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Key Documents

AB10000

Sigma-Aldrich

Anti-CHIP/STUB1 Antibody

Chemicon®, from goat

Synonym(s):

CHIP, STUB1

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

goat

Quality Level

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

purified by

affinity chromatography

species reactivity

human, chimpanzee

manufacturer/tradename

Chemicon®

technique(s)

ELISA: suitable
western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

dry ice

target post-translational modification

unmodified

Gene Information

human ... STUB1(10273)

General description

U box domain E3 ubiquitin ligase. CHIP E3 controls both the association of Hsp70/Hsp90 chaperones with ErbB2 and the down-regulation of ErbB2 induced by inhibitors of Hsp90. CHIP-induced degradation was observed for mutant and wild-type p53, which transiently associate with molecular chaperones Hsc70 and Hsp90 and can be diverted onto a degradation pathway through this association. Also, CHIP can interact with the Smad1/Smad4 proteins and block BMP signal transduction through the ubiquitin-mediated degradation of Smad proteins.

Immunogen

Peptide with sequence DAFISENGWVEDY, from the C-terminus of the protein sequence according to NP_005852.

Application

This Anti-CHIP/STUB1 Antibody is validated for use in ELISA, WB for the detection of CHIP/STUB1.

Physical form

Tris saline, 0.02% sodium azide, pH7.3 with 0.5% bovine serum albumin.

Analysis Note

Control
Positive Control: Highly expressed in brain, heart, skelatal muscle, pancreas and placenta. Weak expression in kidney, liver and lung.

Legal Information

CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany

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Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificates of Analysis (COA)

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Adam J Kanack et al.
Chembiochem : a European journal of chemical biology, 23(6), e202100633-e202100633 (2022-01-22)
The ubiquitin ligase C-terminus of Hsc70 interacting protein (CHIP) is an important regulator of proteostasis. Despite playing an important role in maintaining proteostasis, little progress has been made in developing small molecules that regulate ubiquitin transfer by CHIP. Here we
Monte S Willis et al.
Cell biochemistry and function, 31(8), 724-735 (2013-04-05)
The carboxyl terminus of Hsp70-interacting protein (CHIP) is a ubiquitin ligase/cochaperone critical for the maintenance of cardiac function. Mice lacking CHIP (CHIP-/-) suffer decreased survival, enhanced myocardial injury and increased arrhythmias compared with wild-type controls following challenge with cardiac ischaemia
J Jiang et al.
The Journal of biological chemistry, 276(46), 42938-42944 (2001-09-15)
Proper folding of proteins (either newly synthesized or damaged in response to a stressful event) occurs in a highly regulated fashion. Cytosolic chaperones such as Hsc/Hsp70 are assisted by cofactors that modulate the folding machinery in a positive or negative

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