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GATA4 [G4]
Description Members of the GATA family share a conserved zinc finger DNA-binding domain and are capable of binding the WGATAR consensus sequence. GATA-1 is erythroid-specific and is responsible for the regulated transcription of erythroid genes. It is an essential component in the generation of the erythroid lineage. GATA-2 is expressed in embryonic brain and liver, HeLa and endothelial cells, as well as in erythroid cells. Studies with a modified GATA consensus sequence, AGATCTTA, have shown that GATA-2 and GATA-3 recognize this mutated consensus while GATA-1 has poor recognition of this sequence. This indicates broader regulatory capabilities of GATA-2 and GATA-3 than GATA-1. GATA-3 is highly expressed in T lymphocytes. GATA-4, GATA-5 and GATA-6 comprise a subfamily of transcription factors. Both GATA-4 and GATA-6 are found in heart, pancreas and ovary; lung and liver tissues exhibit GATA-6, but not GATA-4 expression. GATA-5 expression has been observed in differentiated heart and gut tissues an Host Mouse Application Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat 
7 ml more info 
14 days 
€187,20 Add to cart -
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
1 ml more info 14 days
€361,40 Add to cart -
Heat Shock Protein (HSP60) (Mitochondrial Marker) [LK1]
Description Recognizes a 60kDa protein, identified as the heat shock protein 60 (hsp60). Its epitope is localized between aa 383-447 of human hsp60. A wide variety of environmental and pathophysiological stressful conditions trigger the synthesis of a family of proteins known as heat shock proteins (hsps), more appropriately called as stress response proteins (srps). hsp60 is a potential antigen in a number of autoimmune diseases. In human arthritis and in experimentally induced arthritis in animals, disease development coincides with the development of immune reactivity directed against not only bacterial hsp60, but also against its mammalian homolog. Clone LK1, unlike LK2, recognizes only the mammalian (not bacterial) hsp60 and is useful in distinguishing hsp60 from mammals and bacteria. (Shipping Cost: €200.00) Host Mouse Application ELISA, Flow cytometry (FC), Immunocytochemistry (ICC),Immunofluorescence (IF), Immunohistochemistry (IHC), Immunoprecipitation (IP), Western Blot (WB) Reactivity Human, Mouse, Rat, Hamster, Sheep, Rabbit, Bovine, Dog (Canine),Pig (Porcine), Monkey, Chicken, Xenopus laevis, Drosophila
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
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
