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SDS-Page (Recombinant Histone H3.3 (K4I) protein gel 12.5% SDS-PAGE with Coomassie blue staining MW: 15.3 kDa Purity: > 92%)

Histone H3.3 Recombinant Protein | H3.3 recombinant protein

Recombinant Histone H3.3 (K4I)

Gene Names
H3F3A; H3F3; H3.3A
Synonyms
Histone H3.3; Recombinant Histone H3.3 (K4I); H3.3 recombinant protein
Ordering
For Research Use Only!
Host
E Coli
Form/Format
Recombinant Histone H3.3 (K4I) is supplied in 25mM Tris-HCl pH7.4, 150mM NaCl, and 10% glycerol.
Protein Species
Human
Protein Details
Recombinant Histone H3.3 (K4I) was expressed in E Coli cells as full length protein (accession number NP_002098.1) with a point mutation Lys4Ile and has an observed molecular weight of 15.3kDa.
Notes
This product was manufactured as described in Protein Details. Where possible, We has developed functional or activity assays for recombinant proteins. Additional characterization such as enzyme kinetic activity assays, inhibitor screening or other biological activity assays may not have been performed for every product. All available data for this product is shown.
Dry Ice Shipment
Extra charge fee may add to your shipping cost as dry ice is required to ship this product.
Preparation and Storage
Recombinant proteins in solution are temperature sensitive and must be stored at -80 degree C to prevent degradation. Avoid repeated freeze/thaw cycles and keep on ice when not in storage.
Shipping Temp: Dry Ice

SDS-Page

(Recombinant Histone H3.3 (K4I) protein gel 12.5% SDS-PAGE with Coomassie blue staining MW: 15.3 kDa Purity: > 92%)

SDS-Page (Recombinant Histone H3.3 (K4I) protein gel 12.5% SDS-PAGE with Coomassie blue staining MW: 15.3 kDa Purity: > 92%)
Related Product Information for H3.3 recombinant protein
Short Description: Histone H3 is one of the core components of the nucleosome. The nucleosome is the smallest subunit of chromatin and consists of 146 base pairs of DNA wrapped around an octamer of core histone proteins (two each of H2A, H2B, H3 and H4). Histone H1 is a linker protein, present at the interface between the nucleosome core and DNA entry/exit points. Histone H3.1 and Histone H3.3 are the two main Histone H3 variants found in plants and animals. They are known to be important for gene regulation. Histone H3.1 and H3.3 have been shown to demonstrate unique genomic localization patterns thought to be associated with their specific functions in regulation of gene activity. Specifically, Histone H3.1 localization is found to coincide with genomic regions containing chromatin repressive marks (H3K9me3, H3K27me3 and DNA methylation) Deposition of the Histone H3.1 variant into the nucleosome correlates with the canonical DNA synthesis-dependent deposition pathway. Histones are linked to tumorigenesis primarily through alterations in their PTMs and the enzymes regulating these modifications, suggesting that they might disrupt the reading, writing, and/or erasing of these marks. Mutations in histone H3 occur with high genetic penetrance within rare pediatric gliomas and sarcomas. In H3 variants, the mutation is most often a lysine-to-methionine (K-M) mutation, occasionally glycine mutations (G34R/V/W/L) occur too. According to researchers, mutations at H3K4: out of a total of 9 mutations at this site, 8 were a K4M/I substitution. More K-to-M/I mutations were observed, raising the possibility that the functional effects associated with known K-to-M/I changes (that is, function in a dominant fashion to block the methylation of corresponding lysines on wild type histones) may extend to additional contexts.

