Recombinant Human Histone H2A.X (H2AFX) Protein (GST)

Name: Recombinant Human Histone H2A.X (H2AFX) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-03481P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Histone H2A.X (H2AFX) 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	P16104
Target Symbol	H2AFX
Synonyms	H2A histone family member X ; H2A histone family member X; H2A.FX; H2A.X; H2a/x; H2AFX; H2AX; H2AX_HUMAN; Histone H2A.X
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MSGRGKTGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGHYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKTSATVGPKAPSGGKKATQASQEY
Expression Range	1-143aa
Protein Length	Full Length
Mol. Weight	42.0kDa
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	Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C-terminal phosphorylation.
Subcellular Location	Nucleus. Chromosome.
Protein Families	Histone H2A family
Database References	HGNC: 4739 OMIM: 601772 KEGG: hsa:3014 STRING: 9606.ENSP00000364310 UniGene: PMID: 30013081 This study confirms that H2AFX variants are associated with an increased risk of BC. The above-reported sequence variants of MRE11 genes may not constitute a risk factor of breast cancer in the Polish population. PMID: 29678143 gamma-irradiation also decreased the number of cells in the G1 phase, characterized by no interaction between H3S10ph and gammaH2AX. PMID: 30096372 The topology of clusters of gammaH2AX foci can be categorized depending on the distance to heterochromatin. The here presented new method opens up new possibilities to categorize spatial organization of point patterns by parameterization of topological similarity. PMID: 30072594 this study suggests that individual and co-expression pattern of nuclear oxidized-PTP and gamma-H2AX might be used as a prognostic marker of gastric carcinoma PMID: 30126387 Low pH2AX expression is associated with mouth Cancer. PMID: 30275188 Results show that the H2AX 3'U TR is targeted by miR328 and its expression inhibited in osteosarcoma cells under radiation conditions. PMID: 29207178 The results propose a model in which Aurora B-mediated H2AX-phosphorylated serine 121 probably provide a platform for Aurora B autoactivation circuitry at centromeres and thus play a pivotal role in proper chromosome segregation. PMID: 27389782 Data indicate that nuclear H2A histone family, member X protein (gammaH2AX) expression is positively associated with the programmed death-ligand 1 (PD-L1) expression in lung squamous cell carcinoma. PMID: 29275316 phosphorylated histone H2AX was predictive of disease progression epithelial dysplasia of the oral cavity. PMID: 28543539 Gamma-H2AX, phosphorylated KAP-1 and 53BP1 play an important role in the repair of heterochromatic radon-induced DNA double-strand breaks. PMID: 27922110 in a series of human biopsies, non-metastatic SCCs displayed a higher degree of chromosomal alterations and higher expression of the S phase regulator Cyclin E and the DNA damage signal gammaH2AX than the less aggressive, non-squamous, basal cell carcinomas. However, metastatic Squamous cell carcinoma lost the gammaH2AX signal and Cyclin E, or accumulated cytoplasmic Cyclin E. PMID: 28661481 We found that phosphorylation of histone H2AX on Ser139 (gamma-H2AX), a biomarker of DSBs, and phosphorylation of ATM at Ser1981, Chk2 at Thr68, and p53 at Ser15, part of signaling pathways associated with DSBs, are elevated in these cells. PMID: 28388353 number of gammaH2AX foci did not significantly change following cardiac MR (median foci per cell pre-MR = 0.11, post-MR = 0.11, p = .90), but the number of 53BP1 foci significantly increased following MR PMID: 29309426 Study provides evidence that phosphorylated H2AX binds to the promoter of miR-3196 and regulate its expression leading to lung cancer cell apoptosis. PMID: 27780918 there may not be a link between low level phosphorylation gammaH2AX sites and double-strand DNA breaks in cells exposed to topoisomerase I or II inhibitors PMID: 27391338 Residual gammaH2AX foci induced by low dose x-ray radiation in bone marrow mesenchymal stem cells do not cause accelerated senescence in the progeny of irradiated cells. PMID: 29165316 miR-24-mediated knockdown of H2AX may be a novel negative regulator of mitochondrial function and insulin signaling. PMID: 28386126 suggest that pH2AX alone or better in combination with MAP17 may become a novel and valuable prognostic biomarker for patients with laryngeal carcinoma treated with preservation approaches. PMID: 27166270 The findings demonstrate that RNF168 couples PALB2-dependent homologous recombination to H2A ubiquitylation to promote DNA repair and preserve genome integrity. PMID: 28240985 Data show that co-treated with vincristine and XL019, a inhibitor of JAK2 and P-glycoprotein (P-gp), up-regulated expression of p21 and phosphorylated H2A histone family, member X (pH2AX). PMID: 29187454 The bile acid receptor TGR5, inducible nitric oxide synthase (iNOS) and gamma-histone family 2A variant (gamma-H2AX) are up-regulated. PMID: 27247425 Co-localization of gammaH2AX and 53BP1 indicates promotion of (in)effective nonhomologous end-joining repair mechanisms at sites of DSB. Moreover, gammaH2AX/53BP1 foci distribution presumably reveals a non-random spatial organization of the genome in MDS and AML. PMID: 28359030 Cyclin F-mediated degradation of SLBP limits H2A.X accumulation and apoptosis upon genotoxic stress in G2 cell cycle checkpoint. PMID: 27773672 study demonstrates that the individual and combined expression patterns of the DDR