Recombinant Human Histone Chaperone Asf1A (ASF1A) Protein (GST)

Name: Recombinant Human Histone Chaperone Asf1A (ASF1A) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08643P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Histone Chaperone Asf1A (ASF1A) Protein (GST) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9Y294
Target Symbol	ASF1A
Synonyms	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)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLDSVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYTETELRENPPVKPDFSKLQRNILASNPRVTRFHINWEDNTEKLEDAESSNPNLQSLLSTDALPSASKGWSTSENSLNVMLESHMDCM
Expression Range	1-204aa
Protein Length	Full Length
Mol. Weight	50.0kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
Subcellular Location	Nucleus.
Protein Families	ASF1 family
Database References	HGNC: 20995 OMIM: 609189 KEGG: hsa:25842 STRING: 9606.ENSP00000229595 UniGene: PMID: 28625518 ASF1a promotes non-homologous end joining repair by facilitating phosphorylation of MDC1 by ATM at double-strand breaks. PMID: 28943310 Data show that the ubiquitin-conjugating enzyme E2 RAD6A/B-MDM2 ubiquitin ligase machinery regulates anti-silencing function 1A protein (ASF1A) degradation. PMID: 26336826 quaternary complex of histone H3-H4 heterodimer with chaperone ASF1 and the replicative helicase subunit MCM2 PMID: 26186914 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 Data indicate Tousled-like kinases (TLK1) phosphorylation has an impact on cell cycle proteins Asf1a and Asf1b function. PMID: 24598821 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 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 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 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 The authors propose that Codanin-1 acts as a negative regulator of Asf1 function in chromatin assembly. PMID: 22407294 Low ASF1A is associated with familial longevity. PMID: 22247756 HIRA plays a unique, ASF1a-independent role, which is required for the localization of HP1 PMID: 21347226 Identify marks on histones H3-H4 bound to Asf1 and changes induced upon replication stress. PMID: 20227376 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 NMR structure of the conserved core of hAsf1 A PMID: 15213445 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 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 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 Studies provide evidence for TLK1B-mediated phosphorylation of Asf1 triggering DNA repair. PMID: 17054786 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 the crystal structure, at 2.7 A resolution, of CIA-I in complex with histones H3 and H4 PMID: 17293877 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 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 ASF1A and ASF1B play a role in the efficiency of nucleosome assembly in vivo in human cells. PMID: 18378699 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 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

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.