5269 Results for: "Enzo Life Sciences"

Supplier: ENZO LIFE SCIENCES

The CYTAG™ CGH labeling kit produces high quality data for comparative genomic hybridisation (aCGH) using as little as 0,25 µg of genomic DNA, without a need for pre-amplification.

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Human Recombinant TGF-beta1 (from CHO cells)

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Red IHC chromogen (AP) is intended to be used in conjunction with alkaline phosphatase (AP)-based immunostaining or in situ hybridisation systems.

Supplier: ENZO LIFE SCIENCES

CGH labelling kit for BAC arrays has been optimised to label DNA for dual sample comparative genomic hybridisation (CGH) assays on BAC arrays. It is suitable for the preparation of cyanine 3- and cyanine 5-labelled DNA for hybridisation to BAC arrays.

Supplier: ENZO LIFE SCIENCES

HIGHDEF® red IHC chromogen can be used in conjunction with peroxidase-based immunostaining systems.

Supplier: ENZO LIFE SCIENCES

IHC mount is an aqueous-based permanent, high stability mounting medium designed for use with chromogenic labeling. Use for mounting of tissue specimens stained with peroxidase and alkaline phosphatase-based systems and various fluorescent dyes.

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Anti-KDEL Mouse Monoclonal Antibody [clone: 10C3]

Supplier: ENZO LIFE SCIENCES

Rap1, which is a member of the Ras family of GTP-binding proteins, cycles between an active GTP-bound and an unactive GDP-bound form that is mediated by GTPase activating protein (GAP). Rap1 is proposed to regulate Ras-mediated signaling and may also be involved in the regulation of Integrin-mediated cell adhesion although the mechanism of regulation is not known.

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MEK is a dual specificity kinase capable of phosphorylating both tyrosine and threonine residues. The MEK family, which is also known as MAP kinase kinase, phosphorylates MAP kinases on the conserved T-X-Y motif; phosphorylation of MAPK by MEK results in an increase in MAPK activity. MEK is involved in a diverse array of cellular processes such as stress-activated response, apoptosis, cytokine-induced cell proliferation, and DNA recombination during meiosis.

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Anti-p47Phox, NCF1 Rabbit Polyclonal Antibody

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Immunoglobulin G (IgG) is an immunoglobulin monomer consisting of two (gamma) heavy chains and two light chains. Each IgG molecule contains two antigen binding domains and a single effector (Fc) domain. Assay Designs offers isotyping kits and antibodies in a variety of formats for the detection of human, mouse, rabbit, rat, sheep, and goat IgG.

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Heme Oxygenase-1 (HO-1) also known as Hsp32, is the inducible isoform of heme oxygenase that catalyzes the NADPH, oxygen, and cytochrome P450 reductase dependent oxidation of heme to carbon monoxide, ferrous iron and biliverdin which is rapidly reduced to bilirubin.

Supplier: ENZO LIFE SCIENCES

Immunoglobulin G (IgG) is an immunoglobulin monomer consisting of two (gamma) heavy chains and two light chains. Each IgG molecule contains two antigen binding domains and a single effector (Fc) domain. Assay Designs offers isotyping kits and antibodies in a variety of formats for the detection of human, mouse, rabbit, rat, sheep, and goat IgG.

Supplier: ENZO LIFE SCIENCES

SOD (Superoxide dismutase) is responsible for the elimination of cytotoxic active oxygen by catalyzing the dismutation of the superoxide radical to oxygen and hydrogen peroxide. There are three SOD isoenzymes in mammalian cells, they are: EC SOD (extracellular SOD), Cu/Zn SOD (copper and zinc-containing SOD) and Mn SOD (manganese-containing SOD).

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Alpha-crystallins, which are part of the small Heat shock family members, are major water-soluble proteins present in the lens of the mammalian eye. Phosphorylation of serine residues which occurs during development and in response to stress, is intimately linked with its function. Chaperone activity requires, and is modulated by, oligomerization and is limited to binding unfolded intermediates to prevent irreversible aggregation.

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Anti-HDJ2 Rabbit Polyclonal Antibody

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Alpha-crystallins, which are part of the small Heat shock family members, are major water-soluble proteins present in the lens of the mammalian eye.

