Anti-STUB1/CHIP antibody (ab2917)
Key features and details
- Rabbit polyclonal to STUB1/CHIP
- Suitable for: WB
- Reacts with: Mouse, Human
- Isotype: IgG
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Overview
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Product name
Anti-STUB1/CHIP antibody
See all STUB1/CHIP primary antibodies -
Description
Rabbit polyclonal to STUB1/CHIP -
Host species
Rabbit -
Specificity
Detects human carboxyl terminus of hsc70-interacting protein (CHIP).Detects a band of approximately 35 kDa representing CHIP from COS-1 cells overexpressing the human gene including a non-specific band at 80kDa . A customer reported that in mouse cerebrum the antibody detects a band of 35kDa as well as two small mon-specific at 44 and 70 kDa. -
Tested applications
Suitable for: WBmore details -
Species reactivity
Reacts with: Mouse, Human
Predicted to work with: Chicken -
Immunogen
Synthetic peptide corresponding to Human STUB1/CHIP aa 218-232.
Sequence:VDEKRKKRDIPDYLC
(Peptide available asab4934) -
Positive control
- WB: mouse brain, MCF-7 cells, transfected COS-1 cells
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General notes
The Life Science industry has been in the grips of a reproducibility crisis for a number of years. Abcam is leading the way in addressing this with our range of recombinant monoclonal antibodies and knockout edited cell lines for gold-standard validation. Please check that this product meets your needs before purchasing.
If you have any questions, special requirements or concerns, please send us an inquiry and/or contact our Support team ahead of purchase. Recommended alternatives for this product can be found below, along with publications, customer reviews and Q&As
Properties
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Form
Liquid -
Storage instructions
Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle. -
Storage buffer
Preservative: 0.05% Sodium azide
Constituents: 0.1% BSA, 99% PBS -
Concentration information loading...
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Purity
Immunogen affinity purified -
Primary antibody notes
A recently identified protein, termed carboxyl terminus of hsc70-interacting protein (CHIP), has been shown to interact both with the constitutive form of hsc70 and the stress inducible form, hsp70. This novel 35 kDa cytoplasmic protein has been shown to be highly expressed in striated muscle in vivo. Additional studies have shown that this protein is expressed over a broad range of cultured tissues. Through immunoprecipitation experiments, CHIP has been shown to directly bind to the carboxyl terminus of hsc70 and hsp70 where it decreases ATPase activity and reduces overall chaperone efficiency. CHIP has also been identified as an important protein in the ubiquitin-proteasome system. CHIP contains a U-box domain and acts as an E3 ubiquitin-ligase in conjunction with hsc70 and hsp90. -
Clonality
Polyclonal -
Isotype
IgG -
Research areas
Associated products
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Compatible Secondaries
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Isotype control
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Positive Controls
Applications
The Abpromise guarantee
Our Abpromise guarantee covers the use of ab2917 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
Application | Abreviews | Notes |
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WB | (2) |
Use at an assay dependent concentration. Predicted molecular weight: 35 kDa.
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Notes |
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WB
Use at an assay dependent concentration. Predicted molecular weight: 35 kDa. |
Target
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Function
E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. 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. -
Tissue specificity
Highly expressed in skeletal muscle, heart, pancreas, brain and placenta. Detected in kidney, liver and lung. -
Pathway
Protein modification; protein ubiquitination. -
Sequence similarities
Contains 3 TPR repeats.
Contains 1 U-box domain. -
Domain
The TPR domain is essential for ubiquitination mediated by UBE2D1. -
Post-translational
modificationsPhosphorylated upon DNA damage, probably by ATM or ATR.
Auto-ubiquitinated; mediated by UBE2D1 and UBE2D2. -
Cellular localization
Cytoplasm. - Information by UniProt
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Database links
- Entrez Gene: 426918 Chicken
- Entrez Gene: 10273 Human
- Entrez Gene: 56424 Mouse
- Omim: 607207 Human
- SwissProt: Q5ZHY5 Chicken
- SwissProt: Q9UNE7 Human
- SwissProt: Q9WUD1 Mouse
- Unigene: 592081 Human
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Alternative names
- Antigen NY CO 7 antibody
- Antigen NY-CO-7 antibody
- C terminus of Hsp70-interacting protein antibody
see all
Images
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Western blot detection of transfected COS-1 cells expressing STUB1/CHIP using ab2917.
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Western blot analysis of STUB1/CHIP was performed by loading 20ug of total protein extracted from the left hemisphere (Left lane) or right hemisphere (right lane) of a normal C57BL/6 mouse brain per well on an SDS-PAGE gel. Proteins were transferred to a membrane, blocked with 5% non-fat dry milkand probed with a STUB1/CHIP polyclonal antibody (ab2915) at a dilution of 1:1000, followed by a HRP-conjugated goat anti-rabbit IgG secondary antibody. Detection was performed using a chemiluminescent substrate.
Protocols
Datasheets and documents
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SDS download
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Datasheet download
References (12)
ab2917 has been referenced in 12 publications.
- Von Schulze AT et al. Heat Treatment Improves Hepatic Mitochondrial Respiratory Efficiency via Mitochondrial Remodeling. Function (Oxf) 2:zqab001 (2021). PubMed: 33629069
- Mol MO et al. Clinical and pathologic phenotype of a large family with heterozygous STUB1 mutation. Neurol Genet 6:e417 (2020). PubMed: 32337344
- Blasco-Benito S et al. Therapeutic targeting of HER2-CB2R heteromers in HER2-positive breast cancer. Proc Natl Acad Sci U S A 116:3863-3872 (2019). PubMed: 30733293
- Cvjetkovic A et al. Detailed Analysis of Protein Topology of Extracellular Vesicles-Evidence of Unconventional Membrane Protein Orientation. Sci Rep 6:36338 (2016). WB . PubMed: 27821849
- Shi C et al. The Inhibition of Heat Shock Protein 90 Facilitates the Degradation of Poly-Alanine Expanded Poly (A) Binding Protein Nuclear 1 via the Carboxyl Terminus of Heat Shock Protein 70-Interacting Protein. PLoS One 10:e0138936 (2015). Mouse . PubMed: 26414348