Recombinant Human Histone H3.3 (H3F3A) Protein (GST)

Name: Recombinant Human Histone H3.3 (H3F3A) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-08507P
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 H3.3 (H3F3A) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P84243
Target Symbol	H3F3A
Synonyms	H3 histone family 3A; H3 histone family 3B; H3 histone; family 3B (H3.3B); H3.3; H3.3A; H3.3B; H33_HUMAN; H3F3; H3F3A; H3f3b; Histone H3.3; Histone H3.3Q; Histone H3.A; Histone H3.B; MGC87782; MGC87783
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	ARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
Expression Range	2-136aa
Protein Length	partial
Mol. Weight	42.2kDa
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 H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. 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.
Subcellular Location	Nucleus. Chromosome.
Protein Families	Histone H3 family
Database References	HGNC: 4764 OMIM: 137800 KEGG: hsa:3020 STRING: 9606.ENSP00000355778 UniGene: PMID: 29609578 overexpression of H3F3A, encoding H3.3, is associated with lung cancer progression and promotes lung cancer cell migration by activating metastasis-related genes PMID: 27694942 we describe the presence of the mutation p.K27M of H3F3A (H3.3K27M) in two tumours of young patients with classical histopathology of ganglioglioma PMID: 27219822 H3F3 mutations are sensitive and specific markers of giant cell tumors of the bone and chondroblastomas PMID: 28059095 H3F3A is the most frequently mutated giant cell tumor of bone driver gene. H3F3A mutations are not present in atypical giant cell tumor of bone. PMID: 28545165 H3F3A mutational testing may be a useful adjunct to differentiate giant cell tumor of bone from giant cell-rich sarcoma. PMID: 28899740 Report H3F3A/B mutations in cell tumors of bone, chondroblastomas, and aneurysmal bone cysts. PMID: 28882701 Data suggest that H3K9ac (histone 3 lysine 9 acetylation) serves as a substrate for direct binding of the SEC (super elongation complex) to chromatin; at select gene promoters, H3K9ac loss or SEC depletion appears to reduce gene expression. PMID: 28717009 We determined the incidence of H3.3 G34 mutations in primary malignant bone tumors as assessed by genotype and H3.3 G34W immunostaining PMID: 28505000 The kinase activity of Aurora B on serine 31 of histone H3.3 was biochemically confirmed with nucleosomal substrates in vitro. PMID: 28137420 This study showed that heterozygous K27M mutations in H3F3A (n = 4) or HIST1H3B (n = 3) across all primary, contiguous, and metastatic tumor sites in all Diffuse intrinsic pontine glioma. PMID: 26727948 Study examined the relationship of K27M mutations in the distinct histone H3 variants (i.e. HIST1H3B and H3F3A) with specific pontine glioma biology PMID: 26399631 study found spinal high-grade gliomas in children and adults frequently harbor H3F3A (K27M) mutations PMID: 26231952 H3F3A and H3F3B mutation analysis appears to be a highly specific, although less sensitive, diagnostic tool for the distinction of GCTB and chondroblastoma from other giant cell-containing tumors. PMID: 26457357 we describe three interesting cases of paediatric glial and glioneuronal tumours harbouring both BRAF V600E and H3F3A K27M mutations. PMID: 25389051 our observations further extend the knowledge of H3F3A mutation and its location in pediatric glioblastomas PMID: 25479829 The CENP-A/histone H3.3 nucleosome forms an unexpectedly stable structure and allows the binding of the essential centromeric protein, CENP-C, which is ectopically mislocalized in the chromosomes of CENP-A overexpressing tumor cells. PMID: 25408271 On the basis of our findings, H3F3A p.Gly34 Trp or p.Gly34 Leu mutations are not a frequent event in CGCL. PMID: 25442495 These results suggest that immunohistochemical detection of H3.3 K27M is a sensitive and specific surrogate for the H3F3A K27M mutation and defines a prognostically poor subset of pediatric glioblastomas. PMID: 25200322 this study identifies an H3.3K36me3-specific reader and a