Supplier: ENZO LIFE SCIENCES

The 70 kDa heat shock protein Hsp70 belongs to the Hsp70 family of highly-related protein isoforms ranging in size from 66 kDa to 78 kDa. Hsc70 shares close biochemical and biological ties to Hsp70, and also belongs to the Hsp70 family. These proteins include cognate members found within major intracellular compartments and highly inducible isoforms predominantly cytoplasmic or nuclear in distribution. Members of the Hsp70 family function as molecular chaperones involved in such cellular functions as protein folding, transport, maturation and degradation, operating in an ATP-dependent manner. The molecular chaperones of the Hsp70 family recognize and bind to nascent polypeptide chains or partially folded intermediates of proteins, preventing their aggregation and misfolding, and the binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein. Data demonstrates that with a ubiquitin-like domain at its amino terminus and its association with the 26S proteosome in HeLa cells, Bag-1 modulates the chaperone activity of Hsc70 and Hsp70. These findings reveal Bag-1's role as a physical link between the Hsc70/Hsp70 chaperone system and the proteasome. Experimental data also shows that the ATPase domain and the substrate-binding domain of Hsp70 (or Hsc70) cooperate to form a co-chaperone-chaperone complex with the synaptic vesicle cysteine string protein (csp), essential for normal neurotransmitter release.

Supplier: ENZO LIFE SCIENCES

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.

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Anti-HSP90A Mouse Monoclonal Antibody [clone: K41009]

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Hsp60 is a member of the chaperonin family of heat shock proteins, with homologs functioning in the cytosol and mitochondria to fold nascent and aggregated proteins. Hsp60 is the eukaryotic homolog of the E. coli GroEL protein, and forms a multimeric complex in the mitochondria with Hsp10 (Cpn10) to form a large central cavity in which ATP-dependent protein folding takes place. TRiC/CCT, a eukaryotic relative of Hsp60, is expressed in the cytosol and participates in the folding of actin and tubulin substrates, but lacks any association with an Hsp10-like co-factor.

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The Hsp90 family of heat shock proteins represents one of the most abundantly expressed and highly conserved families of cellular chaperones whose expression can be upregulated under conditions of cellular stress, and includes cytoplasmic (Hsp90-alpha/beta), ER (grp94), and mitochondrial (TRAP1) localized members. Structurally, Hsp90 is characterized by an N-terminal ATP-binding domain, a medial substrate-binding domain, and a C-terminal dimerization motif. Hsp90 dimers function in cooperation with cochaperones (e.g. Hsp40, Hsp70, Hop, p23) to stabilize a multitude of client protein substrates, including steroid hormone receptors, protein kinases, and transcription factors. The essential binding and hydrolysis of ATP by Hsp90 is inhibited by ansamycin drugs (e.g. geldanamycin, 17-AAG) which occupy the N-terminal Hsp90 nucleotide-binding pocket. Many Hsp90 client proteins such as erbB2/Her-2, c-raf, bcr-abl, p53, and hTERT, are members of well characterized oncogenic pathways, making Hsp90 inhibitors useful anticancer agents.

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Soluble, stable and more potent Ang-1 variant.

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Produced in E. coli. Non-glycosylated protein, containing 184 amino acids.

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Produced in SF21 cells. Fused to a His-tag.

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Produced in E. coli. Non-glycosylated protein, containing 154 amino acids.

Supplier: ENZO LIFE SCIENCES

Produced in E. coli. Non-glycosylated protein, containing 133 amino acids.

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Produced in E. coli. Non-glycosylated protein, containing 71 amino acids.

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Produced in E. coli. Non-glycosylated protein, containing 54 amino acids, with a molecular weight of 6.3 kDa.

Supplier: ENZO LIFE SCIENCES

Thioredoxin (Trx) is a redox protein of approximately 12 kDa. Its primary domain is conserved across a number of Trx family members and contains a conserved catalytic site Cys-Gly-Pro-Cys. It is ubiquitous and found in many organisms from bacteria to mammals. Trx has been shown to function in cell proliferation, redox signaling and inhibition of apoptosis.