"Enzo Life Sciences"

Supplier: Enzo Life Sciences

Ultra-pure; stabilizes microtubules

Supplier: Enzo Life Sciences

Host: Mouse, Isotype: IgM

Supplier: Enzo Life Sciences

Host: Mouse, Isotype: IgG2a lambda

Supplier: Enzo Life Sciences

FITC-labelled recombinant human annexin V fusion protein (produced in E. coli) shows bright green fluorescence (Ex(max): 488 nm; Em(max): 530 nm).

Supplier: Enzo Life Sciences

Non-ionic, glucose based very mild detergent for membrane protein purification.

Supplier: Enzo Life Sciences

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.

Supplier: Enzo Life Sciences

Produced in insect cells. Full length active enzyme.

Supplier: Enzo Life Sciences

Host: Mouse, Isotype: IgG1

Supplier: Enzo Life Sciences

Produced in Drosophila Schneider 2 (S2) cells. Recombinant human hepsin (aa 45-417) is fused at the C-terminus to a V5-His-tag.

Supplier: Enzo Life Sciences

The Stress-activated protein kinases alpha and gamma (SAPKalpha and gamma), also known as c-Jun NH2-terminal kinases 1 and 2 (Jnk1/2) are serine/ threonine protein kinases belonging to the MAP kinase family. The extracellular stimuli leading to cell stress include inflammatory cytokines (via Rho and Rac), growth factors, protein synthesis inhibitors and osmotic stress amongst others. Both Jnk1 and Jnk2 must be dually phosphorylated in the activation loop, at threonine 183 and tyrosine 185, to achieve full enzymatic activity.

Supplier: Enzo Life Sciences

Ubiquitin (Ub) plays a very important role in regulated non-lysosomal ATP dependent protein degradation. The protein to be degraded is conjugated to Ub and the ubiquinated protein is then selectively degraded by the 26S complex, a multicatalytic cytosolic and nuclear protease. The Ub-proteasome proteolytic pathway, which is a complex process, is implicated to be of great importance for regulating numerous cellular processes.

Supplier: Enzo Life Sciences

TLR4 activator.

Supplier: Enzo Life Sciences

Green 496 [5-Fluorescein] dUTP can replace TTP in reactions in which it serves as a substrate for E. coli DNA polymerase (holoenzyme and Klenow fragment), T4 and Taq DNA polymerases, reverse transcriptase (from AMV and M-MuLV) and terminal transferase.

Supplier: Enzo Life Sciences

Inhibitor of TNF-alpha processing

Supplier: Enzo Life Sciences

TRIP-Br1 (SEI-1) functions as physiological integrator of transcriptional regulatory signals at E2F-responsive promoters to ensure proper execution of E2F-dependent cell cycle progression. TRIP-Br1 is defined as an oncogene.

Supplier: Enzo Life Sciences

Insulin-like growth factor-I (IGF-I) is a polypeptide hormone similar in structure to insulin. It is involved in regulation of neuronal growth and development in the central and peripheral nervous system. IGF-1 is a potent inhibitor of apoptosis in neurons, and activates the Akt signaling pathway via the IGF-1R and Insulin receptors. The IGF-1R acts as a receptor for IGF-1 and the related IGF-2, and is subject to autophosphorylation on multiple tyrosine residues that regulate receptor activation and assembly of signal transduction complexes.