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Histone H3.3 产品

(Histone H3.3)

Categories

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 poyadenylated, unlike most histone genes. The protein encoded is a member of the histone H3 family. [provided by RefSeq, Jul 2008].

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Featured Histone H3.3 Categories

Histone H3.3 抗体

High quality antibodies with extensive validation data.

Histone H3.3 蛋白

Proteins for various applications incl. WB, ELISA, IF etc.

Recommended Histone H3.3 抗体

Product
Reactivity
Application
Validations
Cat. No.
Quantity
Datasheet
Reactivity Human
Application ELISA, WB, IHC, IF, IHC (p)
Validations
  • (4)
Cat. No. ABIN1498570
Quantity 50 μg
Datasheet Datasheet
Reactivity Human
Application WB, IF, DB
Validations
  • (2)
Cat. No. ABIN6971843
Quantity 100 μL
Datasheet Datasheet
Reactivity Chicken, Cow, Drosophila melanogaster, Horse, Human, Mouse, Opossum
Application WB, IHC, IHC (p)
Validations
  • (2)
Cat. No. ABIN1101935
Quantity 50 μg
Datasheet Datasheet

Recommended Histone H3.3 ELISA试剂盒

Product
Reactivity
Analytical Method
Validations
Cat. No.
Quantity
Datasheet
Reactivity Chicken
Analytical Method
Validations
Cat. No. ABIN1136947
Quantity 96 tests
Datasheet Datasheet

Recommended Histone H3.3 蛋白

Product
Reactivity
Source
Validations
Cat. No.
Quantity
Datasheet
Reactivity Human
Source Escherichia coli (E. coli)
Validations
  • (1)
Cat. No. ABIN2669583
Quantity 100 μg
Datasheet Datasheet
Reactivity Human
Source Escherichia coli (E. coli)
Validations
  • (1)
Cat. No. ABIN2669581
Quantity 100 μg
Datasheet Datasheet
Reactivity Human
Source Escherichia coli (E. coli)
Validations
  • (1)
Cat. No. ABIN2722821
Quantity 50 μg
Datasheet Datasheet

Latest Publications for our Histone H3.3 Products

Kong, Zhu, Yi, Huang, Zhao, Chen, Yuan, Wen, Wu, Yi: "Betulinic Acid Alleviates Spleen Oxidative Damage Induced by Acute Intraperitoneal Exposure to T-2 Toxin by Activating Nrf2 and Inhibiting MAPK Signaling Pathways." in: Antioxidants (Basel, Switzerland), Vol. 10, Issue 2, (2021) (PubMed).

Chen, Xu, Lu, Chen, Du, Hou, Huang, Liang: "Asperuloside suppressing oxidative stress and inflammation in DSS-induced chronic colitis and RAW 264.7 macrophages via Nrf2/HO-1 and NF-κB pathways." in: Chemico-biological interactions, Vol. 344, pp. 109512, (2021) (PubMed).

Zhang, Song, Yan, Cai, Zhou, Ke: "High-fat diet accelerate hepatic fatty acids synthesis in offspring male rats induced by perinatal exposure to nonylphenol." in: BMC pharmacology & toxicology, Vol. 22, Issue 1, pp. 22, (2021) (PubMed).

Xia, Hu, Chen, Yuan, Zhang, Wang, Li, Wang, Deng: "Embryonic Stem Cell Derived Small Extracellular Vesicles Modulate Regulatory T Cells to Protect against Ischemic Stroke." in: ACS nano, Vol. 15, Issue 4, pp. 7370-7385, (2021) (PubMed).

Chang, Chan, R McGhie, Udugama, Mayne, Collas, Mann, Wong: "CHK1-driven histone H3.3 serine 31 phosphorylation is important for chromatin maintenance and cell survival in human ALT cancer cells." in: Nucleic acids research, Vol. 43, Issue 5, pp. 2603-14, (2015) (PubMed).

Satterlee, Beckel-Mitchener, McAllister, Procaccini, Rutter, Tyson, Chadwick: "Community resources and technologies developed through the NIH Roadmap Epigenomics Program." in: Methods in molecular biology (Clifton, N.J.), Vol. 1238, pp. 27-49, (2014) (PubMed).

Wong, McGhie, Sim, Anderson, Ahn, Hannan, George, Morgan, Mann, Choo: "ATRX interacts with H3.3 in maintaining telomere structural integrity in pluripotent embryonic stem cells." in: Genome research, Vol. 20, Issue 3, pp. 351-60, (2010) (PubMed).

Elsaesser, Goldberg, Allis: "New functions for an old variant: no substitute for histone H3.3." in: Current opinion in genetics & development, Vol. 20, Issue 2, pp. 110-7, (2010) (PubMed).

Goldberg, Banaszynski, Noh, Lewis, Elsaesser, Stadler, Dewell, Law, Guo, Li, Wen, Chapgier, DeKelver, Miller, Lee, Boydston, Holmes, Gregory, Greally, Rafii, Yang, Scambler, Garrick, Gibbons, Higgs et al.: "Distinct factors control histone variant H3.3 localization at specific genomic regions. ..." in: Cell, Vol. 140, Issue 5, pp. 678-91, (2010) (PubMed).

Shi, Whetstine: "Dynamic regulation of histone lysine methylation by demethylases." in: Molecular cell, Vol. 25, Issue 1, pp. 1-14, (2007) (PubMed).

Synonyms and alternative names related to Histone H3.3

H3 histone family member 3A (H3F3A), H3 histone, family 3A (H3F3A), H3 histone, family 3B (H3F3B), H3 histone, family 3A (H3f3a), H3 histone, family 3C L homeolog (h3f3c.L), histone H3.3 (LOC5567559), Histone H3.3 (Bm1_29875), Histone H3.3 (Bm1_40030), histone H3.3 (PTRG_03457), histone H3.3 (Phum_PHUM492720), histone H3.3 (UREG_07214), histone H3.3 (PAAG_07099), histone H3.3 (PITG_06950), histone H3.3 (PITG_06953), histone H3.3 (PITG_06955), histone H3.3B-like (LOC100361558), histone H3.3 (LOC100521680), H3-IX, H3-X, H3.3A, H3.3B, H3F3, H3F3B, H3F3C

Protein level used designations for Histone H3.3

  • histone H3.3
  • H3 histone, family 3C
  • H3.3A/B
  • family 3B (H3.3B)
  • histone H3 class II
  • Histone H3.3
  • H3 histone, family 3B
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