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AB181166

Anti-ERLEC1 antibody [EPR13849]

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(10 Publications)

Rabbit Recombinant Monoclonal ERLEC1 antibody. Suitable for WB and reacts with Human samples. Cited in 10 publications.

View Alternative Names

C2orf30, XTP3TPB, UNQ1878/PRO4321, ERLEC1, Endoplasmic reticulum lectin 1, ER lectin, XTP3-transactivated gene B protein, Erlectin

3 Images
Western blot - Anti-ERLEC1 antibody [EPR13849] (AB181166)
  • WB

Supplier Data

Western blot - Anti-ERLEC1 antibody [EPR13849] (AB181166)

All lanes:

Western blot - Anti-ERLEC1 antibody [EPR13849] (ab181166) at 1/10000 dilution

All lanes:

HepG2 lysate at 20 µg

Secondary

All lanes:

Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/1000 dilution

Predicted band size: 55 kDa

false

Western blot - Anti-ERLEC1 antibody [EPR13849] (AB181166)
  • WB

Supplier Data

Western blot - Anti-ERLEC1 antibody [EPR13849] (AB181166)

All lanes:

Western blot - Anti-ERLEC1 antibody [EPR13849] (ab181166) at 1/2000 dilution

All lanes:

A375 lysate at 20 µg

Secondary

All lanes:

Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/1000 dilution

Predicted band size: 55 kDa

false

Western blot - Anti-ERLEC1 antibody [EPR13849] (AB181166)
  • WB

CiteAb

Western blot - Anti-ERLEC1 antibody [EPR13849] (AB181166)

ERLEC1 western blot using anti-ERLEC1 antibody [EPR13849] ab181166. Publication image and figure legend from Wang, T., Wang, B., et al., 2017, PLoS Pathog, PubMed 28985237.

ab181166 was used in this publication in western blot. This may not be the same as the application(s) guaranteed by Abcam. For a full list of applications guaranteed by Abcam for ab181166 please see the product overview.

EV71 targets ERAD at multiple points.(A) Diagram of the key molecules involved in ERAD. (B) RD cells were infected with EV71 (MOI = 10) for the indicated times (hpi : hours post-infection). The cells were then harvested and western blot was performed using the indicated antibodies to detect the indicated ERAD components, EV71 2C, and actin. The ERAD molecules assessed in this study were separated into four categories : substrate recognition, retrotranslocation, ubiquitination, and proteasomal degradation. Asterisks indicate the molecules that were obviously downregulated. (C) Full-size western blots for Herp, Hrd1, VIMP, and UBXD8 described in (B). (D) Quantification of Ubc6e, Herp, Hrd1, VIMP, and UBXD8 in (B). The data are presented as means ± SD of three independent experiments.

false

  • Carrier free

    Anti-ERLEC1 antibody [EPR13849] - BSA and Azide free

Key facts

Host species

Rabbit

Clonality

Monoclonal

Clone number

EPR13849

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB

applications

Immunogen

The exact immunogen used to generate this antibody is proprietary information.

Reactivity data

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Product details

Patented technology
Our RabMAb® technology is a patented hybridoma-based technology for making rabbit monoclonal antibodies. For details on our patents, please refer to RabMAb® patents.

What are the advantages of a recombinant monoclonal antibody?
This product is a recombinant monoclonal antibody, which offers several advantages including:

  • - High batch-to-batch consistency and reproducibility
  • - Improved sensitivity and specificity
  • - Long-term security of supply
  • - Animal-free batch production

For more information, read more on recombinant antibodies.

Properties and storage information

Form
Liquid
Purification technique
Affinity purification Protein A
Storage buffer
Preservative: 0.01% Sodium azide Constituents: PBS, 40% Glycerol (glycerin, glycerine), 0.05% 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
-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.

