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AB64830

Anti-RED1 antibody

4

(1 Review)

|

(7 Publications)

Rabbit Polyclonal RED1 antibody. Suitable for ELISA, WB, IHC-P, ICC/IF and reacts with Mouse, Human samples. Cited in 7 publications. Immunogen corresponding to Synthetic Peptide within Human ADARB1.

View Alternative Names

ADAR2, DRADA2, RED1, ADARB1, Double-stranded RNA-specific editase 1, RNA-editing deaminase 1, RNA-editing enzyme 1, dsRNA adenosine deaminase

2 Images
Immunocytochemistry/ Immunofluorescence - Anti-RED1 antibody (AB64830)
  • ICC/IF

Unknown

Immunocytochemistry/ Immunofluorescence - Anti-RED1 antibody (AB64830)

ICC/IF image of ab64830 stained HeLa cells. The cells were 4% PFA fixed (10 min) and then incubated in 1%BSA / 10% normal goat serum / 0.3M glycine in 0.1% PBS-Tween for 1h to permeabilise the cells and block non-specific protein-protein interactions. The cells were then incubated with the antibody (ab64830, 1µg/ml) overnight at +4°C. The secondary antibody (green) was Alexa Fluor® 488 goat anti-rabbit IgG (H+L) used at a 1/1000 dilution for 1h. Alexa Fluor® 594 WGA was used to label plasma membranes (red) at a 1/200 dilution for 1h. DAPI was used to stain the cell nuclei (blue) at a concentration of 1.43µM.

Western blot - Anti-RED1 antibody (AB64830)
  • WB

Unknown

Western blot - Anti-RED1 antibody (AB64830)

All lanes:

Western blot - Anti-RED1 antibody (ab64830) at 1/500 dilution

Lane 1:

HepG2 cell extract (5-30 µg total protein)

Lane 2:

HepG2 cell extract (5-30 µg total protein) ) with 5-10 µg of the immunising peptide

Predicted band size: 81 kDa

Observed band size: 81 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human, Mouse

Applications

ICC/IF, WB, IHC-P, ELISA

applications

Immunogen

Synthetic Peptide within Human ADARB1. The exact immunogen used to generate this antibody is proprietary information.

P78563

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7.4 Preservative: 0.02% Sodium azide Constituents: PBS, 50% Glycerol (glycerin, glycerine), 0.87% Sodium chloride
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Storage information
Stable for 12 months at -20°C

Supplementary information

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

RED1 also known as ADARB1 is a protein involved in RNA editing. It weighs approximately 73 kDa. RED1 mainly expresses itself in the central nervous system but also appears in other tissues. This protein modifies RNA molecules by catalyzing the conversion of adenosine to inosine which can alter the coding potential and metabolism of the RNA it acts upon.
Biological function summary

The protein RED1 functions within RNA editing complexes. It co-operates with other proteins like ADAR1 to carry out its editing role. In particular RED1 affects the regulation of gene expression influencing neuronal function and development in the brain. Through its editing capabilities the protein contributes to the diversity and stability of RNA transcripts.

Pathways

RED1 plays a role in neurotransmission and neurodevelopment pathways. It interacts with other editing proteins in the ADAR family to ensure proper RNA sequence modifications critical for brain function. The editing process that RED1 participates in impacts synaptic transmission important for neuronal communication and neural network formation.

The protein RED1 is associated with neurological disorders. Changes in RED1 expression or mutations can link to conditions such as epilepsy and schizophrenia. Aberrations in RNA editing performed by RED1 might lead to the dysfunction of proteins involved in neuronal signaling. It also connects with proteins like ADAR2 influencing the pathological progress of these conditions.

