAGE
Scientific Background: CHIP(STUB1) or STIP1 homology and U-box containing protein 1 (also known as E3 ubiquitin protein ligase) is a ubiquitin ligase/cochaperone that participates in protein quality control by targeting a broad range of chaperone protein substrates for degradation (1). CHIP acts as a molecular switch for the degradation of misfolded proteins via the proteasome and lysosome pathways (2). CHIP controls the cellular level of BER enzymes and, correspondingly, the efficiency and capacity of BER. CHIP E3 ubiquitin ligases act sequentially in ER membrane and cytosol to monitor the folding status of CFTR and delF508.CHIP possesses intrinsic E3 ubiquitin ligase activity and promotes ubiquitylation.
2. Shin, Y.et.al: The co-chaperone carboxyl terminus of Hsp70-interacting protein (CHIP) mediates alpha-synuclein degradation decisions between proteasomal and lysosomal pathways. J. Biol. Chem. 280: 23727-23734, 2005.
NCBI and Uniprot Product Information
NCBI Description
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]).[supplied by OMIM, Jul 2009]
Uniprot Description
Function: E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. 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. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. 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. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation. Ref.2 Ref.10 Ref.11 Ref.12 Ref.22 Ref.23 Ref.25
Pathway: Protein modification; protein ubiquitination.
Subunit structure: Homodimer
By similarity. Interacts with BAG2, and with the E2 ubiquitin conjugating enzymes UBE2D1, UBE2D2 and UBE2D3. Interacts with the C-terminal domains of HSPA8 and HSPA1A. Detected in a ternary complex containing STUB1, HSPA1A and HSPBP1. Interacts with MKKS. Interacts with DYX1C1 and POLB. Interacts (via TPR repeats) with HSP90AA1. Interacts (when monoubiquitinated) with ATXN3. Interacts with UBE2W
By similarity. Interacts (via the U-box domain) with the UBE2V2-UBE2N heterodimer; the complex has a specific 'Lys-63'-linked polyubiquitination activity. Interacts with DNAJB6. Ref.2 Ref.10 Ref.11 Ref.13 Ref.14 Ref.15 Ref.18 Ref.23 Ref.24 Ref.31
Subcellular location: Cytoplasm Ref.2.
Tissue specificity: Highly expressed in skeletal muscle, heart, pancreas, brain and placenta. Detected in kidney, liver and lung. Ref.2
Domain: The TPR domain is essential for ubiquitination mediated by UBE2D1. Ref.17
Post-translational modification: Monoubiquitinated at Lys-2 following cell stress by UBE2W, promoting the interaction with ATXN3
By similarity. Auto-ubiquitinated; mediated by UBE2D1 and UBE2D2.
Miscellaneous: Antibodies against STUB1 are found in patients with chronic lymphocytic leukemia (CLL) and in colorectal cancer patients.
Sequence similarities: Contains 3 TPR repeats.Contains 1 U-box domain.
Research Articles on STUB1 (CHIP)
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Product Notes
The STUB1 (CHIP) stub1 (Catalog #AAA515140) is a Recombinant Protein produced from E Coli and is intended for research purposes only. The product is available for immediate purchase. The tag for this protein is His tag!!Expression System||E.coli!!Source Note||Recombinant full length human STUB1 (CHIP) was expressed in E. coli cells. AAA Biotech's STUB1 (CHIP) can be used in a range of immunoassay formats including, but not limited to, Western Blot (WB). Researchers should empirically determine the suitability of the STUB1 (CHIP) stub1 for an application not listed in the data sheet. Researchers commonly develop new applications and it is an integral, important part of the investigative research process. It is sometimes possible for the material contained within the vial of "STUB1 (CHIP), Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.Precautions
All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.Disclaimer
Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.Item has been added to Shopping Cart
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