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ENZO LIFE SCIENCES
Numéro de catalogue:
(ENZOBMLSE7610025)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Ubiquitin-rhodamine is a high purity industry standard substrate for studying deubiquitinylating activity where detection sensitivity or continuous monitoring of activity.
UOM:
1 * 25 µG
New Product
Numéro de catalogue:
(ENZOBMLSE5230020)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Produced in <i>E. coli</i>. Active catalytic domain of phosphodiesterase 4D.
UOM:
1 * 20 µG
New Product
Numéro de catalogue:
(ENZOADI900120)
Fournisseur:
ENZO LIFE SCIENCES
Description:
For the quantitative determination of IgM in ascites fluid, culture supernatants, and serum of mouse origin.
UOM:
1 * 1 KIT
New Product
Numéro de catalogue:
(ENZOADI900175)
Fournisseur:
ENZO LIFE SCIENCES
Description:
The Serotonin EIA kit is a colorimetric competitive enzyme immunoassay kit with results in 3 hours.
UOM:
1 * 1 KIT
New Product
Numéro de catalogue:
(ENZOADI900115)
Fournisseur:
ENZO LIFE SCIENCES
Description:
For the quantitative determination of human Myeloperoxidase of culture supernatants, nasal lavage, Lithium-heparin plasma, sputum supernatant, and urine.
UOM:
1 * 1 KIT
New Product
Numéro de catalogue:
(ENZOADI900074)
Fournisseur:
ENZO LIFE SCIENCES
Description:
The GRO/CINC-1 (Rat), EIA kit is a colorimetric immunometric enzyme immunoassay kit with results in 2 hours. Absorbance is read at 450 nm. Assay up to 39 samples in duplicate per kit.
UOM:
1 * 1 KIT
New Product
Numéro de catalogue:
(ENZOADI900118A)
Fournisseur:
ENZO LIFE SCIENCES
Description:
The IL-2 (human), EIA kit is a colorimetric immunometric enzyme immunoassay kit with results in 3 hours.
UOM:
1 * 1 KIT
New Product
Numéro de catalogue:
(ENZOADI900166)
Fournisseur:
ENZO LIFE SCIENCES
Description:
COMET SCGE Assay measures DNA damage by fluorescently detecting the integrity of DNA liberated from cells embedded in low melting point agarose. Upon electrophoresis, fragmented DNA produces a characteristic "comet" shaped tail as small DNA fragments migrate in the gel more rapidly than in-tact genomic DNA.
UOM:
1 * 50 Tests
New Product
Fournisseur:
ENZO LIFE SCIENCES
Description:
Hsp27 is one of the most common members of the highly conserved and ubiquitously expressed family of small heat shock proteins (sHsp), which also includes alphaB-crystallin. It is characterized by a conserved C-terminal alpha-crystallin domain consisting of two anti-parallel beta-sheets that promote oligomer formation required for its primary chaperone function as inhibitor of irreversible protein aggregation. Hsp27 oligomerization is modulated by post-translational phosphorylation of Hsp27 at three serine residues, Ser15, Ser78, and Ser82, by a variety of protein kinases including MAPKAPK-3, PKAc-alpha, p70 S6K, PKD I, and PKC-delta. Hsp27 has been shown to inhibit actin polymerization by binding of unphosphorylated Hsp27 monomers to actin intermediate filaments. Anti-apoptotic functions of Hsp27 have also been identified through interactions with DAXX7, activation of Akt, and inhibition of apoptosome formation. Evidence suggests altered expression of Hsp27 is implicated in the pathogenesis of breast, ovarian, and prostate cancer.
Numéro de catalogue:
(ENZOADISPA757D)
Fournisseur:
ENZO LIFE SCIENCES
Description:
The Hsp70 family of heat shock protiens contains multiple homologs ranging in size from 66-78 kDa, and are the eukaryotic equivalents of the bacterial DnaK. The most studied Hsp70 members include the cytosolic stress-induced Hsp70 (Hsp72), the constitutive cytosolic Hsc70 (Hsp73), and the ER-localized BiP (Grp78). Hsp70 family members contain highly conserved N-terminal ATP-ase and C-terminal protein binding domains. Binding of peptide to Hsp70 is assisted by Hsp40, and stimulates the inherent ATPase activity of Hsp70, facilitating ATP hydrolysis and enhanced peptide binding. Hsp70 nucleotide exchange and substrate binding coordinates the folding of newly synthesized proteins, the re-folding of misfolded or denatured proteins, coordinates trafficking of proteins across cellular membranes, inhibits protein aggregation, and targets the degradation of proteins via the proteasomal pathway.
UOM:
1 * 50 µG
New Product
Fournisseur:
ENZO LIFE SCIENCES
Description:
The Hsp60 of Heliothis viescens belongs to a highly conserved family of molecular chaperones from several species, including plant Hsp60 (known as Rubisco binding protein), GroEL, the E.coli Hsp60, and 65 kDa major antigen of mycobacteria. In eukaryotes, Hsp60 is localized in the mitochondrial matrix, and in plants Hsp60 is localized in the chloroplast. Mitochondria, chloroplasts and bacteria share a common ancestry (>1 billion years), and this coupled with the high degree of homology between the divergent Hsp60s suggests that these proteins perform a primitive but vital function similar to all the different species. The common characteristics shared by the Hsp60s from the divergent species include high abundance; induction with environmental stress such as heat shock; homo-oligomeric structures of either 7 or 14 subunits which reversibly dissociate in the presence of Mg2+ and ATP; ATPase activity; and a role in folding and assembly of oligomeric protein structures. Studies support these similarities, showing expression of the single-ring human mitochondrial homolog Hsp60 with its co-chaperonin Hsp10, in a E. coli strain engineered so that the groE operon remained under strict regulatory control. The findings demonstrate that expression of Hsp60-Hsp10 enabled successful performance of all essential in vivo functions of GroEL and its co-chaperonin, GroES. Consistent with their functions as chaperones, Hsp60 and Hsp10 may act as docking molecules with a passive role in the maturation of caspase processing. Data incidates that recombinant Hsp60 and Hsp10 accelerate the activation of procaspase-3 by cytochrome c and dATP in an ATP-dependent manner. Hsps are intracellular proteins thought to serve protective functions against infection and cellular stress; however, several studies reveal a possible link between members of the Hsp60 and a number of autoimmune diseases, atherosclerosis, and chlamydial disease.