Product protocols

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

Target data

Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins; pre-mRNA splicing by altering splice site recognition sequences; RNA stability by changing sequences involved in nuclease recognition; genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication; and RNA structure-dependent activities such as microRNA production or targeting or protein-RNA interactions. Can edit both viral and cellular RNAs and can edit RNAs at multiple sites (hyper-editing) or at specific sites (site-specific editing). Its cellular RNA substrates include : bladder cancer-associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2 and GRIK2) and serotonin (HTR2C), GABA receptor (GABRA3) and potassium voltage-gated channel (KCNA1). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alter their functional activities. Edits GRIA2 at both the Q/R and R/G sites efficiently but converts the adenosine in hotspot1 much less efficiently. Can exert a proviral effect towards human immunodeficiency virus type 1 (HIV-1) and enhances its replication via both an editing-dependent and editing-independent mechanism. The former involves editing of adenosines in the 5'UTR while the latter occurs via suppression of EIF2AK2/PKR activation and function. Can inhibit cell proliferation and migration and can stimulate exocytosis.. Isoform 1. Has a lower catalytic activity than isoform 2.. Isoform 2. Has a higher catalytic activity than isoform 1.
See full target information ADARB1

Publications (7)

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

Molecular therapy. Nucleic acids 21:932-953 PubMed32814251

2020

Adenosine-to-Inosine Editing of Vasoactive MicroRNAs Alters Their Targetome and Function in Ischemia.

Applications

Unspecified application

Species

Unspecified reactive species

Reginald V C T van der Kwast,Laura Parma,M Leontien van der Bent,Eva van Ingen,Fabiana Baganha,Hendrika A B Peters,Eveline A C Goossens,Karin H Simons,Meindert Palmen,Margreet R de Vries,Paul H A Quax,A Yaël Nossent

Nucleic acids research 46:7379-7395 PubMed29992293

2018

SRSF9 selectively represses ADAR2-mediated editing of brain-specific sites in primates.

Applications

Unspecified application

Species

Unspecified reactive species

Raghuvaran Shanmugam,Fan Zhang,Harini Srinivasan,John Lalith Charles Richard,Kaiwen I Liu,Xiujun Zhang,Cheok Wei A Woo,Zi Hao M Chua,Jan Paul Buschdorf,Michael J Meaney,Meng How Tan

Nucleic acids research 46:7323-7338 PubMed29733375

2018

Tissue-selective restriction of RNA editing of CaV1.3 by splicing factor SRSF9.

Applications

Unspecified application

Species

Unspecified reactive species

Hua Huang,Katannya Kapeli,Wenhao Jin,Yuk Peng Wong,Thiruma Valavan Arumugam,Joanne Huifen Koh,Sumitra Srimasorn,Karthik Mallilankaraman,John Jia En Chua,Gene W Yeo,Tuck Wah Soong

Genes 9: PubMed29419780

2018

Differential Enzymatic Activity of Rat ADAR2 Splicing Variants Is Due to Altered Capability to Interact with RNA in the Deaminase Domain.

Applications

Unspecified application

Species

Unspecified reactive species

Alice Filippini,Daniela Bonini,Edoardo Giacopuzzi,Luca La Via,Fabrizio Gangemi,Marina Colombi,Alessandro Barbon

Molecular cell 69:126-135.e6 PubMed29304330

2018

N-Methyladenosines Modulate A-to-I RNA Editing.

Applications

Unspecified application

Species

Unspecified reactive species

Jian-Feng Xiang,Qin Yang,Chu-Xiao Liu,Man Wu,Ling-Ling Chen,Li Yang

RNA biology 14:1580-1591 PubMed28640668

2017

Absence of the Fragile X Mental Retardation Protein results in defects of RNA editing of neuronal mRNAs in mouse.

Applications

Unspecified application

Species

Unspecified reactive species

Alice Filippini,Daniela Bonini,Caroline Lacoux,Laura Pacini,Maria Zingariello,Laura Sancillo,Daniela Bosisio,Valentina Salvi,Jessica Mingardi,Luca La Via,Francesca Zalfa,Claudia Bagni,Alessandro Barbon

PloS one 9:e91288 PubMed24608178

2014

Down-regulation of the RNA editing enzyme ADAR2 contributes to RGC death in a mouse model of glaucoma.

Applications

IHC-P

Species

Mouse

Ai Ling Wang,Reed C Carroll,Scott Nawy
View all publications

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