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Recombinant RING1 Antibody - Primary antibody, specific to RING1, Rabbit IgG

  • ExactAb™
  • Recombinant
  • Validated
  • 0.4 mg/mL
Features and benefits
  • Short Overview:

    Recombinant; Rabbit anti Human RING1 Antibody; WB; Unconjugated

  • Species reactivity(Reacts with): Human,Mouse
  • Isotype: Rabbit IgG
    Application:
  • WB
Item Number
Ab125377
Grouped product items
SKUSizeAvailabilityPrice Qty
Ab125377-10μl
10μl
In stock
$69.90
Ab125377-50μl
50μl
In stock
$189.90
Ab125377-100μl
100μl
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$299.90
Ab125377-1ml
1ml
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$2,599.90

Recombinant; Rabbit anti Human RING1 Antibody; WB; Unconjugated

View related series
Accession#:Q06587 Gene ID:6015 RING1

Basic Description

Product NameRecombinant RING1 Antibody - Primary antibody, specific to RING1, Rabbit IgG
SynonymsRing1A antibody | E3 ubiquitin-protein ligase RING1 antibody | Polycomb complex protein RING1 antibody | Really interesting new gene 1 protein antibody | RING finger protein 1 antibody | Ring1 antibody | RING1_HUMAN antibody | Rnf1 antibody | Transcriptio
Specifications & PurityExactAb™, Validated, Recombinant, 0.4 mg/mL
Host speciesRabbit
SpecificityRING1
ImmunogenA synthetic peptide derived from human RING1 (AA 140-195)
Positive ControlWB: Ramos, HeLa, LNCaP, MOLT-4, THP-1 and NIH/3T3 cell lysates.
ConjugationUnconjugated
GradeExactAb™, Recombinant, Validated
Product Description

Rabbit anti Human RING1 Antibody, Recombinant, could be used for WB and so on.

Application:
WB: 1/500-1/1000
Protein Function:
Constitutes one of the E3 ubiquitin-protein ligases that mediate monoubiquitination of 'Lys-119' of histone H2A, thereby playing a central role in histone code and gene regulation. H2A 'Lys-119' ubiquitination gives a specific tag for epigenetic transcriptional repression and participates in × chromosome inactivation of female mammals. Essential component of the Polycomb group (PcG) multiprotein PRC1 complex, a complex required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex act via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. Compared to RNF2/RING2, it does not have the main E3 ubiquitin ligase activity on histone H2A, and it may rather act as a modulator of RNF2/RING2 activity.

Product Properties

IsotypeRabbit IgG
Light Chain Typekappa
SDS-PAGE150 kDa
Purification MethodProtein A purified
FormLiquid
Concentration0.4 mg/mL
Storage TempStore at -20°C,Avoid repeated freezing and thawing
Shipped InIce chest + Ice pads
Stability And StorageStore at 4℃ short term (1-2 weeks). Store at -20℃ long term (24 months). Upon delivery aliquot. Avoid freeze/thaw cycle.

Images

Recombinant RING1 Antibody (Ab125377) - Western Blot
All lanes: Recombinant RING1 Antibody (Ab125377) at 1/1000 dilution
Samples: Lysates at 20 µg per lane
Secondary: Goat Anti-Rabbit IgG H&L (HRP) (Ab170144) at 1/20000 dilution

Predicted band size: 42 kDa
Observed band size: 49, 50 kDa
Exposure time: 14.5 s

Associated Targets

RING1 Tbio E3 ubiquitin-protein ligase RING1 0 Activities

Activity TypeActivity Value -log(M)Mechanism of ActionActivity ReferencePublications (PubMed IDs)

Application

ApplicationDilution info
WB

1/500-1/1000

Certificates

Certificate of Analysis(COA)

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2 results found

Lot NumberCertificate TypeDateItem
ZJ24F0405041Certificate of AnalysisApr 29, 2024 Ab125377
ZJ24F0405040Certificate of AnalysisApr 29, 2024 Ab125377

Related Documents

References

1. Lovering, R R and 9 more authors..  (1993)  Identification and preliminary characterization of a protein motif related to the zinc finger..  Proceedings of the National Academy of Sciences of the United States of America,    (15):   [PMID:7681583]
2. Satijn, D P DP and 9 more authors..  (1997)  RING1 is associated with the polycomb group protein complex and acts as a transcriptional repressor..  Molecular and cellular biology,      [PMID:9199346]
3. Satijn, D P DP and Otte, A P AP..  (1999)  RING1 interacts with multiple Polycomb-group proteins and displays tumorigenic activity..  Molecular and cellular biology,      [PMID:9858531]
4. Ogawa, Hidesato H, Ishiguro, Kei-Ichiro K, Gaubatz, Stefan S, Livingston, David M DM and Nakatani, Yoshihiro Y..  (2002)  A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells..  Science (New York, N.Y.),    (10):   [PMID:12004135]
5. Akasaka, Takeshi T and 5 more authors..  (2002)  MBLR, a new RING finger protein resembling mammalian Polycomb gene products, is regulated by cell cycle-dependent phosphorylation..  Genes to cells : devoted to molecular & cellular mechanisms,      [PMID:12167161]
6. Levine, Stuart S SS and 5 more authors..  (2002)  The core of the polycomb repressive complex is compositionally and functionally conserved in flies and humans..  Molecular and cellular biology,      [PMID:12167701]
7. Wang, Hengbin H and 6 more authors..  (2004)  Role of histone H2A ubiquitination in Polycomb silencing..  Nature,    (14):   [PMID:15386022]
8. Cao, Ru R, Tsukada, Yu-Ichi Y and Zhang, Yi Y..  (2005)  Role of Bmi-1 and Ring1A in H2A ubiquitylation and Hox gene silencing..  Molecular cell,    (22):   [PMID:16359901]
9. Gearhart, Micah D MD, Corcoran, Connie M CM, Wamstad, Joseph A JA and Bardwell, Vivian J VJ..  (2006)  Polycomb group and SCF ubiquitin ligases are found in a novel BCOR complex that is recruited to BCL6 targets..  Molecular and cellular biology,      [PMID:16943429]
10. Maertens, Goedele N GN and 7 more authors..  (2009)  Several distinct polycomb complexes regulate and co-localize on the INK4a tumor suppressor locus..  PloS one,    (28):   [PMID:19636380]
11. Mayya, Viveka V and 7 more authors..  (2009)  Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions..  Science signaling,    (18):   [PMID:19690332]
12. Vandamme, Julien J, Völkel, Pamela P, Rosnoblet, Claire C, Le Faou, Perrine P and Angrand, Pierre-Olivier PO..  (2011)  Interaction proteomics analysis of polycomb proteins defines distinct PRC1 complexes in mammalian cells..  Molecular & cellular proteomics : MCP,      [PMID:21282530]
13. Blanchard, Maxime G MG and 13 more authors..  (2015)  De novo gain-of-function and loss-of-function mutations of SCN8A in patients with intellectual disabilities and epilepsy..  Journal of medical genetics,      [PMID:25725044]
14. Miyake, Noriko and 22 more authors..  (2020)  Gain-of-Function MN1 Truncation Variants Cause a Recognizable Syndrome with Craniofacial and Brain Abnormalities..  American journal of human genetics,    (2):   [PMID:31839203]

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