Anti-ubiquitinyl-H2AK119ub

Item number Size Datasheet Manual SDS Delivery time Quantity Price
BPS-25229 50 µg - -

3 - 15 business days*

873.00€
 
Monoubiquitination of Lys-119 (H2AK119Ub) by RING1 and RNF2/RING2 complex gives a specific tag... more
Product information "Anti-ubiquitinyl-H2AK119ub"
Monoubiquitination of Lys-119 (H2AK119Ub) by RING1 and RNF2/RING2 complex gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. It is involved in the initiation of both imprinted and random X inactivation. Ubiquitinated H2A is enriched in inactive X chromosome chromatin. Ubiquitination of H2A functions downstream of methylation of 'Lys-27' of histone H3 (H3K27me). H2AK119Ub by RNF2/RING2 can also be induced by ultraviolet and may be involved in DNA repair. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties by the E2 ligase UBE2N and the E3 ligases RNF8 and RNF168, leading to the recruitment of repair proteins to sites of DNA damage. Ubiquitination at Lys-13 and Lys-15 (H2AK13Ub and H2AK15Ub, respectively) in response to DNA damage is initiated by RNF168 that mediates monoubiquitination at these 2 sites, and 'Lys-63'-linked ubiquitin are then conjugated to monoubiquitin, RNF8 is able to extend 'Lys-63'-linked ubiquitin chains in vitro. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination (H2AK13Ub and H2AK15Ub) are distinct events.
Keywords: Anti-Histone H2A type 3, Anti-H2A-clustered histone 25,
Supplier: BPS Bioscience
Supplier-Nr: 25229

Properties

Application: ChIP, ELISA, Dot Blot, WB
Antibody Type: Polyclonal
Conjugate: No
Species reactivity: human
Immunogen: region of histone H2A containing the ubiquitinylated lysine 119 (H2AK119ub), using a KLH conjugated synthetic peptide
Format: Affinity Purified

Handling & Safety

Storage: -80°C
Shipping: -20°C (International: -20°C)
Caution
Our products are for laboratory research use only: Not for administration to humans!
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