Recombinant Human ASF1A protein (His tag N-Terminus)
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Recombinant Human ASF1A protein (His tag N-Terminus) is a Human Full Length protein, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.
View Alternative Names
CGI-98, HSPC146, ASF1A, Histone chaperone ASF1A, Anti-silencing function protein 1 homolog A, CCG1-interacting factor A, hAsf1, hAsf1a, CIA, hCIA
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human ASF1A protein (AB84211)
3µg by SDS-PAGE under reducing condition and visualized by coomassie blue stain.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
ASF1A is part of the chromatin remodeling machinery ensuring proper chromatin dynamics and genome integrity. It acts in conjunction with other proteins such as CAF-1 and HIRA as part of the histone deposition process. ASF1A contributes to DNA replication repair and transcription regulation. Through interaction with these complexes ASF1A supports the replacement of histones during S-phase and post-replication repair which is essential for cell cycle progression and genome stability.
Pathways
ASF1A has significant engagement in pathways associated with DNA replication and chromatin modification. It operates within the DNA damage checkpoint pathway where it collaborates with proteins like ATR and CHK1 to ensure proper DNA damage response and cell cycle control. ASF1A also associates with the replication fork protection pathway important for the stabilization of halted replication forks and prevention of genomic instability.
Specifications
Form
Liquid
Additional notes
ab84211 is purified using conventional chromatography techniques.
General info
Function
Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly (PubMed : 10759893, PubMed : 11897662, PubMed : 12842904, PubMed : 14718166, PubMed : 15664198, PubMed : 16151251, PubMed : 21454524). Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly (PubMed : 11897662, PubMed : 14718166, PubMed : 15664198). Promotes homologous recombination-mediated repair of double-strand breaks (DSBs) at stalled or collapsed replication forks : acts by mediating histone replacement at DSBs, leading to recruitment of the MMS22L-TONSL complex and subsequent loading of RAD51 (PubMed : 29478807). Also involved in the nuclear import of the histone H3-H4 dimer together with importin-4 (IPO4) : specifically recognizes and binds newly synthesized histones with the monomethylation of H3 'Lys-9' and acetylation at 'Lys-14' (H3K9me1K14ac) marks, and diacetylation at 'Lys-5' and 'Lys-12' of H4 (H4K5K12ac) marks in the cytosol (PubMed : 21454524, PubMed : 29408485). Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit (PubMed : 15621527).
Sequence similarities
Belongs to the ASF1 family.
Post-translational modifications
Phosphorylated by TLK1 and TLK2 (PubMed:11470414, PubMed:20016786, PubMed:35136069). Highly phosphorylated in S-phase and at lower levels in M-phase (PubMed:11470414). TLK2-mediated phosphorylation at Ser-192 prevents proteasome-dependent degradation (PubMed:20016786). Phosphorylation at Ser-192 by PRKDC in response to DNA damage promotes the histone chaperone activity and ability to replace histones at double-strand breaks (DSBs) at stalled or collapsed replication forks, leading to RAD51 recruitment (PubMed:29478807).
Subcellular localisation
Nucleus
Target data
Product promise
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