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HIF-1 alpha [EP118]
Description The HIF-1 Alpha subunit of hypoxia-inducible factor 1 is a transcription factor that functions as a master transcriptional regulator of the adaptive response to hypoxia. HIF-1 activates the transcription of many genes, thus playing a role in various biological processes, including cardiovascular development, angiogenesis, energy metabolism, and cell survival. (Shipping Cost: €200.00) Host Rabbit Application Immunohistochemistry (IHC) Reactivity Human -
HIF-1 alpha [H1α67]
Description The HIF-1 Alpha subunit of hypoxia-inducible factor 1 is a transcription factor that functions as a master transcriptional regulator of the adaptive response to hypoxia. HIF-1 activates the transcription of many genes, thus playing a role in various biological processes, including cardiovascular development, angiogenesis, energy metabolism, and cell survival. (Shipping Cost: €200.00) Host Mouse Application EMSA, Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat, Ferret -
HIF-2 alpha/EPAS1 [190b]
Description Hypoxia-inducible factor (HIF) is essential for the cellular response to hypoxia. Under normoxia conditions, the α subunit of HIF is ubiquitinated by von Hippel-Lindau (VHL) protein and is degraded in the ubiquitin/proteasome pathway. Hypoxia inhibits the degradation of the α subunit, which leads to its stabilization. HIF, in turn, regulates the transcription of a variety of genes that respond to hypoxia conditions. There are several isoforms of the HIF α subunit. Studies have found that HIF-1α and HIF-2α expression is increased in some human cancers. HIF-1α has both pro- and anti-proliferative activities, whereas HIF-2α does not possess anti-proliferative activity. Therefore, HIF-2α likely plays an important role in tumorigenesis. (Shipping Cost: €200.00) Host Mouse Application ELISA, Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat -
Histone H1 (Nuclear Marker) [AE-4]
Description Eukaryotic histones are basic and water-soluble nuclear proteins that form hetero-octameric nucleosome particles by wrapping 146 base pairs of DNA in a left-handed super-helical turn sequentially to form chromosomal fiber. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form the octamer; formed of two H2A-H2B dimers and two H3-H4 dimers, forming two nearly symmetrical halves by tertiary structure. Over 80% of nucleosomes contain the linker Histone H1, derived from an intronless gene that interacts with linker DNA between nucleosomes and mediates compaction into higher order chromatin. Histones are subject to posttranslational modification by enzymes primarily on their N-terminal tails, but also in their globular domains. Such modifications include methylation, citrullination, acetylation, phosphorylation, sumoylation, ubiquitination and ADP-ribosylation. (Shipping Cost: €200.00) Host Mouse Application Flow cytometry (FC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC) Reactivity Human, Mouse, Rat -
Histone H3 Acetyl Lys27/H3K27ac [MD162R]
Description The Histone H3 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H3 is involved with the structure of the nucleosomes of the 'beads on a string' structure. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of epigenetic modifications that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine. Histone H3 is primarily acetylated at Lys9, 14, 18, 23, 27, and 56. Acetylation of H3 at Lys27 appears to have a dominant role in histone deposition and chromatin assembly in some organisms. (Shipping Cost: €200.00) Host Rabbit Application Immunohistochemistry (IHC) Reactivity Human -
Histone H3 Acetyl Lys9/H3K9ac [MD161R]
Description The Histone H3 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H3 is involved with the structure of the nucleosomes of the 'beads on a string' structure. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of epigenetic modifications that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine. Arginine methylation of histones H3 (Arg2, 17, 26) and H4 (Arg3) promotes transcriptional activation and is mediated by a family of protein arginine methyltransferases (PRMTs), including the co-activators PRMT1 and CARM1 (PRMT4). In contrast, a more diverse set of histone lysine methyltransferases have been identified, all but one of which contain a conserved catalytic SET domain origin Host Rabbit Application Immunohistochemistry (IHC) Reactivity Human -
Histone H3 Family 3A/H3F3A [MD148R]
Description Histone H3 is one of the DNA-binding proteins found in the chromatin of all eukaryotic cells. H3 along with four core histone proteins binds to DNA forming the structure of the nucleosome. Post translationally, histones are modified in a variety of ways to either directly change the chromatin structure or allow for the binding of specific transcription factors. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of post-translational modification that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine. 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 throu Host Rabbit Application Immunohistochemistry (IHC) Reactivity Human -
Histone H3 K27M Mutant/H3K27M [RM192]
Description Histone H3 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Featuring a main globular domain and a long N-terminal tail, H3 is involved with the structure of the nucleosomes of the 'beads on a string' structure. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of epigenetic modifications that influence cellular processes. These modifications include the covalent attachment of methyl or acetyl groups to lysine and arginine amino acids and the phosphorylation of serine or threonine. Histone variant H3.3 is typically enriched in active chromatin. (Shipping Cost: €200.00) Host Rabbit Application ELISA, Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blot (WB) Reactivity Human, Mouse, Rat -
Histone H3 Phospho (PHH3) Polyconal
Description Phosphohistone-H3 (PHH3) is a core histone protein, which together with other histones forms the major protein constituents of the chromatin in eukaryotic cells. In mammalian cells, phosphohistone H3 is negligible during interphase but reaches a maximum for chromatin condensation during mitosis. Immunohistochemical studies showed anti-PHH3 detected specifically the core protein histone H3 only when phosphorylated at serine 10 or serine 28. Studies have also revealed no hosphorylation on the histone H3 during apoptosis. Therefore, PHH3 can serve as a mitotic marker to separate mitotic figures from apoptotic bodies and karyorrhectic debris, which may be a very useful tool in diagnosis of tumor grades, especially in CNS, skin, Gyn., Soft tissue, and GIST. (Shipping Cost: €200.00) Host Rabbit Application Immunohistochemistry (IHC) Reactivity Human -
Histone H3 Phospho (PHH3) Polyconal
Description Phosphohistone-H3 (PHH3) is a core histone protein, which together with other histones forms the major protein constituents of the chromatin in eukaryotic cells. In mammalian cells, phosphohistone H3 is negligible during interphase but reaches a maximum for chromatin condensation during mitosis. Immunohistochemical studies showed anti-PHH3 detected specifically the core protein histone H3 only when phosphorylated at serine 10 or serine 28. Studies have also revealed no phosphorylation on the histone H3 during apoptosis. Therefore, PHH3 can serve as a mitotic marker to separate mitotic figures from apoptotic bodies and karyorrhectic debris, which may be a very useful tool in diagnosis of tumor grades, especially in CNS, skin, Gyn., Soft tissue, and GIST. (Shipping Cost: €200.00) Host Rabbit Application Immunohistochemistry (IHC) Reactivity Human