ERLEC1 also known as Endoplasmic Reticulum Lectin 1 or XTP3-B is a protein involved in maintaining protein quality control in the endoplasmic reticulum (ER). ERLEC1 has a molecular mass of about 38 kDa. The protein localizes in the ER where it participates in the calnexin/calreticulin cycle and binds to misfolded glycoproteins. Its role as a lectin allows it to recognize specific glycan structures on proteins aiding in their proper folding and maturation.
Biological function summary

ERLEC1 contributes to the ER-associated degradation (ERAD) pathway by interacting with other ER chaperones and lectin-like proteins. ERLEC1 forms part of a protein complex that identifies misfolded glycoproteins and targets them for degradation. Its function is important for relieving the ER of protein overload therefore maintaining cellular homeostasis. This role is particularly significant in tissues with high protein synthesis rates such as the liver and pancreas.

Pathways

ERLEC1 plays an important role in the unfolded protein response (UPR) by assisting in the degradation of malfunctioning proteins. It interacts with other proteins such as HRD1 and SEL1L which are part of the ERAD pathway to achieve this function. ERLEC1 contributes to maintaining cellular health by ensuring only correctly folded proteins proceed to their destination therefore preventing stress induced by protein aggregation.

ERLEC1's role in protein degradation links it to neurodegenerative diseases like Parkinson's and Alzheimer's. Misfolded protein accumulation which ERLEC1 helps prevent is a hallmark of these diseases. Disruption of ERLEC1 function may also relate to conditions like cystic fibrosis where improper protein folding and processing are involved. Protein connections to disorders include interactions with well-studied pathological proteins like alpha-synuclein and amyloid-beta highlighting its therapeutic potential.

Product protocols

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

Target data

Probable lectin that binds selectively to improperly folded lumenal proteins. May function in endoplasmic reticulum quality control and endoplasmic reticulum-associated degradation (ERAD) of both non-glycosylated proteins and glycoproteins.
See full target information ERLEC1

Publications (10)

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

Journal of biomedical science 32:11 PubMed39838427

2025

The endoplasmic reticulum degradation-enhancing α-mannosidase-like protein 3 attenuates the unfolded protein response and has pro-survival and pro-viral roles in hepatoma cells and hepatocellular carcinoma patients.

Applications

Unspecified application

Species

Unspecified reactive species

Alina-Veronica Ghionescu,Mihaela Uta,Andrei Sorop,Catalin Lazar,Petruta R Flintoaca-Alexandru,Gabriela Chiritoiu,Livia Sima,Stefana-Maria Petrescu,Simona Olimpia Dima,Norica Branza-Nichita

Nature communications 15:1440 PubMed38365914

2024

SEL1L-HRD1 interaction is required to form a functional HRD1 ERAD complex.

Applications

Unspecified application

Species

Unspecified reactive species

Liangguang Leo Lin,Huilun Helen Wang,Brent Pederson,Xiaoqiong Wei,Mauricio Torres,You Lu,Zexin Jason Li,Xiaodan Liu,Hancheng Mao,Hui Wang,Linyao Elina Zhou,Zhen Zhao,Shengyi Sun,Ling Qi

The Journal of clinical investigation 134: PubMed37943617

2024

Biallelic Cys141Tyr variant of SEL1L is associated with neurodevelopmental disorders, agammaglobulinemia, and premature death.

Applications

Unspecified application

Species

Unspecified reactive species

Denisa Weis,Liangguang L Lin,Huilun H Wang,Zexin Jason Li,Katarina Kusikova,Peter Ciznar,Hermann M Wolf,Alexander Leiss-Piller,Zhihong Wang,Xiaoqiong Wei,Serge Weis,Katarina Skalicka,Gabriela Hrckova,Lubos Danisovic,Andrea Soltysova,Tingxuan T Yang,René Günther Feichtinger,Johannes A Mayr,Ling Qi

The Journal of clinical investigation 134: PubMed37943610

2024

Hypomorphic variants of SEL1L-HRD1 ER-associated degradation are associated with neurodevelopmental disorders.

