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AB183102

Anti-RNF126 antibody

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(5 Publications)

Rabbit Polyclonal RNF126 antibody. Suitable for WB and reacts with Human samples. Cited in 5 publications. Immunogen corresponding to Synthetic Peptide within Human E3 ubiquitin-protein ligase RNF126 aa 100-150.

View Alternative Names

E3 ubiquitin-protein ligase RNF126, RING finger protein 126, RNF126

2 Images
Western blot - Anti-RNF126 antibody (AB183102)
  • WB

Supplier Data

Western blot - Anti-RNF126 antibody (AB183102)

10%SDS-PAGE

All lanes:

Western blot - Anti-RNF126 antibody (ab183102) at 1/350 dilution

Lane 1:

Jurkat cell lysate at 40 µg

Lane 2:

K562 cell lysate at 40 µg

Secondary

All lanes:

Goat anti Rabbit IgG - H&L (HRP) at 1/10000 dilution

Predicted band size: 36 kDa

false

Exposure time: 20s

Western blot - Anti-RNF126 antibody (AB183102)
  • WB

Supplier Data

Western blot - Anti-RNF126 antibody (AB183102)

Immunohistochemical analysis of paraffin embedded Human thyroid cancer tissue labeling RNF126 with ab183102 at 1/20 dilution. Image on the right is treated with the synthetic peptide.

All lanes:

Western blot - Anti-RNF126 antibody (ab183102)

Predicted band size: 36 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB

applications

Immunogen

Synthetic Peptide within Human E3 ubiquitin-protein ligase RNF126 aa 100-150. The exact immunogen used to generate this antibody is proprietary information.

Q9BV68

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Species", "Dilution Info", "Notes"], "tabs": { "all-applications": {"fullname" : "All Applications", "shortname": "All Applications"}, "WB" : {"fullname" : "Western blot", "shortname":"WB"} }, "product-promise": { "all": "all", "testedAndGuaranteed": "tested", "guaranteed": "expected", "predicted": "predicted", "notRecommended": "not-recommended" } }, "values": { "Human": { "WB-species-checked": "testedAndGuaranteed", "WB-species-dilution-info": "1/350 - 1/2000", "WB-species-notes": "<p></p>" }, "Mouse": { "WB-species-checked": "predicted", "WB-species-dilution-info": "", "WB-species-notes": "" }, "Rat": { "WB-species-checked": "predicted", "WB-species-dilution-info": "", "WB-species-notes": "" } } }

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7.4 Preservative: 0.05% Sodium azide Constituents: 50% Glycerol (glycerin, glycerine), 49% PBS
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.

RNF126 also known as RING finger protein 126 functions as an E3 ubiquitin ligase. It possesses a molecular mass of approximately 30 kDa and is expressed in various tissues including the brain heart and kidneys. The protein contains a RING finger domain which helps mediate substrate ubiquitination. This post-translational modification marks proteins for degradation by the proteasome regulating protein turnover and function in cells.
Biological function summary

RNF126 plays significant roles in protein homeostasis and cellular stress responses. It interacts with the p97/VCP complex facilitating the extraction of polyubiquitinated proteins from cellular structures for subsequent degradation. Additionally RNF126 regulates the stability of various substrates involved in cellular processes such as DNA repair and the cell cycle. This regulation ensures proper cell function and adaptation to varying environmental conditions.

Pathways

RNF126 participates in the ubiquitin-proteasome system which is critical for the degradation of misfolded or damaged proteins. It also takes part in pathways related to DNA damage response where its function overlaps with proteins like BRCA1 and RAD51. The protein's involvement in these pathways highlights its importance in maintaining genomic stability and proper cellular function. RNF126 ensures proteins are appropriately degraded when no longer needed or damaged maintaining cellular integrity.

RNF126 has been linked to cancer and neurodegenerative diseases. In cancer RNF126 is associated with tumor progression and resistance to therapy potentially through its interaction with proteins such as HER2 and p53. In neurodegenerative diseases impairments in RNF126 function could impact protein clearance contributing to the accumulation of toxic protein aggregates. These relationships suggest that RNF126 might serve as a target for therapeutic intervention in these conditions.

