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S1073

Sigma-Aldrich

Anti-STUB1/CHIP antibody, mouse monoclonal

clone ST21.55, purified from hybridoma cell culture

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Synonym(s):
Anti-C terminus of HSC70-interacting protein (CHIP), Anti-HSPABP2, Anti-Heat shock protein A binding protein 2 (c-terminal), Anti-NY-CO-7, Anti-SDCCAG7, Anti-STIP1 homologous and box-containing protein 1 (STUB1), Anti-Serologically defined colon cancer antigen 7, Anti-UBOX1
MDL number:
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

purified from hybridoma cell culture

antibody product type

primary antibodies

clone

ST21.55, monoclonal

form

buffered aqueous solution

mol wt

antigen ~35 kDa

species reactivity

rat, human, bovine

concentration

~1.0 mg/mL

technique(s)

indirect ELISA: suitable
western blot: 2.5-5 μg/mL using HeLa total cell extract.

isotype

IgG2b

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

bovine ... STUB1(504565)
human ... STUB1(10273)
mouse ... Stub1(56424)
rat ... Stub1(287155)

General description

Monoclonal Anti-STUB1/CHIP (mouse IgG2b isotype) is derived from the hybridoma ST21.55 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a synthetic peptide corresponding to amino acids 30-45 of human STUB1/CHIP. STUB1/CHIP (carboxyl terminus of Hsc70-interacting protein) consists of three functional domains: a tetratricopeptide repeat (TRP) at the amino terminus, a U- box domain at the C-terminus, and a highly charged region separating the two.
STUB1 (STIP1 homology and U-box containing protein 1) or CHIP (carboxyl terminus of Hsc70- interacting protein) is an E3 ubiquitin ligase, (2) that is located on human chromosome 16p13.3.

Immunogen

synthetic peptide corresponding to amino acids 30-45 of human STUB1/CHIP.

Application

Anti-STUB1/CHIP antibody, mouse monoclonal has been used in immunoblotting and enzyme-linked immunosorbent assay (ELISA).

Biochem/physiol Actions

In lens epithelial cells, knocking down CHIP (carboxyl terminus of Hsc70- interacting protein) decreased the reaction of heat shock and potential of protein quality control. It plays a major role in neurodegeneration and also controls autophagic flux. It can deactivate NF-κB signaling and damage the capability of migration and invasion in gastric cancer cells.
STUB1/CHIP (carboxyl terminus of Hsc70-interacting protein) is such a cofactor, which interacts, among others, with Hsc70 and acts as a U-box-dependent E3 ubiquitin ligase. STUB1/CHIP can also act as a direct chaperone of p53, both under physiological and stress conditions.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

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CHIP Knockdown Reduced Heat Shock Response and Protein Quality Control Capacity in Lens Epithelial Cells
Zhang W, et al.
Current Molecular Medicine, 15(7), 652-662 (2015)
Regulation of autophagic flux by CHIP
Guo D, et al.
Neuroscience Bulletin, 31(4), 469-479 (2015)
CHIP (carboxyl terminus of Hsc70-interacting protein) promotes basal and geldanamycin-induced degradation of estrogen receptor-alpha
Fan M, et al.
Molecular Endocrinology, 19(12), 2901-2914 (2005)
Ataxia and hypogonadism caused by the loss of ubiquitin ligase activity of the U box protein CHIP
Shi CH, et al.
Human Molecular Genetics, 23(4), 1013-1024 (2013)
Izumi Horikawa et al.
Nature communications, 5, 4706-4706 (2014-08-22)
Δ133p53α, a p53 isoform that can inhibit full-length p53, is downregulated at replicative senescence in a manner independent of mRNA regulation and proteasome-mediated degradation. Here we demonstrate that, unlike full-length p53, Δ133p53α is degraded by autophagy during replicative senescence. Pharmacological

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