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AB264213

Anti-STUB1/CHIP antibody

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Rabbit Polyclonal STUB1/CHIP antibody. Suitable for IP, WB and reacts with Human, Mouse samples. Immunogen corresponding to Synthetic Peptide within Human STUB1 aa 1-50.

View Alternative Names

CHIP, PP1131, STUB1, E3 ubiquitin-protein ligase CHIP, Antigen NY-CO-7, CLL-associated antigen KW-8, Carboxy terminus of Hsp70-interacting protein, RING-type E3 ubiquitin transferase CHIP, STIP1 homology and U box-containing protein 1

2 Images
Immunoprecipitation - Anti-STUB1/CHIP antibody (AB264213)
  • IP

Supplier Data

Immunoprecipitation - Anti-STUB1/CHIP antibody (AB264213)

STUB1/CHIP was immunoprecipitated from 1mg of HeLa (Human epithelial cell line from cervix adenocarcinoma) whole cell lysate with ab264213 at 3 μg/mg lysate. Western blot was performed from the immunoprecipitate using ab264213 at 0.1 μg/ml.
Lane 1 : ab264213 IP in HeLa whole cell lysate.
Lane 2 : Control IgG.

Exposure time : 30 secs.

All lanes:

Immunoprecipitation - Anti-STUB1/CHIP antibody (ab264213)

Predicted band size: 17 kDa,35 kDa

Observed band size: 17 kDa

false

Western blot - Anti-STUB1/CHIP antibody (AB264213)
  • WB

Supplier Data

Western blot - Anti-STUB1/CHIP antibody (AB264213)

Detected with chemilimuniscence with exposure time of 30 seconds.

4-20% SDS-PAGE.

All lanes:

Western blot - Anti-STUB1/CHIP antibody (ab264213) at 0.04 µg/mL

Lane 1:

HeLa whole cell lysate at 50 µg

Lane 2:

HeLa whole cell lysate at 15 µg

Lane 3:

HeLa whole cell lysate at 5 µg

Lane 4:

HEK-293T whole cell lysate at 50 µg

Lane 5:

NIH/3T3 whole cell lysate at 50 µg

Predicted band size: 35 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Mouse, Human

Applications

WB, IP

applications

Immunogen

Synthetic Peptide within Human STUB1 aa 1-50. The exact immunogen used to generate this antibody is proprietary information.

Q9UNE7

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "IP" : {"fullname" : "Immunoprecipitation", "shortname":"IP"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "IP-species-checked": "testedAndGuaranteed", "IP-species-dilution-info": "2-5 µg/mg of lysate", "IP-species-notes": "<p></p>", "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/2000 - 1/10000", "WB-species-notes": "<p></p>" }, "Mouse": { "IP-species-checked": "guaranteed", "IP-species-dilution-info": "", "IP-species-notes": "", "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/2000 - 1/10000", "WB-species-notes": "<p></p>" } } }

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 6.8 - 7.4 Preservative: 0.09% Sodium azide Constituents: Tris buffered saline, 0.1% BSA
Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
+4°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

STUB1 also known as CHIP (C-Terminal of Hsc70 Interacting Protein) is a protein with a molecular mass of approximately 35 kDa. It has ubiquitin ligase activity and functions as a co-chaperone. STUB1 interacts with chaperone proteins such as Hsp70 and Hsp90 modulating their activity. You can observe STUB1 expression in various tissues with higher levels found in the brain heart and skeletal muscle.
Biological function summary

STUB1 plays an important role in protein quality control by targeting misfolded or damaged proteins for degradation. It forms a complex with chaperone proteins Hsp70 and Hsp90 facilitating the ubiquitination process. This helps maintain cellular proteostasis. STUB1 has a critical role in preventing protein aggregation which is important in stress responses and normal cellular function.

Pathways

STUB1 has significant involvement in the protein degradation pathway and the heat shock response pathway. It works closely with proteasome-associated proteins to ensure proteostasis. In these pathways STUB1 interacts with other proteins such as Hsc70 and Hsp70 which assist in protein folding and stability under stress conditions.

STUB1 has links to neurodegenerative diseases and cancer. A dysfunction in STUB1 can lead to protein aggregation a hallmark of neurodegenerative conditions like Alzheimer's disease. In certain cancers altered STUB1 expression might affect cell survival pathways with related proteins including Hsp70 and Hsp90. Therapeutic strategies that modulate STUB1 and its interactions may provide avenues for disease intervention.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation (PubMed : 10330192, PubMed : 11146632, PubMed : 11557750, PubMed : 23990462, PubMed : 26265139). Plays a role in the maintenance of mitochondrial morphology and promotes mitophagic removal of dysfunctional mitochondria; thereby acts as a protector against apoptosis in response to cellular stress (By similarity). Negatively regulates vascular smooth muscle contraction, via degradation of the transcriptional activator MYOCD and subsequent loss of transcription of genes involved in vascular smooth muscle contraction (By similarity). Promotes survival and proliferation of cardiac smooth muscle cells via ubiquitination and degradation of FOXO1, resulting in subsequent repression of FOXO1-mediated transcription of pro-apoptotic genes (PubMed : 19483080). Ubiquitinates ICER-type isoforms of CREM and targets them for proteasomal degradation, thereby acts as a positive effector of MAPK/ERK-mediated inhibition of apoptosis in cardiomyocytes (PubMed : 20724525). Inhibits lipopolysaccharide-induced apoptosis and hypertrophy in cardiomyocytes, via ubiquitination and subsequent proteasomal degradation of NFATC3 (PubMed : 30980393). Collaborates with ATXN3 in the degradation of misfolded chaperone substrates : ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension (PubMed : 10330192, PubMed : 11146632, PubMed : 11557750, PubMed : 23990462). Ubiquitinates NOS1 in concert with Hsp70 and Hsp40 (PubMed : 15466472). Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90 (PubMed : 10330192, PubMed : 11146632, PubMed : 15466472). Ubiquitinates CHRNA3 targeting it for endoplasmic reticulum-associated degradation in cortical neurons, as part of the STUB1-VCP-UBXN2A complex (PubMed : 26265139). Ubiquitinates and promotes ESR1 proteasomal degradation in response to age-related circulating estradiol (17-beta-estradiol/E2) decline, thereby promotes neuronal apoptosis in response to ischemic reperfusion injury (By similarity). Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation (PubMed : 11557750, PubMed : 23990462). 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 (PubMed : 19713937). Mediates polyubiquitination of CYP3A4 (PubMed : 19103148). Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation (PubMed : 19567782). Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation (PubMed : 27708256). Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner (PubMed : 23973223). Catalyzes monoubiquitination of SIRT6, preventing its degradation by the proteasome (PubMed : 24043303). Likely mediates polyubiquitination and down-regulates plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity (PubMed : 28813410). Negatively regulates TGF-beta signaling by modulating the basal level of SMAD3 via ubiquitin-mediated degradation (PubMed : 24613385). Plays a role in the degradation of TP53 (PubMed : 26634371). Mediates ubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation (PubMed : 29883609). May regulate myosin assembly in striated muscles together with UBE4B and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation (PubMed : 17369820). Ubiquitinates PPARG in macrophages playing a role in M2 macrophages polarization and angiogenesis (By similarity).
See full target information STUB1

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