Product protocols

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

Target data

E3 ubiquitin-protein ligase that mediates ubiquitination oF target proteins (PubMed : 23277564, PubMed : 24275455, PubMed : 24981174, PubMed : 36563124). Depending on the associated E2 ligase, mediates 'Lys-27'-, 'Lys-29'-, 'Lys-48'- and/or 'Lys-63'-linked polyubiquitination of substrates (PubMed : 36563124). Part of a BAG6-dependent quality control process ensuring that proteins of the secretory pathway that are mislocalized to the cytosol are degraded by the proteasome. Probably acts by providing the ubiquitin ligase activity associated with the BAG6 complex and be responsible for ubiquitination of the hydrophobic mislocalized proteins and their targeting to the proteasome (PubMed : 24981174, PubMed : 29042515). May also play a role in the endosomal recycling of IGF2R, the cation-independent mannose-6-phosphate receptor (PubMed : 24275455). May play a role in the endosomal sorting and degradation of several membrane receptors including EGFR, FLT3, MET and CXCR4, by mediating their ubiquitination (PubMed : 23418353). By ubiquitinating CDKN1A/p21 and targeting it for degradation, may also promote cell proliferation (PubMed : 23026136). May monoubiquitinate AICDA (PubMed : 23277564). Acts as a regulator of DNA repair by mediating 'Lys-27'- and 'Lys-29'-linked polyubiquitination of MRE11, thereby promoting the exonuclease activity of MRE11 (PubMed : 36563124).
See full target information E3 ubiquitin-protein ligase RNF126

Publications (5)

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

iScience 26:106652 PubMed37182096

2023

Protein quality control machinery supports primary ciliogenesis by eliminating GDP-bound Rab8-family GTPases.

Applications

Unspecified application

Species

Unspecified reactive species

Toshiki Takahashi,Jun Shirai,Miyo Matsuda,Sae Nakanaga,Shin Matsushita,Kei Wakita,Mizuki Hayashishita,Rigel Suzuki,Aya Noguchi,Naoto Yokota,Hiroyuki Kawahara

ACS chemical biology 16:2280-2296 PubMed34553588

2021

Deorphanizing Caspase-3 and Caspase-9 Substrates In and Out of Apoptosis with Deep Substrate Profiling.

Applications

Unspecified application

Species

Unspecified reactive species

Luam E Araya,Ishankumar V Soni,Jeanne A Hardy,Olivier Julien

Cell death & disease 12:239 PubMed33664240

2021

E3 ubiquitin ligase RNF126 affects bladder cancer progression through regulation of PTEN stability.

Applications

Unspecified application

Species

Unspecified reactive species

Huimin Xu,Lingao Ju,Yaoyi Xiong,Mengxue Yu,Fenfang Zhou,Kaiyu Qian,Gang Wang,Yu Xiao,Xinghuan Wang

Anticancer research 40:1367-1374 PubMed32132033

2020

RNF126 as a Marker of Prognosis and Proliferation of Gastric Cancer.

Applications

Unspecified application

Species

Unspecified reactive species

Kazuhiro Migita,Sohei Matsumoto,Kohei Wakatsuki,Tomohiro Kunishige,Hiroshi Nakade,Shintaro Miyao,Masayuki Sho

Clinical cancer research : an official journal of 24:1629-1643 PubMed29326282

2018

RNF126 as a Biomarker of a Poor Prognosis in Invasive Breast Cancer and CHEK1 Inhibitor Efficacy in Breast Cancer Cells.

Applications

Unspecified application

Species

Unspecified reactive species

Xiaosong Yang,You Pan,Zhaojun Qiu,Zhanwen Du,Yao Zhang,Pengyan Fa,Shashank Gorityala,Shanhuai Ma,Shunqiang Li,Ceshi Chen,Hongbing Wang,Yan Xu,Chunhong Yan,Keri Ruth,Zhefu Ma,Junran Zhang
View all publications

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