regulator of intron retention and reveals that BS69 connects histone H3.3K36me3 to regulated RNA splicing, providing significant, important insights into chromatin regulation of pre-mRNA processing. PMID: 25263594 The mutually exclusive associations of HDAC1/p300, p300/histone, and HDAC1/histone on chromatin contribute to the dynamic regulation of histone acetylation. PMID: 24722339 Loss of H3.3 from pericentromeric heterochromatin upon DAXX or PML depletion suggests that the targeting of H3.3 to PML-NBs is implicated in pericentromeric heterochromatin organization. PMID: 24200965 These data suggest that adult brainstem gliomas differ from adult supratentorial gliomas. In particular, histone genes HIST1H3B (K27M) ) mutations are frequent in adult brainstem gliomas. PMID: 24242757 H3F3A K27M mutation is associated with thalamic gliomas. PMID: 24285547 The results of this study indicate that H3F3A K27M mutant GBMs show decreased H3K27me3 that may be of both diagnostic and biological relevance. PMID: 23414300 H3F3A exon 2 mutation analyzed in solid tumors from 1351 South Korean patients PMID: 23758177 A remarkable picture of tumor type specificity for histone H3.3 driver alterations emerges, indicating that histone H3.3 residues, mutations and genes have distinct functions. PMID: 24162739 Reduced H3K27me3 and/or DNA hypomethylation are the major driving forces of activated gene expression in K27M mutant pediatric high-grade gliomas. PMID: 24183680 All reported H3.3 mutations identified in human tumors have been in the H3F3A gene leading to single codon changes within the N-terminal tail of the H3.3 protein. [Review] PMID: 24229707 This study suggested that none of H3.3 G34R mutated tumors presented primitive neuroectodermal tumors of central nervous system and pediatric glioblastomas. PMID: 23354654 diffuse intrinsic pontine gliomas containing K27M mutation display lower overall amounts of H3 with trimethylated lysine 27(H3K27me3);H3K27M inhibits enzymatic activity of Polycomb repressive complex 2 through interaction with the EZH2 subunit; propose a model where aberrant epigenetic silencing through H3K27M-mediated inhibition of PRC2 activity promotes gliomagenesis PMID: 23539183 Low frequency of H3.3 mutations in myelodysplastic syndromes patients. PMID: 23660862 indicate that H3.3K27M mutation reprograms epigenetic landscape and gene expression, which may drive tumorigenesis PMID: 23603901 H3F3A K27M mutations occur exclusively in pediatric diffuse high-grade astrocytomas PMID: 23429371 Somatic mutation of H3F3A, a chromatin remodeling gene, is rare in acute leukemias and non-Hodgkin lymphoma. PMID: 23116151 K27M mutation in H3.3 is universally associated with short survival in diffuse intrinsic pontine gliomas, while patients wild-type for H3.3 show improved survival. PMID: 22661320 demonstrate that the two H3F3A mutations give rise to glioblastomas in separate anatomic compartments, with differential regulation of transcription factors OLIG1, OLIG2, and FOXG1, possibly reflecting different cellular origins PMID: 23079654 recurrent mutations in a regulatory histone in humans; data suggest that defects of the chromatin architecture underlie paediatric and young adult GBM pathogenesis PMID: 22286061 discussion of the importance of H3.3 deposition as a salvage pathway to maintain chromatin integrity PMID: 22195966 Part of multiple H3.3-specific histone chaperone complexes PMID: 21047901 Studies indicate that H3.3 accomplishes a surprising variety of cellular and developmental processes. PMID: 20153629 Histone H3 lysine 4 methylation disrupts binding of nucleosome remodeling and deacetylase (NuRD) repressor complex PMID: 11850414 analysis of histone posttranslational modifications on H3.1 and H3.3 PMID: 17052464 Data reveal that TPA activates transcription of TBX2 through activating MSK1, which leads to an increase in phosphorylated histone H3 and the recruitment of Sp1 to the TBX2 gene. PMID: 19633291

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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.