PC711
Anti-CHIP Rabbit pAb
liquid, Calbiochem®
Synonym(s):
Anti-Carboxyl Terminus of Hcs70-Interacting Protein
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.43
Recommended Products
biological source
rabbit
Quality Level
antibody form
serum
antibody product type
primary antibodies
clone
polyclonal
form
liquid
contains
≤0.1% Sodium azide as preservative
species reactivity
Drosophila, hamster, rat, human, monkey, mouse
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
avoid repeated freeze/thaw cycles
isotype
IgG
shipped in
wet ice
storage temp.
−20°C
target post-translational modification
unmodified
Related Categories
General description
Rabbit polyclonal antibody supplied as undiluted serum. Recognizes the ~35 kDa CHIP protein.
Recognizes the ~35 kDa CHIP protein. May also detect bands at ~43, ~51, and ~70 kDa corresponding to the mono-ubiquitinated, di-ubiquitinated, and dimeric forms of CHIP, respectively.
This Anti-CHIP Rabbit pAb is validated for use in Immunoblotting for the detection of CHIP.
Immunogen
a recombinant protein consisting of full-length human CHIP fused to a His•Tag sequence
Application
Immunoblotting (1:200-1:1000)
Immunofluorescence (1:250)
Immunoprecipitation (1:20)
Immunofluorescence (1:250)
Immunoprecipitation (1:20)
Warning
Toxicity: Standard Handling (A)
Physical form
Undiluted serum.
Reconstitution
Following initial thaw, aliquot and freeze (-20°C).
Analysis Note
Positive Control
COS-7 cells
COS-7 cells
Other Notes
May also detect bands at 43, 51, and 70 kDa, wich correspond to the mono-ubiquitinated, di-ubiquitinated, and dimeric forms of CHIP, respectively. Antibody should be titrated for optimal results in individual systems.
Xu, W., et al. 2002. Proc. Natl. Acad. Sci. USA99, 12847.
Demand, J., et al. 2001. Curr. Biol.11, 1569.
Connell, P., et al. 2001. Nat. Cell Biol.3, 93.
Jiang. J., et al. 2001. J. Biol. Chem. 276, 42938.
Meacham, G.C., et al. 2001. Nat. Cell. Biol.3, 100.
Ballinger, C.A., et al. 1999. Mol. Cell. Biol.19, 4535.
Demand, J., et al. 2001. Curr. Biol.11, 1569.
Connell, P., et al. 2001. Nat. Cell Biol.3, 93.
Jiang. J., et al. 2001. J. Biol. Chem. 276, 42938.
Meacham, G.C., et al. 2001. Nat. Cell. Biol.3, 100.
Ballinger, C.A., et al. 1999. Mol. Cell. Biol.19, 4535.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
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Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Britney N Lizama et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 38(31), 6825-6840 (2018-06-24)
The C terminus of HSC70-interacting protein (CHIP, STUB1) is a ubiquitously expressed cytosolic E3-ubiquitin ligase. CHIP-deficient mice exhibit cardiovascular stress and motor dysfunction before premature death. This phenotype is more consistent with animal models in which master regulators of autophagy
Rudolf A Kley et al.
Brain : a journal of neurology, 135(Pt 9), 2642-2660 (2012-09-11)
Mutations in FLNC cause two distinct types of myopathy. Disease associated with mutations in filamin C rod domain leading to expression of a toxic protein presents with progressive proximal muscle weakness and shows focal destructive lesions of polymorphous aggregates containing
Jeannette N Stankowski et al.
Antioxidants & redox signaling, 14(10), 1787-1801 (2010-08-04)
The decision to remove or refold oxidized, denatured, or misfolded proteins by heat shock protein 70 and its binding partners is critical to determine cell fate under pathophysiological conditions. Overexpression of the ubiquitin ligase C-terminus of HSC70 interacting protein (CHIP)
Xinjia Wang et al.
Molecular endocrinology (Baltimore, Md.), 19(6), 1474-1482 (2005-03-12)
The ubiquitin/proteasome-dependent protein degradation pathway (UPP) is responsible for the accelerated down-regulation of glucocorticoid receptor (GR) levels in cells subjected to chronic glucocorticoid exposure. Whereas hormone-dependent down-regulation of GR operates in most cells, the receptor is not down-regulated after long-term
Nadja Kettern et al.
PloS one, 6(1), e16398-e16398 (2011-02-02)
The maturation of mouse macrophages and dendritic cells involves the transient deposition of ubiquitylated proteins in the form of dendritic cell aggresome-like induced structures (DALIS). Transient DALIS formation was used here as a paradigm to study how mammalian cells influence
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