Applications

Unspecified application

Species

Unspecified reactive species

Huilun H Wang,Liangguang L Lin,Zexin J Li,Xiaoqiong Wei,Omar Askander,Gerarda Cappuccio,Mais O Hashem,Laurence Hubert,Arnold Munnich,Mashael Alqahtani,Qi Pang,Margit Burmeister,You Lu,Karine Poirier,Claude Besmond,Shengyi Sun,Nicola Brunetti-Pierri,Fowzan S Alkuraya,Ling Qi

Journal for immunotherapy of cancer 9: PubMed34341130

2021

THADA drives Golgi residency and upregulation of PD-L1 in cancer cells and provides promising target for immunotherapy.

Applications

Unspecified application

Species

Unspecified reactive species

Chushu Li,Hao Chi,Shouyan Deng,Huanbin Wang,Han Yao,Yungang Wang,Dawei Chen,Xun Guo,Jing-Yuan Fang,Fang He,Jie Xu

Molecular & cellular proteomics : MCP 20:100125 PubMed34332121

2021

Affinity Proteomics and Deglycoproteomics Uncover Novel EDEM2 Endogenous Substrates and an Integrative ERAD Network.

Applications

Unspecified application

Species

Unspecified reactive species

Cristian V A Munteanu,Gabriela N Chirițoiu,Marioara Chirițoiu,Simona Ghenea,Andrei-Jose Petrescu,Ştefana M Petrescu

Human mutation 41:1435-1446 PubMed32442352

2020

Identification of pathogenic variants of ERLEC1 in individuals with Class III malocclusion by exome sequencing.

Applications

Unspecified application

Species

Unspecified reactive species

Chunbao Rao,Biyang Guan,Dong Luo,Qin Deng,Qi Peng,Zitian Lin,Meihua Huang,Ming Qi,Baimao Zhong,Xiaomei Lu

International journal of molecular sciences 21: PubMed32423001

2020

EDEM1 Drives Misfolded Protein Degradation via ERAD and Exploits ER-Phagy as Back-Up Mechanism When ERAD Is Impaired.

Applications

Unspecified application

Species

Unspecified reactive species

Marioara Chiritoiu,Gabriela N Chiritoiu,Cristian V A Munteanu,Florin Pastrama,N Erwin Ivessa,Stefana M Petrescu

Molecular cell 71:606-620.e7 PubMed30118680

2018

Metformin Promotes Antitumor Immunity via Endoplasmic-Reticulum-Associated Degradation of PD-L1.

Applications

Unspecified application

Species

Unspecified reactive species

Jong-Ho Cha,Wen-Hao Yang,Weiya Xia,Yongkun Wei,Li-Chuan Chan,Seung-Oe Lim,Chia-Wei Li,Taewan Kim,Shih-Shin Chang,Heng-Huan Lee,Jennifer L Hsu,Hung-Ling Wang,Chu-Wei Kuo,Wei-Chao Chang,Sirwan Hadad,Colin A Purdie,Aaron M McCoy,Shirong Cai,Yizheng Tu,Jennifer K Litton,Elizabeth A Mittendorf,Stacy L Moulder,William F Symmans,Alastair M Thompson,Helen Piwnica-Worms,Chung-Hsuan Chen,Kay-Hooi Khoo,Mien-Chie Hung

PLoS pathogens 13:e1006674 PubMed28985237

2017

Enterovirus 71 protease 2Apro and 3Cpro differentially inhibit the cellular endoplasmic reticulum-associated degradation (ERAD) pathway via distinct mechanisms, and enterovirus 71 hijacks ERAD component p97 to promote its replication.

Applications

Unspecified application

Species

Unspecified reactive species

Tao Wang,Bei Wang,He Huang,Chongyang Zhang,Yuanmei Zhu,Bin Pei,Chaofei Cheng,Lei Sun,Jianwei Wang,Qi Jin,Zhendong Zhao
View all publications

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