molecules PARP1, gammaH2AX, BRCA1, and BRCA2 could be predictive of the prognosis of STS patients and suggests that controlling the activity of these DDR molecules could be employed in new therapeutic stratagems for the treatment of STS PMID: 27643881 Further analysis suggested that H2AX, a PARP-1 protein interaction partner, was coordinated with PARP-1 in hepatocellular carcinoma tumorigenesis. Overall, some new characteristics of PARP-1 expression were noted in the Zhuang population. PARP-1 is a novel promising diagnostic marker for hepatocellular carcinoma in the Southern Chinese Zhuang population PMID: 28714367 we found that gamma-H2AX foci at chromosome boundaries after carbon-ion irradiation contain DNA double strand breaks undergoing DNA-end resection, which promotes repair utilizing microhomology mediated end-joining during translocation. PMID: 27113385 this study demonstrates an early DDR defect of attenuated gammaH2AX signals in G0/G1 phase HGPS cells and provides a plausible connection between H3K9me3 loss and DDR deficiency. PMID: 27907109 Data indicate an important role for histone H2A.X (H2AX) Tyr39 phosphorylation in gamma-H2A.X formation and cancer progression. PMID: 27813335 we suggest that the XAB2 complex mediates DNA damage response events important for the end resection step of homologous recombination , and speculate that its adjacent-localization relative to double-strand break marked by gH2AX is important for this function PMID: 27084940 the epithelial-mesenchymal transition-related transcription factor Twist1 cooperates with Slug to regulate EMT upon H2A.X Loss. PMID: 27315462 Upon DNA damage, an increase in the levels of chromatin bound motor protein nuclear myosin 1 (NM1) ensues, which appears to be functionally linked to Upsilon-H2AX signaling. PMID: 27365048 TRAF6 and H2AX overexpression and gammaH2AX-mediated HIF1alpha enrichment in the nucleus of cancer cells lead to overactivation of HIF1alpha-driven tumorigenesis, glycolysis and metastasis. PMID: 27918549 gammaH2AX, claimed to be a marker of DNA double-strand breaks, was found in cell extracts of HeLa cells at elevated temperature vs. 37.0 degrees C, and these gammaH2AX signals were intensified in the presence of 3-aminobenzamide, a PARP inhibitor. PMID: 27262441 Data provide evidence that the acetylation of H2AX at Lys5 by TIP60 is required for the (ADPribosyl) ation activity and the dynamic binding of PARP-1 to chromatin after the induction of DNA damage. PMID: 26976643 data cannot finally exclude H2AX methylation of SUV39H2 in cells, additional experimental evidence is required to validate this claim. PMID: 27177470 This review outlines the role of gamma-H2AX in cell cycle, and its formation as a result of DNA damage. We investigate the role of gamma-H2AX formation in several cancer types and its correlation with other prognostic factors, and we try to find out whether it fulfills the requirements for its establishment as a classical cancer prognostic factor PMID: 28351323 this study identified histone H2AX as an antigen of systemic lupus erythematosus by comparing highly ranked genes from all the built network-derived gene lists, which was confirmed the with real-world clinical samples PMID: 27226232 dyserythropoiesis was increased in MDS patients with the deletion of chromosome 11q23, where H2AX is located. Although loss of H2AX did not affect the early stage of terminal erythropoiesis, enucleation was decreased. PMID: 26791933 the formation of 53BP1, gammaH2AX foci and their co-localization induced by gamma-rays (2, 5, 10, 50, 200 cGy) in human lymphocytes, was analyzed. PMID: 26243567 5-Hydroxymethylcytosine (5hmC) accumulates at DNA damage foci and colocalizes with major DNA damage response proteins 53BP1 and gH2AX, revealing 5hmC as an epigenetic marker of DNA damage. PMID: 26854228 Anacardic acid sensitizes prostate cancer cells to radiation therapy by repressing H2AX expression. PMID: 26884865 Results reveal a pathway controlled by ATM, SIRT6, and SNF2H to block HUWE1, which stabilizes H2AX and induces its incorporation into chromatin only when cells are damaged. PMID: 26711340 Gene expression analysis identified deregulation of histone H2A and H2B genes in all four cell lines ;histone pathways are associated with epirubicin resistance PMID: 26852132 kinetics of the accumulation of selected DNA repair-related proteins is protein specific at locally induced DNA lesions, and that the formation of gH2AX- and NBS1-positive foci, but not 53BP1-positive NBs, is cell cycle dependent in HeLa cells PMID: 26482424 The interaction of MDC1 with RNF8, but not with ATM requires WRAP53beta, suggesting that WRAP53beta facilitates the former interaction without altering phosphorylation of MDC1 by ATM. PMID: 26734725 the interaction of 53BP1 with gammaH2AX is required for sustaining the 53BP1-dependent focal concentration of activated ATM that facilitates repair of DNA double-strand breaks in heterochromatin in G1. PMID: 26628370 X-rays induce prolonged and ATM-independent persistence of gammaH2AX foci in human gingival mesenchymal stem cells PMID: 26314960 Cell levels of gammaH2Ax define the G2 phase of the cell cycle. PMID: 26317799 The study shows higher expression of gamma-H2AX and 53BP1 foci in rectal cancer patients compared with healthy individuals. Yet the data in vitro were not predictive in regard to the radiotherapy outcome. PMID: 26541290

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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.

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