The Screen-Well® Wnt pathway library v 2.0 is a focused collection of 71 compounds with defined and diverse Wnt pathway activity, including activators and inhibitors of Wnts, Dishevelled, GSK-3β and other Wnt pathway kinases, TCF/β-catenin, DKK, LRP, Axin, Porcupine, and more. Compounds are dissolved in DMSO at 10 mM or 1 mM and aliquoted into deep-well plates at 100 or 500 µl per well. A variety of structurally and mechanistically different compound classes are included. A useful tool for studying the roles of pro- and anti-Wnt pathway molecules in cells as well as for use in in vitro applications.

Expand 4 Items

Anti-LAG3 Mouse Monoclonal Antibody

Supplier: ENZO LIFE SCIENCES

The lymphocyte activation gene-3 (LAG-3, CD223), a member of the immunoglobulin superfamily (IgSF) related to CD4, binds to the major histocompatibility complex (MHC) class II molecules but with higher affinity than CD4. Several alternative mRNA splice-variants of human LAG-3 have been described, two of them encoding potential secreted forms: LAG-3V1 (i.e. the D1-D2 domains of the protein, 36 kDa) and LAG-3V3 (D1-D3, 52 kDa). The longer form was detected by ELISA in the serum of healthy individuals as well as of tuberculosis patients with a favorable outcome. LAG-3 expression by T cell clones correlated with IFN-γ production, and hence soluble LAG-3 has been suggested as a serological marker of Th1 responses.

Expand 2 Items

Anti-LAG3 Mouse Monoclonal Antibody

Supplier: ENZO LIFE SCIENCES

Expand 2 Items

CHO Host Cell Protein Standards

Supplier: ENZO LIFE SCIENCES

Quantitative protein standards for Western blotting internal controls or ELISA standards.

Expand 2 Items

Human Recombinant HGF (from Insect cells)

Supplier: ENZO LIFE SCIENCES

Human Recombinant HGF (from Insect cells)

Expand 1 Items

10x Ubiquitinylation buffer

Supplier: Enzo Life Sciences

Assay Buffer from the Ubiquitinylation Kits. Packaged as 5×1 ml.

Expand 1 Items

Methanandamide ≥98% (by TLC)

Supplier: Enzo Life Sciences

Cannabinoid receptor ligand

Expand 2 Items

Anti-Cop9 Signalosome Csn1 Subunit Rabbit Polyclonal Antibody

Supplier: Enzo Life Sciences

The COP9 signalosome, once defined as a repressor complex of light activated development in Arabidopsis, has recently been found in humans and is probably present in most multicellular organisms. The COP9 signalosome is closely related to the lid sub-complex of the 26S proteasome in structural composition and probably shares a common evolutionary ancestor. A multifaceted role of the COP9 signalosome in cell-signalling processes is hinted at by its associated novel kinase activity, as well as the involvement of its subunits in regulating multiple cell-signalling pathways and cell-cycle progression. The molecular genetic studies in Arabidopsis suggest that the complex functions as part of a highly conserved regulatory network, whose physiological role in animals has yet to be determined. The COP9 signalosome, also known as the the COP9 complex and JAB1-containing signalosome, is a conserved nuclear protein complex found in plants and animals. It is composed of eight distinct subunits, designated S1 to S8 (very recently re-designated Csn1-Csn82) according to the molecular weight of the mammalian complex subunits. Subunit composition and the subunit sequences are substantially conserved between the mammalian and the plant complexes, implying that the complex has a conserved cellular function in higher eukaryotic organisms. Subunit 1 (Csn1) was previously identified as GPS1, which was isolated by its ability to rescue the lethality of a S. cerevisiae mutant deleted for the α-subunit of trimeric G protein. Transient expression of full length GPS1 in mammalian cells was shown to inhibit JNK1 and to repress JUN-dependent promoter activity. Csn1 shows homology to 19S proteasome regulatory subunit Rpn7 (S10a).

Expand 2 Items

Human recombinant IL-1beta (soluble) (fromE. coli)

Supplier: Enzo Life Sciences

Produced in E. coli. Human IL-1β (interleukin-1β) (aa 117-270) is fused to a linker peptide (10 aa) and an N-terminal FLAG®-tag.

Expand 4 Items

Phosphatase inhibitor library, Screen-Well®

Supplier: Enzo Life Sciences

The Screen-Well™ Phosphatase Inhibitor Library contains 33 known phosphatase inhibitors of well-defined activity. Inhibitors are supplied dissolved in DMSO at 10 mM and aliquoted into deep-well plates at either 100 µl or 500 µl per well. The library is ideal for chemical genomics, assay development, and as a reference set for secondary screening. Includes inhibitors of these important phosphatases: Calcineurin(PP2B), JSP-1, PRL-1, CD45, PP1, PRL-3, CDC25, PP2A, PTEN, and many more.

Expand 4 Items

Anti-Cop9 Signalosome Csn3 Subunit Rabbit Polyclonal Antibody

Supplier: Enzo Life Sciences

Host: Rabbit

Expand 2 Items

Anti-SPTAN1 Mouse Monoclonal Antibody

Supplier: Enzo Life Sciences

Fodrin, also referred to as non-erythroid (αII-; brain) spectrin, is a tetrameric (αγ)2 actin-binding, fibrous protein, widely distributed in vertebrates, which forms part of the sub-membranous cytoskeleton within many cell types including neurons, and is particularly abundant with axons. The α-subunits of fodrins and spectrin are highly conserved phylogenetically, with the exception of human α-fodrin, which shares only 55-59% homology with erythroid-specific α-spectrins. The β-subunits of spectrin (and γ-subunits of fodrins) are species specific. The interleukin-1 converting enzyme (ICE) family of proteases has been implicated as important effectors of the apoptotic pathway, perhaps acting hierarchically in a protease cascade. Neuronal fodrin is known to be cleaved by calpain following ischaemic insult and it has been proposed that calpain and an unidentified protease play a role in the onset of neuronal death following transient forebrain ischaemia. Recently, an ICE-like protease has been implicated in the early cleavage of fodrin, producing a 150kDa fragment, proximal to CPP32 in Fas-induced and C2-ceramide mediated apoptosis. A cleavage product of α-fodrin has been proposed as a candidate autoantigen in primary Sjögren’s syndrome and α-fodrin has been shown to be the source of a so-called ‘inhibitory protein factor’ family, members of which have been shown to inhibit both GABA and ATP-dependent glutamate uptake into purified synaptic vesicles.