Recombinant Human Histone H4 (H4C1) Protein (His)

Name: Recombinant Human Histone H4 (H4C1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-00462P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Histone H4 (H4C1) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P62805
Target Symbol	H4C1
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	C-6His
Target Protein Sequence	SGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
Expression Range	2-103aa
Protein Length	Full Length of Mature Protein
Mol. Weight	18.1 kDa
Research Area	Others
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	Core component of nucleosome. 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 H4 family
Database References	HGNC: 4781 OMIM: 142750 KEGG: hsa:121504 STRING: 9606.ENSP00000367034 UniGene: PMID: 28977641 Data suggest post-translational modifications of histones, trimethylation of lysine 36 in H3 (H3K36me3) and acetylation of lysine 16 in H4 (H4K16ac), have roles in DNA damage repair; H3K36me3 stimulates H4K16ac upon DNA double-strand break; SETD2, LEDGF, and KAT5 are required for these epigenetic changes. (SETD2 = SET domain containing 2; LEDGF = lens epithelium-derived growth factor; KAT5 = lysine acetyltransferase 5) PMID: 28546430 Data show that Omomyc protein co-localized with proto-oncogene protein c-myc (c-Myc), protein arginine methyltransferase 5 (PRMT5) and histone H4 H4R3me2s-enriched chromatin domains. PMID: 26563484 H4K12ac is regulated by estrogen receptor-alpha and is associated with BRD4 function and inducible transcription PMID: 25788266 Systemic lupus erythematosus appears to be associated with an imbalance in histone acetyltransferases and histone deacetylase enzymes favoring pathologic H4 acetylation. PMID: 25611806 Sumoylated human histone H4 prevents chromatin compaction by inhibiting long-range internucleosomal interactions. PMID: 25294883 Acetylation at lysine 5 of histone H4 associated with lytic gene promoters during reactivation of Kaposi's sarcoma-associated herpesvirus. PMID: 25283865 An increase in histone H4 acetylation caused by hypoxia in human neuroblastoma cell lines corresponds to increased levels of N-myc transcription factor in these cells. PMID: 24481548 Data indicate that G1-phase histone assembly is restricted to CENP-A and H4. PMID: 23363600 This study focused on the distribution of a specific histone modification, namely H4K12ac, in human sperm and characterized its specific enrichment sites in promoters throughout the whole human genome. PMID: 22894908 SRP68/72 heterodimers as major nuclear proteins whose binding of histone H4 tail is inhibited by H4R3 methylation. PMID: 23048028 TNF-alpha inhibition of AQP5 expression in human salivary gland acinar cells is due to the epigenetic mechanism by suppression of acetylation of histone H4. PMID: 21973049 our data suggest that global histone H3 and H4 modification patterns are potential markers of tumor recurrence and disease-free survival in non-small cell lung cancer PMID: 22360506 HAT1 differentially impacts nucleosome assembly of H3.1-H4 and H3.3-H4. PMID: 22228774 phosphorylation of histone H4 Ser 47 catalyzed by the PAK2 kinase, promotes nucleosome assembly of H3.3-H4 and inhibits nucleosome assembly of H3.1-H4 by increasing the binding affinity of HIRA to H3.3-H4 and reducing association of CAF-1 with H3.1-H4 PMID: 21724829 the imatinib-induced hemoglobinization and erythroid differentiation in K562 cells are associated with global histone H4 PMID: 20949922 Our findings reveal the molecular mechanisms whereby the DNA sequences within specific gene bodies are sufficient to nucleate the monomethylation of histone H4 lysine 200 which, in turn, reduces gene expression by half. PMID: 20512922 Downregulated by zinc and upregulated by docosahexaenoate in a neuroblastoma cell line. PMID: 19747413 low levels of histone acetylation is associated with the development and progression of gastric carcinomas, possibly through alteration of gene expression PMID: 12385581 overexpression of MTA1 protein and acetylation level of histone H4 protein are closely related PMID: 15095300 peptidylarginine deiminase 4 regulates histone Arg methylation by converting methyl-Arg to citrulline and releasing methylamine; data suggest that PAD4 mediates gene expression by regulating Arg methylation and citrullination in histones PMID: 15345777 lack of biotinylation of K12 in histone H4 is an early signaling event in response to double-strand breaks PMID: 16177192 incorporation of acetylated histone H4-K16 into nucleosomal arrays inhibits the formation of compact 30-nanometer-like fibers and impedes the ability of chromatin to form cross-fiber interactions PMID: 16469925 Apoptosis is associated with global DNA hypomethylation and histone deacetylation events in leukemia cells. PMID: 16531610 BTG2 contributes to retinoic acid activity by favoring differentiation through a gene-specific modification of histone H4 arginine methylation and acetylation levels. PMID: 16782888 Relationship between histone H4 modification, epigenetic regulation of BDNF gene expression, and long-term memory for extinction of conditioned fear. PMID: 17522015 H4 tail and its acetylation have novel roles in mediating recruitment of multiple regulatory factors that can change chromatin states for transcription regulation PMID: 17548343 Brd2 bromodomain 2 is monomeric in solution and dynamically interacts with H4-AcK12; additional secondary elements in the long ZA loop may be a common characteristic of BET bromodomains. PMID: 17848202 Spermatids Hypac-H4 impairment in mixed atrophy did not deteriorate further by AZFc region deletion. PMID: 18001726 the SET8 and PCNA interaction couples H4-K20 methylation with DNA replication PMID: 18319261 H4K20 monomethylation and PR-SET7 are important for L3MBTL1 function PMID: 18408754 High expression of acetylated H4 is more common in aggressive than indolent cutaneous T-cell lymphoma. PMID: 18671804 Our findings indicate an important role of histone H4 modifications in bronchial carcinogenesis PMID: 18974389 results indicate, by acetylation of histone H4 K16 during S-phase, early replicating chromatin domains acquire the H4K16ac-K20me2 epigenetic label that persists on the chromatin throughout mitosis & is deacetylated in early G1-phase of the next cell cycle PMID: 19348949 acetylated H4 is overexpressed in diffuse large B-cell lymphoma and peripheral T-cell lymphoma relative to normal lymphoid tissue. PMID: 19438744 The release of histone H4 by holocrine secretion from the sebaceous gland may play an important role in innate immunity. PMID: 19536143 histone modification including PRC2-mediated repressive histone marker H3K27me3 and active histone marker acH4 may involve in CD11b transcription during HL-60 leukemia cells reprogramming to terminal differentiation PMID: 19578722 A role of Cdk7 in regulating elongation is further suggested by enhanced histone H4 acetylation and diminished histone H4 trimethylation on lysine 36-two marks of elongation-within genes when the kinase was inhibited. PMID: 19667075 Data showed the dynamic fluctuation of histone H4 acetylation levels during mitosis, as well as acetylation changes in response to structurally distinct histone deacetylase inhibitors. PMID: 19805290 Data directly implicate BBAP in the monoubiquitylation and additional posttranslational modification of histone H4 and an associated DNA damage response. PMID: 19818714

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.