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HDAC1/HD1 [10E2]
Description Acetylation of the histone tail causes chromatin to adopt an “open” conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription. HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate non-histone proteins, suggesting multiple roles for these enzymes. In contrast, histone deacetylation promotes a “closed” chromatin conformation and typically leads to repression of gene activity. Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases. Class I (HDACs 1, 2, 3 and 8) proteins are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9 and 10) are related to yeast Hda1-like proteins and class III proteins are related to the yeast Host Mouse Application ELISA, Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat -
Heat Shock Protein (HSP27) [G3.1]
Description HSP 27 also known as 24K estrogen-regulated protein or HSP 28 is a small heat shock protein that has been shown to correlate with the expression of estrogen-receptor. Immunohistochemical studies of HSP 27 has shown that it is localized mainly in the female reproductive tract and in ER and PR positive breast tumor cell lines. Increased levels of HSP 27 have been shown to correlate with the presence of ER and PR in human breast tumor biopsy samples. (Shipping Cost: €200.00) Host Mouse Application Flow cytometry (FC), Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blot (WB) Reactivity Human, Chimpanzee, Monkey, Sheep, Rat, Mouse, Chicken -
Heat Shock Protein (HSP27) [G3.1]
Description HSP 27 also known as 24K estrogen-regulated protein or HSP 28 is a small heat shock protein that has been shown to correlate with the expression of estrogen-receptor. Immunohistochemical studies of HSP 27 has shown that it is localized mainly in the female reproductive tract and in ER and PR positive breast tumor cell lines. Increased levels of HSP 27 have been shown to correlate with the presence of ER and PR in human breast tumor biopsy samples. (Shipping Cost: €200.00) Host Mouse Application Flow cytometry (FC), Immunofluorescence (IF), Immunohistochemistry (IHC), Western Blot (WB) Reactivity Human, Chimpanzee, Monkey, Sheep, Rat, Mouse, Chicken -
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 -
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 -
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 -
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 -
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 -
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