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AB187976

Anti-RNF31/HOIP antibody

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(4 Publications)

Rabbit Polyclonal RNF31/HOIP antibody. Suitable for IHC-P, ICC/IF and reacts with Human samples. Cited in 4 publications. Immunogen corresponding to Recombinant Fragment Protein within Human RNF31 aa 650-800.

View Alternative Names

ZIBRA, RNF31, E3 ubiquitin-protein ligase RNF31, HOIL-1-interacting protein, RING finger protein 31, RING-type E3 ubiquitin transferase RNF31, Zinc in-between-RING-finger ubiquitin-associated domain protein, HOIP

2 Images
Immunocytochemistry/ Immunofluorescence - Anti-RNF31/HOIP antibody (AB187976)
  • ICC/IF

Supplier Data

Immunocytochemistry/ Immunofluorescence - Anti-RNF31/HOIP antibody (AB187976)

Immunocytochemical analysis of PC-3 (Human prostate adenocarcinoma cell line) whole cells labeling RNF31/HOIP in the cytosol with ab187976 at 2 μg/ml.

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-RNF31/HOIP antibody (AB187976)
  • IHC-P

Supplier Data

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-RNF31/HOIP antibody (AB187976)

Immunohistochemical analysis of paraffin embedded human kidney tissue labeling RNF31/HOIP in the cytoplasm and membrane of cells in tubules with ab187976 at a 1/50 dilution.

Performed heat mediated antigen retrieval with citrate buffer pH 6 before commencing with IHC staining protocol.

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

IHC-P, ICC/IF

applications

Immunogen

Recombinant Fragment Protein within Human RNF31 aa 650-800. The exact immunogen used to generate this antibody is proprietary information.

Q96EP0

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7.2 Preservative: 0.02% Sodium azide Constituents: PBS, 40% Glycerol (glycerin, glycerine)
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.

RNF31 also known as HOIP (HOIL-1 Interacting Protein) is a large protein with a molecular weight of around 119 kDa. It is a part of the ubiquitin-proteasome system and functions mechanically as a E3 ubiquitin ligase. RNF31 forms the catalytic component of the Linear Ubiquitin Chain Assembly Complex (LUBAC). Expression of RNF31 occurs in many tissues with notable levels in immune cells and the testes. The protein features a RING-in-between-RING (RBR) motif structure that is critical for its ligase activity.
Biological function summary

RNF31/HOIP plays an important role in immune response regulation. It functions as part of the LUBAC complex alongside SHARPIN and RBCK1 (also known as HOIL-1L) which together catalyze the linear ubiquitination of substrates. These modifications regulate NF-kB signaling which is an important pathway involved in immune and inflammatory responses. RNF31's ubiquitin ligase activity adds linear ubiquitin chains to target proteins influencing their stability and function therefore impacting the immune cell function and survival.

Pathways

RNF31/HOIP integrates into the NF-kB and the apoptosis pathways. In the NF-kB pathway it acts as a regulator of cytokine production and cell survival. RNF31 achieves this through modification of NEMO (NF-kB essential modulator) an important protein in this pathway. In apoptosis regulation linear ubiquitination by RNF31 modulates the activity of proteins such as caspases preventing inappropriate cell death during immune responses. This helps to maintain balance between survival and death signals in cells allowing for proper immune function.

RNF31/HOIP has implications in inflammatory diseases and certain cancers. Dysregulation of LUBAC components including HOIP has been linked with chronic inflammatory conditions like rheumatoid arthritis where inappropriate NF-kB activation occurs. Furthermore aberrations in RNF31 activity have associations with tumorigenesis where its altered signaling pathways can lead to uncontrolled cell proliferation. In these contexts proteins such as A20 may interact with RNF31 affecting the regulation of NF-kB signaling therefore influencing disease progression.