Background: Histone H3 is one of the core components of the nucleosome. The nucleosome is the smallest subunit of chromatin and consists of 146 base pairs of DNA wrapped around an octamer of core histone proteins (two each of H2A, H2B, H3 and H4). Histone H1 is a linker protein, present at the interface between the nucleosome core and DNA entry/exit points. Histone H3.1 and Histone H3.3 are the two main Histone H3 variants found in plants and animals. They are known to be important for gene regulation. Histone H3.1 and H3.3 have been shown to demonstrate unique genomic localization patterns thought to be associated with their specific functions in regulation of gene activity. Specifically, Histone H3.1 localization is found to coincide with genomic regions containing chromatin repressive marks (H3K9me3, H3K27me3 and DNA methylation) Deposition of the Histone H3.1 variant into the nucleosome correlates with the canonical DNA synthesis-dependent deposition pathway. Histones are linked to tumorigenesis primarily through alterations in their PTMs and the enzymes regulating these modifications, suggesting that they might disrupt the reading, writing, and/or erasing of these marks. Mutations in histone H3 occur with high genetic penetrance within rare paediatric gliomas and sarcomas. In H3 variants, the mutation is most often a lysine-to-methionine (K-M) mutation, occasionally glycine mutations (G34R/V/W/L) occur too. According to researchers, mutations at H3K4: out of a total of 9 mutations at this site, 8 were a K4M/I substitution. More K-to-M/I mutations were observed, raising the possibility that the functional effects associated with known K-to-M/I changes (that is, function in a dominant fashion to block the methylation of corresponding lysines on wild type histones) may extend to additional contexts.
Product Categories/Family for H3.3 recombinant protein

NCBI and Uniprot Product Information

NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Accession #
Molecular Weight
15,328 Da
NCBI Official Full Name
histone H3.3
NCBI Official Synonym Full Names
H3 histone, family 3A
NCBI Official Symbol
H3F3A
NCBI Official Synonym Symbols
H3F3; H3.3A
NCBI Protein Information
histone H3.3
UniProt Protein Name
Histone H3.3
Protein Family
UniProt Gene Name
H3F3A
UniProt Synonym Gene Names
H3.3A; H3F3
UniProt Entry Name
H33_HUMAN

NCBI Description

Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene contains introns and its mRNA is polyadenylated, unlike most histone genes. The protein encoded is a replication-independent member of the histone H3 family. [provided by RefSeq, Jul 2008]

Uniprot Description

H3F3A: 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. The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. Interacts with HIRA, a chaperone required for its incorporation into nucleosomes. Belongs to the histone H3 family.

Protein type: DNA-binding

Chromosomal Location of Human Ortholog: 1q42.12

Cellular Component: nucleoplasm; nuclear chromosome; protein complex; extracellular region; nucleosome; nucleus

Molecular Function: protein binding; nucleosomal DNA binding; protein heterodimerization activity

Biological Process: chromatin silencing at rDNA; nucleosome assembly; DNA replication-independent nucleosome assembly; negative regulation of gene expression, epigenetic; gene expression; blood coagulation; DNA methylation on cytosine; positive regulation of cell growth; regulation of gene expression, epigenetic

Research Articles on H3.3

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Product Notes

The H3.3 h3f3a (Catalog #AAA389293) is a Recombinant Protein produced from E Coli and is intended for research purposes only. The product is available for immediate purchase. It is sometimes possible for the material contained within the vial of "Histone H3.3, Recombinant Protein" to become dispersed throughout the inside of the vial, particularly around the seal of said vial, during shipment and storage. We always suggest centrifuging these vials to consolidate all of the liquid away from the lid and to the bottom of the vial prior to opening. Please be advised that certain products may require dry ice for shipping and that, if this is the case, an additional dry ice fee may also be required.

Precautions

All products in the AAA Biotech catalog are strictly for research-use only, and are absolutely not suitable for use in any sort of medical, therapeutic, prophylactic, in-vivo, or diagnostic capacity. By purchasing a product from AAA Biotech, you are explicitly certifying that said products will be properly tested and used in line with industry standard. AAA Biotech and its authorized distribution partners reserve the right to refuse to fulfill any order if we have any indication that a purchaser may be intending to use a product outside of our accepted criteria.

Disclaimer

Though we do strive to guarantee the information represented in this datasheet, AAA Biotech cannot be held responsible for any oversights or imprecisions. AAA Biotech reserves the right to adjust any aspect of this datasheet at any time and without notice. It is the responsibility of the customer to inform AAA Biotech of any product performance issues observed or experienced within 30 days of receipt of said product. To see additional details on this or any of our other policies, please see our Terms & Conditions page.

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