RNF2 / RING2 / RING1B Antibody (aa189-201)
Goat Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC-P, IF, E |
---|---|
Primary Accession | Q99496 |
Reactivity | Human, Mouse, Rat, Chicken, Bovine, Dog |
Host | Goat |
Clonality | Polyclonal |
Calculated MW | 38kDa |
Dilution | ELISA (1:5000-1:25000), IHC-P (2.5 µg/ml), WB (1:500-1:2000) |
Gene ID | 6045 |
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Other Names | E3 ubiquitin-protein ligase RING2, 6.3.2.-, Huntingtin-interacting protein 2-interacting protein 3, HIP2-interacting protein 3, Protein DinG, RING finger protein 1B, RING1b, RING finger protein 2, RING finger protein BAP-1, RNF2, BAP1, DING, HIPI3, RING1B |
Target/Specificity | aa 189-201 of human RING1B protein. |
Reconstitution & Storage | +4°C or -20°C, Avoid repeated freezing and thawing. |
Precautions | RNF2 / RING2 / RING1B Antibody (aa189-201) is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | RNF2 |
---|---|
Synonyms | BAP1, DING, HIPI3, RING1B |
Function | E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), thereby playing a central role in histone code and gene regulation (PubMed:15386022, PubMed:16359901, PubMed:25519132, PubMed:33864376, PubMed:21772249, PubMed:25355358, PubMed:26151332). H2AK119Ub gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. May be involved in the initiation of both imprinted and random X inactivation (By similarity). Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development (PubMed:16359901, PubMed:26151332). PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility (PubMed:26151332). E3 ubiquitin-protein ligase activity is enhanced by BMI1/PCGF4 (PubMed:21772249). Acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity (Probable). Association with the chromosomal DNA is cell-cycle dependent. In resting B- and T-lymphocytes, interaction with AURKB leads to block its activity, thereby maintaining transcription in resting lymphocytes (By similarity). Also acts as a negative regulator of autophagy by mediating ubiquitination of AMBRA1, leading to its subsequent degradation (By similarity). |
Cellular Location | Nucleus. Cytoplasm {ECO:0000250|UniProtKB:Q9CQJ4}. Chromosome {ECO:0000250|UniProtKB:Q9CQJ4}. Note=Enriched on inactive X chromosome (Xi) in female trophoblast stem (TS) cells as well as differentiating embryonic stem (ES) cells. The enrichment on Xi is transient during TS and ES cell differentiation. The association with Xi is mitotically stable in non-differentiated TS cells. {ECO:0000250|UniProtKB:Q9CQJ4} |
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Background
E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), thereby playing a central role in histone code and gene regulation. H2AK119Ub gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. May be involved in the initiation of both imprinted and random X inactivation. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. E3 ubiquitin-protein ligase activity is enhanced by BMI1/PCGF4. Acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity. In resting B- and T-lymphocytes, interaction with AURKB leads to block its activity, thereby maintaining transcription in resting lymphocytes.
References
Dyer M.J.S.,et al.Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
Li S.-F.,et al.Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Gregory S.G.,et al.Nature 441:315-321(2006).
Mural R.J.,et al.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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