Recombinant Human Histone chaperone ASF1A (ASF1A)

Code CSB-EP896689HU
Size $224
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.

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Product Details

Purity
Greater than 90% as determined by SDS-PAGE.
Target Names
ASF1A
Uniprot No.
Research Area
Epigenetics and Nuclear Signaling
Alternative Names
Anti silencing function 1A; Anti-silencing function protein 1 homolog A; ASF1 anti silencing function 1 homolog A (S. cerevisiae); ASF1 anti silencing function 1 homolog A; asf1a; ASF1A_HUMAN; CCG1 interacting factor A; CCG1-interacting factor A; CGI 98; CIA; hAsf1; hAsf1a; hCIA; Histone chaperone ASF1A; HSPC146
Species
Homo sapiens (Human)
Source
E.coli
Expression Region
1-204aa
Target Protein Sequence
MAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLDSVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYTETELRENPPVKPDFSKLQRNILASNPRVTRFHINWEDNTEKLEDAESSNPNLQSLLSTDALPSASKGWSTSENSLNVMLESHMDCM
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
50.0kDa
Protein Length
Full Length
Tag Info
N-terminal GST-tagged
Form
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.

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Target Background

Function
Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with HIRA to promote replication-independent chromatin assembly. Required for the formation of senescence-associated heterochromatin foci (SAHF) and efficient senescence-associated cell cycle exit.
Gene References into Functions
  1. ASF1A is aberrantly over-expressed in GIC tumors and plays key roles in GIC development and progression by stimulating the transcription of beta-catenin target genes. PMID: 28625518
  2. ASF1a promotes non-homologous end joining repair by facilitating phosphorylation of MDC1 by ATM at double-strand breaks. PMID: 28943310
  3. Data show that the ubiquitin-conjugating enzyme E2 RAD6A/B-MDM2 ubiquitin ligase machinery regulates anti-silencing function 1A protein (ASF1A) degradation. PMID: 26336826
  4. quaternary complex of histone H3-H4 heterodimer with chaperone ASF1 and the replicative helicase subunit MCM2 PMID: 26186914
  5. Thermodynamic analysis of the quaternary complex together with structural modeling support that ASF1 and MCM2 could form a chaperoning module for histones H3 and H4 protecting them from promiscuous interactions. PMID: 25618846
  6. Data indicate Tousled-like kinases (TLK1) phosphorylation has an impact on cell cycle proteins Asf1a and Asf1b function. PMID: 24598821
  7. findings show that ASF1A, a histone-remodeling chaperone specifically enriched in the metaphase II oocyte, is necessary for reprogramming of adult dermal fibroblasts into undifferentiated induced pluripotent stem cell PMID: 25035411
  8. The ATR checkpoint pathway causes a histone chaperone normally associated with the replication fork, ASF1a, to degrade through a CRL1(betaTRCP)-dependent ubiquitination/proteasome pathway, leading to the localized dechromatinization and gene repression. PMID: 24700029
  9. Co-depletion of the histone chaperones ASF1a and ASF1b in human cells induces all hallmarks of alternative lengthening of telomeres in both primary and cancer cells. PMID: 24413054
  10. Asf1a plays a role in regulating IE genes by assembling chromatin onto histone-free viral DNA by 3 h postinfection with herpes simplex virus 1 PMID: 22951827
  11. The authors propose that Codanin-1 acts as a negative regulator of Asf1 function in chromatin assembly. PMID: 22407294
  12. Low ASF1A is associated with familial longevity. PMID: 22247756
  13. HIRA plays a unique, ASF1a-independent role, which is required for the localization of HP1 PMID: 21347226
  14. Identify marks on histones H3-H4 bound to Asf1 and changes induced upon replication stress. PMID: 20227376
  15. model is proposed in which the synergism between hAsf1 and CAF-1 for nucleosome formation during DNA repair is achieved through a transient physical interaction allowing histone delivery from Asf1 to CAF-1 PMID: 11897662
  16. NMR structure of the conserved core of hAsf1 A PMID: 15213445
  17. Data suggest that Asf1 provides cells with a buffering system for histone excess generated in response to stalled replication and explains how cells maintain an "active" histone pool available during recovery from replication stresses. PMID: 15664198
  18. Evidence of binding between a histone and one of its chaperones and genetic data suggesting that this interaction is important in both the DNA damage response and transcriptional silencing. PMID: 15840725
  19. The N- and C-terminal regions of ASF1a and ASF1b determine the different affinities of these two proteins for HIRA, by contacting regions outside the HIRA B domain. CAF-1 p60 also uses B domain-like motifs for binding to ASF1a. PMID: 16980972
  20. Studies provide evidence for TLK1B-mediated phosphorylation of Asf1 triggering DNA repair. PMID: 17054786
  21. The structure of the conserved domain of human ASF1A in complex with the C-terminal helix of histone H3 using nuclear magnetic resonance spectroscopy was solved. PMID: 17292837
  22. the crystal structure, at 2.7 A resolution, of CIA-I in complex with histones H3 and H4 PMID: 17293877
  23. the expression of human ASF1A and ASF1B are upregulated followed by cell proliferation signal, but that of ASF1B is uniquely regulated by transcription factors E2F during cell cycle progression PMID: 17328667
  24. data link Asf1 chaperone function, histone supply, and replicative unwinding of DNA in chromatin; proposed that Asf1, as a histone acceptor and donor, handles parental and new histones at the replication fork via an Asf1-(H3-H4)-MCM2-7 intermediate PMID: 18096807
  25. ASF1A and ASF1B play a role in the efficiency of nucleosome assembly in vivo in human cells. PMID: 18378699
  26. IE63 of VZV preferentially bound to ASF1a, and the amino-terminal 30 amino acids of ASF1a were critical for its interaction with IE63. PMID: 18971269
  27. Hpc2-related domain of UBN1, UBN2, and Hpc2p is an evolutionarily conserved HIRA/Hir-binding domain, which directly interacts with the N-terminal WD repeats of HIRA/Hir. PMID: 19029251

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Subcellular Location
Nucleus.
Protein Families
ASF1 family
Tissue Specificity
Ubiquitously expressed.
Database Links

HGNC: 20995

OMIM: 609189

KEGG: hsa:25842

STRING: 9606.ENSP00000229595

UniGene: Hs.292316

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