Fournisseur:
ENZO LIFE SCIENCES
Description:
The Hsp70 family of heat shock proteins contains multiple homologs ranging in size from 66-78 kDa, and are the eukaryotic equivalents of the bacterial DnaK. The most studied Hsp70 members include the cytosolic stress-induced Hsp70 (Hsp72), the constitutive cytosolic Hsc70 (Hsp73), and the ER-localized BiP (Grp78). Hsp70 family members contain highly conserved N-terminal ATP-ase and C-terminal protein binding domains. Binding of peptide to Hsp70 is assisted by Hsp40, and stimulates the inherent ATPase activity of Hsp70, facilitating ATP hydrolysis and enhanced peptide binding. Hsp70 nucleotide exchange and substrate binding coordinates the folding of newly synthesized proteins, the re-folding of misfolded or denatured proteins, coordinates trafficking of proteins across cellular membranes, inhibits protein aggregation, and targets the degradation of proteins via the proteasomal pathway.
Fournisseur:
ENZO LIFE SCIENCES
Description:
Hsp27 is one of the most common members of the highly conserved and ubiquitously expressed family of small heat shock proteins (sHsp), which also includes alphaB-crystallin. It is characterized by a conserved C-terminal alpha-crystallin domain consisting of two anti-parallel beta-sheets that promote oligomer formation required for its primary chaperone function as inhibitor of irreversible protein aggregation. Hsp27 oligomerization is modulated by post-translational phosphorylation of Hsp27 at three serine residues, Ser15, Ser78, and Ser82, by a variety of protein kinases including MAPKAPK-3, PKAc-alpha, p70 S6K, PKD I, and PKC-delta. Hsp27 has been shown to inhibit actin polymerization by binding of unphosphorylated Hsp27 monomers to actin intermediate filaments. Anti-apoptotic functions of Hsp27 have also been identified through interactions with DAXX7, activation of Akt, and inhibition of apoptosome formation. Evidence suggests altered expression of Hsp27 is implicated in the pathogenesis of breast, ovarian, and prostate cancer.
Fournisseur:
ENZO LIFE SCIENCES
Description:
The Hsp70 family of heat shock protiens contains multiple homologs ranging in size from 66-78 kDa, and are the eukaryotic equivalents of the bacterial DnaK. The most studied Hsp70 members include the cytosolic stress-induced Hsp70 (Hsp72), the constitutive cytosolic Hsc70 (Hsp73), and the ER-localized BiP (Grp78). Hsp70 family members contain highly conserved N-terminal ATP-ase and C-terminal protein binding domains. Binding of peptide to Hsp70 is assisted by Hsp40, and stimulates the inherent ATPase activity of Hsp70, facilitating ATP hydrolysis and enhanced peptide binding. Hsp70 nucleotide exchange and substrate binding coordinates the folding of newly synthesized proteins, the re-folding of misfolded or denatured proteins, coordinates trafficking of proteins across cellular membranes, inhibits protein aggregation, and targets the degradation of proteins via the proteasomal pathway.
Numéro de catalogue:
(ENZOALX210898R100)
Fournisseur:
ENZO LIFE SCIENCES
Description:
VASP (vasodilator stimulated phosphoprotein) is a proline-rich protein substrate of cAMP- and cGMP-dependent protein kinases. Phosphorylation of VASP at Ser-157 causes a mobility shift in SDS gel electrophoresis from 46 to 50 kDa, which has been used as a convenient marker to monitor cyclic nucleotide-dependent protein kinase activity. VASP is the founding member of the Ena-VASP protein family, comprising the Drosophila protein Enabled (Ena), its mouse homologue Mena (mammalian Enabled), and mouse EVL (Ena-VASP-like protein). With these proteins VASP shares a conserved overall domain organization:
a) the conserved N-terminal Ena-VASP homology domain 1 (EVH1), which mediates binding to a proline-rich motif b) a more divergent proline-rich central domain (which is responsible for profilin binding) c) a conserved C-terminal EVH2 domain. VASP is expressed in a variety of mammalian cell types and tissues. In cultured cells, VASP is associated with focal adhesions, cell-cell contacts, microfilaments, and highly dynamic membrane regions. From in vitro binding data VASP has been suggested to link profilin to zyxin, vinculin, and the Listeria spp. surface protein ActA, respectively. Functional evidence indicates that VASP is a crucial factor involved in the enhancement of actin filament formation and the actin-dependent motility of intracellular bacterial pathogens.
UOM:
1 * 100 µl
New Product
Numéro de catalogue:
(ENZOALX210732R100)
Fournisseur:
ENZO LIFE SCIENCES
Description:
Host: Rabbit
UOM:
1 * 100 µl
New Product
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