"Enzo Life Sciences"

Supplier: Enzo Life Sciences

Membrin, also known as GS27 (Golgi SNARE of 27K), is an integral membrane protein present on the surface of the Golgi apparatus. GS27 is a member of a protein complex that consists of cis-Golgi vesicle receptor syntaxin 5 and GS28, v-SNARE rbet1 and Rsec22, and Rsly1. These complexes are postulated to direct the fusion of ER-derived vesicles with vesicular tubular cluster (VTC), and the fusion of VTCs to form cis-Golgi compartment.

Supplier: Enzo Life Sciences

Produced in E. coli.

Supplier: Enzo Life Sciences

A colorimetric immunometric ELISA kit for the rapid measurement of NGAL in dog samples

Supplier: Enzo Life Sciences

Monomeric G-protein Ras functions as a molecular switch linking receptor and nonreceptor tyrosine kinase activation to a number of downstream signaling pathways. Oncogenic mutations, which occur in approximately 30% of all cases of human cancer, lead to the stimulation of proliferation and the inhibition of apoptosis.

Supplier: Enzo Life Sciences

The mammalian PDI (Protein disulfide-isomerase) family encompasses several highly divergent proteins which are involved in the processing and maturation of secretory proteins in the endoplasmic reticulum by catalyzing the rearrangement of disulfide bonds.

Supplier: Enzo Life Sciences

Produced in E. coli.

Supplier: Enzo Life Sciences

Hsp65 is a member of the Hsp60 family of heat shock proteins isolated from Mycobacterium bovis BCG. Hsp65 from M. bovis is identical to that of M. tuberculosis, and similar to that of M. leprae, two highly pathogenic strains of mycobacterium. Hsp65 is the immunodominant antigen during mycobacterial infection and vaccination, and has been linked to the development of autoimmune adjuvant arthritis in rats.

Supplier: Enzo Life Sciences

Nuclear factor kappa-B (NFk) B) functions as a sequence specific transcriptional activator that binds to the intronic enhancer of kappa light chain gene in B lymphocytes. NF-kB is a heterodimer consisting of a 50 kDa DNA binding subunit (p50) and a 65 kDa transactivation subunit (p65/RelA) (ref. 3), both of which exhibit sequence homology to the protooncogene c-Rel. p50 has an isoform called p49/p52, and both proteins derive from the amino-terminal of precursor protein p105 and p100, respectively. The p50/p65 heterodimer remains in inactive form in the cytosol as a complex with its inhibitor, IkB. Upon stimulation of cells by a variety of stimuli, including lipopolysaccharide (LPS), pro-inflammatory cytokines like interleukin-1 and tumor necrosis factor, and viral infection, IkB becomes phosphorylated and degraded by the proteosome. The active NF-kB heterodimer translocates into the nucleus and induces gene expression.

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.

Supplier: Enzo Life Sciences

The 90 kDa molecular chaperone family includes 90 kDa heat shock protein Hsp90 and 94 kDa glucose-regulated protein grp94, both major molecular chaperones of the cytosol and the endoplasmic reticulum. Mammalian cells express inducible Hsp90 alpha and constitutive Hsp90 beta isoforms that are encoded by separate genes. The amino acid sequences of human and yeast Hsp90 alpha are 85% and 90% homologous to those of Hsp90 beta, respectively. All known members of the Hsp90 protein family are highly conserved, especially in the N-terminal and C-terminal regions containing independent chaperone sites with different substrate specificity. These ubiquitous and highly conserved proteins account for 1-2% of all cellular protein in most cells. Hsp90 functions as part of the cell's powerful network of chaperones to fight the deleterious consequences of protein unfolding caused by non-physiological conditions. In the absence of stress, however, Hsp90 provides a necessary component of such fundamental cellular processes as hormone signaling and cell cycle control by serving as a chaperone for many key signaling molecules including steroid receptors, cell cycle kinases involved in signal transduction, and p53. As many of these client proteins are known oncogenes, Hsp90 inhibitors such as 17-AAG, a geldanamycin analog, have been of benefit in the treatment of many cancers.

Supplier: Enzo Life Sciences

Highly sensitive PGE2 ELISA kit for inflammation and eicosanoid research.

Supplier: Enzo Life Sciences

For the quantitative determination of TXB2 in culture supernatants, plasma, serum, saliva, and urine from any species

Supplier: Enzo Life Sciences

Highly sensitive ELISA, detecting as low as 1.40pg/ml in just 3 hours.

Supplier: Enzo Life Sciences

For the quantitative determination of PGE1 in culture supernatants, plasma, serum, saliva, and urine from any species

Supplier: Enzo Life Sciences

For the quantitative determination of 17β-Estradiol in culture supernatants and saliva from any species

Supplier: Enzo Life Sciences

For the quantitative determination of 8-iso-PGF2α in culture supernatants, tissue, and urine from any species