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AB122

Anti-Ubiquitin antibody [1B4-UB]

4

(1 Review)

|

(5 Publications)

Mouse Monoclonal UBB antibody. Suitable for IHC-P and reacts with Human samples. Cited in 5 publications. Immunogen corresponding to Recombinant Protein within Cow UBB.

View Alternative Names

Polyubiquitin-B, UBB

1 Images
Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Ubiquitin antibody [1B4-UB] (AB122)
  • IHC-P

Unknown

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Ubiquitin antibody [1B4-UB] (AB122)

ab122 staining Ubiquitin in the tissue of human hypophysis by Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections).

Key facts

Host species

Mouse

Clonality

Monoclonal

Clone number

1B4-UB

Isotype

IgG1

Light chain type

unknown

Carrier free

No

Reacts with

Human

Applications

IHC-P

applications

Immunogen

Recombinant Protein within Cow UBB. The exact immunogen used to generate this antibody is proprietary information.

P0CG53

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "IHCP" : {"fullname" : "Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections)", "shortname":"IHC-P"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "IHCP-species-checked": "testedAndGuaranteed", "IHCP-species-dilution-info": "1/500 - 1/1000", "IHCP-species-notes": "<p></p>" } } }

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein G
Purification notes
Purified IgG prepared by affinity chromatography on Protein G from tissue culture supernatant
Storage buffer
Preservative: 0.1% Sodium azide
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
-20°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.

Ubiquitin is a small regulatory protein found in almost all tissues of eukaryotic organisms. It has a molecular weight of approximately 8.6 kilodaltons. It functions mechanically by attaching to proteins through a process called ubiquitination which involves the formation of an isopeptide bond. Ubiquitin molecules can form polyubiquitin chains through different lysine residues such as K48 and K63 that determine their function. These chains label substrate proteins for various fates including degradation. Ubiquitin is expressed ubiquitously in cells reflecting its essential role in maintaining protein homeostasis.
Biological function summary

The ubiquitin system plays a critical role in regulating protein turnover and quality control within cells. It is part of a larger complex known as the ubiquitin-proteasome system (UPS) which is responsible for degrading proteins that need to be turned over. This process is essential for cell cycle control response to oxidative stress and DNA repair. Ubiquitin's role in tagging proteins for degradation or signaling allows cells to respond quickly to changes in their environment and maintain balance.

Pathways

Ubiquitin functions in several important biological pathways including the Wnt and NF-kB pathways. In the Wnt signaling pathway ubiquitination modulates the stability of key components thereby affecting the pathway's overall activity. In the NF-kB signaling pathway ubiquitin labels inhibitor proteins for degradation which releases and activates NF-kB. These pathways highlight ubiquitin's interaction with proteins such as beta-catenin in Wnt and IkB in NF-kB illustrating how it regulates diverse cellular processes.

The dysfunction of the ubiquitin system is linked to neurodegenerative diseases and cancers. Ubiquitin-related defects in protein degradation can lead to the buildup of unwanted proteins contributing to conditions like Parkinson's disease. Connections with cancer are evident as ubiquitin controls cell cycle proteins and aberrant ubiquitination may drive tumor growth and progression. The protein p53 known to be controlled by ubiquitination plays a significant role in cancer related mechanisms when dysregulated. Understanding and targeting ubiquitin-related pathways may provide new therapeutic opportunities for treating these conditions.

Product protocols

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

Target data

Ubiquitin. Exists either covalently attached to another protein, or free (unanchored) (By similarity). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains) (PubMed : 26116755). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked : Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B (By similarity). Linear polymer chains formed via attachment by the initiator Met lead to cell signaling (By similarity). Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed (By similarity). When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
See full target information UBB

Publications (5)

Recent publications for all applications. Explore the full list and refine your search

Cell reports 41:111800 PubMed36516753

2022

Hypoxia induces transgenerational epigenetic inheritance of small RNAs.

Applications

Unspecified application

Species

Unspecified reactive species

Simon Yuan Wang,Kathleen Kim,Zach Klapholz O'Brown,Aileen Levan,Anne Elizabeth Dodson,Scott G Kennedy,Chaim Chernoff,Eric Lieberman Greer

Science advances 8:eabh1824 PubMed35363524

2022

Deubiquitinase CYLD acts as a negative regulator of dopamine neuron survival in Parkinson's disease.

Applications

Unspecified application

Species

Unspecified reactive species

Sheila K Pirooznia,Hu Wang,Nikhil Panicker,Manoj Kumar,Stewart Neifert,Mohamad Aasif Dar,Evan Lau,Bong Gu Kang,Javier Redding-Ochoa,Juan C Troncoso,Valina L Dawson,Ted M Dawson

Molecular neurodegeneration 15:17 PubMed32138754

2020

PARIS induced defects in mitochondrial biogenesis drive dopamine neuron loss under conditions of parkin or PINK1 deficiency.

Applications

Unspecified application

Species

Unspecified reactive species

Sheila K Pirooznia,Changqing Yuan,Mohammed Repon Khan,Senthilkumar S Karuppagounder,Luan Wang,Yulan Xiong,Sung Ung Kang,Yunjong Lee,Valina L Dawson,Ted M Dawson

PloS one 8:e72687 PubMed24009698

2013

Food vacuole associated enolase in plasmodium undergoes multiple post-translational modifications: evidence for atypical ubiquitination.

Applications

Unspecified application

Species

Unspecified reactive species

Saudamini Shevade,Nitin Jindal,Sneha Dutta,Gotam K Jarori

The Journal of biological chemistry 286:22227-34 PubMed21540183

2011

Sirtuin 1 (SIRT1) protein degradation in response to persistent c-Jun N-terminal kinase 1 (JNK1) activation contributes to hepatic steatosis in obesity.

Applications

WB

Species

Human

Zhanguo Gao,Jin Zhang,Indu Kheterpal,Norm Kennedy,Roger J Davis,Jianping Ye
View all publications

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