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
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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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
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)
Amy M Palubinsky et al.
Antioxidants & redox signaling, 23(6), 535-549 (2015-01-21)
Determine the mechanism by which C-terminus of HSC70-interacting protein (CHIP) induction alters neuronal survival under conditions of mitochondrial stress induced by oxygen glucose deprivation. We report that animals deficient in the E3 ubiquitin ligase, CHIP, have high baseline levels of
Xiaodong Ding et al.
PloS one, 4(6), e5949-e5949 (2009-06-19)
Dominantly inherited mutations in the leucine-rich repeat kinase 2 gene (LRRK2) are the most common cause of familial Parkinson's disease (PD) and have also been identified in individuals with sporadic PD. Although the exact cellular function of LRRK2 remains unknown
Rick F Nelson et al.
The Journal of biological chemistry, 281(29), 20242-20251 (2006-05-10)
In SCF (Skp1/Cullin/F-box protein) ubiquitin ligases, substrate specificity is conferred by a diverse array of F-box proteins. Only in fully assembled SCF complexes, it is believed, can substrates bound to F-box proteins become ubiquitinated. Here we show that Fbx2, a
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