Product protocols

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

Target data

E3 ubiquitin-protein ligase component of the LUBAC complex which conjugates linear ('Met-1'-linked) polyubiquitin chains to substrates and plays a key role in NF-kappa-B activation and regulation of inflammation (PubMed : 17006537, PubMed : 19136968, PubMed : 20005846, PubMed : 21455173, PubMed : 21455180, PubMed : 21455181, PubMed : 22863777, PubMed : 28189684, PubMed : 28481331). LUBAC conjugates linear polyubiquitin to IKBKG and RIPK1 and is involved in activation of the canonical NF-kappa-B and the JNK signaling pathways (PubMed : 17006537, PubMed : 19136968, PubMed : 20005846, PubMed : 21455173, PubMed : 21455180, PubMed : 21455181, PubMed : 22863777, PubMed : 28189684). Linear ubiquitination mediated by the LUBAC complex interferes with TNF-induced cell death and thereby prevents inflammation (PubMed : 21455173, PubMed : 28189684). LUBAC is recruited to the TNF-R1 signaling complex (TNF-RSC) following polyubiquitination of TNF-RSC components by BIRC2 and/or BIRC3 and to conjugate linear polyubiquitin to IKBKG and possibly other components contributing to the stability of the complex (PubMed : 20005846, PubMed : 27458237). The LUBAC complex is also involved in innate immunity by conjugating linear polyubiquitin chains at the surface of bacteria invading the cytosol to form the ubiquitin coat surrounding bacteria (PubMed : 28481331, PubMed : 34012115). LUBAC is not able to initiate formation of the bacterial ubiquitin coat, and can only promote formation of linear polyubiquitins on pre-existing ubiquitin (PubMed : 28481331). Recruited to the surface of bacteria by RNF213, which initiates the bacterial ubiquitin coat (PubMed : 34012115). The bacterial ubiquitin coat acts as an 'eat-me' signal for xenophagy and promotes NF-kappa-B activation (PubMed : 28481331, PubMed : 34012115). Together with OTULIN, the LUBAC complex regulates the canonical Wnt signaling during angiogenesis (PubMed : 23708998). RNF31 is required for linear ubiquitination of BCL10, thereby promoting TCR-induced NF-kappa-B activation (PubMed : 27777308). Binds polyubiquitin of different linkage types (PubMed : 23708998).
See full target information RNF31

Publications (4)

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

Oncology letters 24:394 PubMed36276481

2022

Identification and molecular analysis of RNF31 Q622H germline polymorphism.

Applications

Unspecified application

Species

Unspecified reactive species

Seshiru Nakazawa,Ryo Mamiya,Reika Kawabata-Iwakawa,Daisuke Oikawa,Kyoichi Kaira,Fuminori Tokunaga,Sumihito Nobusawa,Yusuke Sato,Atsushi Sasaki,Toshiki Yajima,Ken Shirabe

Molecular cell 82:2415-2426.e5 PubMed35477005

2022

Liquid phase separation of NEMO induced by polyubiquitin chains activates NF-κB.

Applications

Unspecified application

Species

Unspecified reactive species

Mingjian Du,Chee-Kwee Ea,Yan Fang,Zhijian J Chen

Bioengineered 12:3188-3200 PubMed34238116

2021

Identification of key genes involved in the recurrence of glioblastoma multiforme using weighted gene co-expression network analysis and differential expression analysis.

Applications

Unspecified application

Species

Unspecified reactive species

Peng Ren,JingYa Wang,Lei Li,XiaoWan Lin,GuangHan Wu,JiaYi Chen,ZhiRui Zeng,HongMei Zhang

Journal of neuropathology and experimental neurology 79:256-265 PubMed31951008

2020

Linear Polyubiquitin Chain Modification of TDP-43-Positive Neuronal Cytoplasmic Inclusions in Amyotrophic Lateral Sclerosis.

Applications

Unspecified application

Species

Unspecified reactive species

Yoshiaki Nakayama,Kazumi Tsuji,Takashi Ayaki,Megumi Mori,Fuminori Tokunaga,Hidefumi Ito
View all publications

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