Hledali jste: ENZO LIFE SCIENCES

Katalogové číslo: (ENZOENZABS1050100)

Dodavatel: ENZO LIFE SCIENCES

Popis: Recommended Applications: ICC, IHC, IP, WB, Immunoelectron microscopy

Měrná jednotka: 1 * 100 µl

New Product Akce

Katalogové číslo: (ENZOENZABS1460100)

Dodavatel: ENZO LIFE SCIENCES

Popis: Recommended Applications: Flow Cytometry, IHC (PS)

Species reactivity: Human

Měrná jednotka: 1 * 100 µG

New Product Akce

Katalogové číslo: (ENZOENZABS1600100)

Dodavatel: ENZO LIFE SCIENCES

Popis: Recommended Applications: Flow Cytometry

Species reactivity: Human

Měrná jednotka: 1 * 100 µG

New Product Akce

Katalogové číslo: (ENZOENZABS1220100)

Dodavatel: ENZO LIFE SCIENCES

Popis: Recommended Applications: Flow Cytometry, IF, IHC

Species reactivity: Mouse

Měrná jednotka: 1 * 100 µG

New Product Akce

Katalogové číslo: (ENZOENZABS1510100)

Dodavatel: ENZO LIFE SCIENCES

Popis: Recommended Applications: Flow Cytometry

Species reactivity: Human

Měrná jednotka: 1 * 100 µG

New Product Akce

Katalogové číslo: (ENZOADISPA807E)

Dodavatel: ENZO LIFE SCIENCES

Popis: 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.

Měrná jednotka: 1 * 100 µG

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Dodavatel: ENZO LIFE SCIENCES

Popis: 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.

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Dodavatel: ENZO LIFE SCIENCES

Popis: 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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Dodavatel: ENZO LIFE SCIENCES

Popis: Cytochrome p450 is a highly conserved and diverse family of heme-containing proteins that function in the metabolism of numerous endogenous and exogenous substrates.

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Katalogové číslo: (ENZOADIMSA200E)

Dodavatel: ENZO LIFE SCIENCES

Popis: The thymidine analogue BrdU (5-Bromo-2-Deoxyuridine), a derivative of uridine, can substitute for thymidine during DNA synthesis.

Měrná jednotka: 1 * 100 µG

New Product Akce

Katalogové číslo: (ENZOALX804855C100)

Dodavatel: ENZO LIFE SCIENCES

Popis: Host: Mouse, Isotype: IgG1

Měrná jednotka: 1 * 100 µG

New Product Akce

Katalogové číslo: (ENZOALX805043C100)

Dodavatel: ENZO LIFE SCIENCES

Popis: Host: Mouse, Isotype: IgG1

Měrná jednotka: 1 * 100 µG

New Product Akce

Katalogové číslo: (ENZOALX805062C100)

Dodavatel: ENZO LIFE SCIENCES

Popis: Host: Mouse, Isotype: IgG1

Měrná jednotka: 1 * 100 µG

New Product Akce

Katalogové číslo: (ENZOALX805041C100)

Dodavatel: ENZO LIFE SCIENCES

Popis: Host: Mouse, Isotype: IgG1

Měrná jednotka: 1 * 100 µG

New Product Akce

Dodavatel: ENZO LIFE SCIENCES

Popis: Host: Mouse, Isotype: IgG1

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Dodavatel: ENZO LIFE SCIENCES

Popis: The tumor suppressor CYLD is a deubiquitinylating enzyme (DUB) that antagonises NF-κB and JNK signaling by disassembly of Lys63-linked ubiquitin chains synthesised in response to cytokine stimulation. The DUB activity of CYLD is mediated by its C-terminal ubiquitin specific protease (USP) domain, pathogenic truncations and mutations of which are associated with the hypertrophic skin tumor cylindromatosis through disruption of the USP domain and subsequent loss of CYLD catalytic activity.

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