Anticorps primaires Anti-Drosophile - FITC

Anticorps primaires Anti-Drosophile - FITC

 Anticorps primaires anti-drosophile couplés FITC

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  • FITC 306
  • drosophila 306
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  • Primary antibody 306
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Description
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Prix HT
GTX47838-50ug
 50ug 
GTX47887-50ug
 50ug 
orb27912-100ug
 100ug 
orb151497-100ul
Rabbit polyclonal to Erk1 (FITC). The extracellular signal-regulated kinases 1 and 2 (ERK1 and ERK2), also called p44 and p42 MAP kinases, are members of the Mitogen Activated Protein Kinase (MAPK) family of proteins found in all eukaryotes. Because the 44 kDa ERK1 and the 42 kDa ERK2 are highly homologous and both function in the same protein kinase cascade, the two proteins are often referred to collectively as ERK1/2 or p44/p42 MAP kinase. They are both located in the cytosol and mitochondria. While the role of cytosol ERK1/2 is well studied and involved in multiple cellular functions, the role of mitochondrial ERK1/2 remains poorly understood. Both ERK 1 and 2 are activated by MEK1 or MEK2, by dual phosphorylation of a threonine and tyrosine residue in the activation loop (TEY motif) (1, 3). Either phosphorylation alone can induce an electrophoretic mobility shift, but both are required for activation of the kinase. This dual phosphorylation is efficiently detected by phosphorylation state-specific antibody directed to the pTEpY motif. Once activated, MAP kinases phosphorylate a broad spectrum of substrates, including cytoskeletal proteins, translation regulators, transcription factors, and the Rsk family of protein kinases. ERK1/2 activation is generally thought to confer a survival advantage to cells; however there is increasing evidence that suggests that the activation of ERK1/2 also contributes to cell death under certain conditions. ERK1/2 also is activated in neuronal and renal epithelial cells upon exposure to oxidative stress and toxicants or deprivation of growth factors, and inhibition of the ERK pathway blocks apoptosis..
 100ul 
orb146753-200ug
Mouse monoclonal to Hsp70 (FITC). Hsp70 genes encode abundant heat-inducible 70-kDa hsps (hsp70s). In most eukaryotes hsp70 genes exist as part of a multigene family. They are found in most cellular compartments of eukaryotes including nuclei, mitochondria, chloroplasts, the endoplasmic reticulum and the cytosol, as well as in bacteria. The genes show a high degree of conservation, having at least 5O% identity. The N-terminal two thirds of hsp70s are more conserved than the C-terminal third. Hsp70 binds ATP with high affinity and possesses a weak ATPase activity which can be stimulated by binding to unfolded proteins and synthetic peptides. When hsc70 (constitutively expressed) present in mammalian cells was truncated, ATP binding activity was found to reside in an N-terminal fragment of 44 kDa which lacked peptide binding capacity. Polypeptide binding ability therefore resided within the C-terminal half. The structure of this ATP binding domain displays multiple features of nucleotide binding proteins. All hsp70s, regardless of location, bind proteins, particularly unfolded ones. The molecular chaperones of the hsp70 family recognize and bind to nascent polypeptide chains as well as partially folded intermediates of proteins preventing their aggregation and misfolding. The binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein. The universal ability of hsp70s to undergo cycles of binding to and release from hydrophobic stretches of partially unfolded proteins determines their role in a great variety of vital intracellular functions such as protein synthesis, protein folding and oligomerization and protein transport.
 200ug 
orb2570641-200ul
 200ul 
orb2570662-200ul
 200ul 
orb2570683-200ul
 200ul 
orb2571789-200ul
 200ul 
orb2571278-200ul
 200ul 
orb2572076-200ul
 200ul 
orb2571586-200ul
 200ul 
orb2571593-200ul
 200ul 
orb2571600-200ul
 200ul 
orb2573280-200ul
 200ul 
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