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Heat Shock Protein (HSP70)/HSC70 [W27]
Description The HSP 70 family is composed of four highly conserved proteins: HSP 70, HSC 70, GRP 75 and GRP 78. These proteins serve a variety of roles: they act as molecular chaperones facilitating the assembly of multi-protein complexes, participate in the translocation of polypeptides across cell membranes and to the nucleus and aid in the proper folding of nascent polypeptide chains. All members of the family, except HSP 70, are constitutively expressed in primate cells. HSP 70 expression is strongly induced in response to heat stress. HSP 70 and HSC 70 play key roles in the cytosolic endoplasmic reticulum and mitochondrial import machinery and are found in both the cytosol and nucleus of mammalian cells. Both HSP 70 and HSC 70 are involved in the chaperoning of nascent polypeptide chains and in protecting cells against the accumulation of improperly folded proteins. GRP 78 is localized in the endoplasmic reticulum, where it receives imported secretory proteins and is involved in the folding a Host Mouse Application Flow cytometry (FC), Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat 
1 ml more info 
14 days 
€361,40 Add to cart -
Heat Shock Protein (HSP70)/HSC70 [W27]
Description The HSP 70 family is composed of four highly conserved proteins: HSP 70, HSC 70, GRP 75 and GRP 78. These proteins serve a variety of roles: they act as molecular chaperones facilitating the assembly of multi-protein complexes, participate in the translocation of polypeptides across cell membranes and to the nucleus and aid in the proper folding of nascent polypeptide chains. All members of the family, except HSP 70, are constitutively expressed in primate cells. HSP 70 expression is strongly induced in response to heat stress. HSP 70 and HSC 70 play key roles in the cytosolic endoplasmic reticulum and mitochondrial import machinery and are found in both the cytosol and nucleus of mammalian cells. Both HSP 70 and HSC 70 are involved in the chaperoning of nascent polypeptide chains and in protecting cells against the accumulation of improperly folded proteins. GRP 78 is localized in the endoplasmic reticulum, where it receives imported secretory proteins and is involved in the folding a Host Mouse Application Flow cytometry (FC), Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat
7 ml more info 14 days
€187,20 Add to cart -
Heme Oxygenase 2/Hemlet 2 [B3]
Description Heme Oxygenases are microsomal enzymes that cleave heme to produce the antioxidant biliverdin, inorganic iron and carbon monoxide (CO). The activity of Heme Oxygenase 1 (HO-1), also designated HSP 32, is highly inducible in response to numerous stimuli, including heme, heavy metals, hormones and oxidative stress. Heme Oxygenase 2, in contrast, appears to be constitutively expressed in mammalian tissues. Heme Oxygenase 2 is involved in the production of carbon monoxide (CO) in brain, where CO is thought to act as a neurotransmitter. The CO signaling system closely parallels the signaling pathway involving nitric oxide, and regulation of the two systems is closely linked. Heme Oxygenase 3 is found in the spleen, liver, thymus, prostate, heart, kidney, brain and testis. A poor Heme catalyst, Heme Oxygenase 3 has two heme regulatory motifs that may be involved in Heme binding. (Shipping Cost: €200.00) Host Mouse Application ELISA, Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat
1 ml more info 14 days
€361,40 Add to cart -
HES1/ES1/c21orf33 [E5]
Description The Drosophila Hairy and enhancer of split genes encode basic helix-loophelix (bHLH) transcriptional repressors that function in the Notch signaling pathway and control segmentation and neural development during embryogenesis. The mammalian homolog of Drosophila Hairy and enhancer of split are the HES gene family members HES1-6, which also encode bHLH transcriptional repressors that regulate myogenesis and neurogenesis. The HES family members form a complex with TLE, the mammalian homolog of groucho, and this interaction is mediated by the carboxy-terminal WRPW motif of the HES proteins. The HES/TLE complex functions by directly binding to DNA instead of interfering with activator proteins. Most HES family members, including HES1 and HES5, preferentially bind to the N box (CACNAG) as opposed to the E box (CANNTG). HES1 and HES2 are expressed in a variety of adult and embryonic tissues. (Shipping Cost: €200.00) Host Mouse Application Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat
1 ml more info 14 days
€361,40 Add to cart -
HES1/ES1/c21orf33 [E5]
Description The Drosophila Hairy and enhancer of split genes encode basic helix-loophelix (bHLH) transcriptional repressors that function in the Notch signaling pathway and control segmentation and neural development during embryogenesis. The mammalian homolog of Drosophila Hairy and enhancer of split are the HES gene family members HES1-6, which also encode bHLH transcriptional repressors that regulate myogenesis and neurogenesis. The HES family members form a complex with TLE, the mammalian homolog of groucho, and this interaction is mediated by the carboxy-terminal WRPW motif of the HES proteins. The HES/TLE complex functions by directly binding to DNA instead of interfering with activator proteins. Most HES family members, including HES1 and HES5, preferentially bind to the N box (CACNAG) as opposed to the E box (CANNTG). HES1 and HES2 are expressed in a variety of adult and embryonic tissues. (Shipping Cost: €200.00) Host Mouse Application ELISA, Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat
7 ml more info 14 days
€187,20 Add to cart -
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
1 ml more info 14 days
€401,70 Add to cart -
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
1 ml more info 14 days
€401,70 Add to cart -
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
1 ml more info 14 days
€361,40 Add to cart -
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
1 ml more info 14 days
€455,00 Add to cart -
Histone H3 Tri-Methyl Lys27/H3K27Me3 [MD48R]
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 Flow cytometry (FC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat, Monkey
1 ml more info 14 days
€416,00 Add to cart
