5303 Results for: "Enzo Life Sciences"

Supplier: ENZO LIFE SCIENCES

Highly active

Supplier: ENZO LIFE SCIENCES

Produced in E. coli. Active catalytic domain of phosphodiesterase 10A.

Supplier: ENZO LIFE SCIENCES

Highly active

Supplier: ENZO LIFE SCIENCES

Produced in E. coli. Active recombinant matrix metalloproteinase-20 (MMP-20, enamelysin) cloned from human cDNA. The enzyme consists of residues Tyr108-Phe276 (NM_004771), which comprises the catalytic domain of human MMP-20, with a C-terminal purification tag. This represents a naturally-occurring active form of MMP-20 which lacks the C-terminal hemopexin domain.

Supplier: ENZO LIFE SCIENCES

Estrogen receptor ligand.

Supplier: ENZO LIFE SCIENCES

A potent, irreversible inhibitor of various plant β-glucosidases and mammalian glucocerebrosidase. Has been employed in in vitro and animal models for Gaucher’s disease. It raises intracellular levels of glucosylceramide by inhibiting glucosylceramidase.

Supplier: ENZO LIFE SCIENCES

Prostanoid receptor ligand.

Supplier: ENZO LIFE SCIENCES

Anti-Peptide tyrosine tyrosine Mouse Monoclonal Antibody [clone: 4]

Supplier: ENZO LIFE SCIENCES

Linear polyubiquitin chains are useful tools for investigating, amongst other things, the specificity and reactivity of deubiquitinylating enzymes (DUBs) and the recognition and interaction of linear polyubiquitin modified proteins with ubiquitin binding domain (UBDs) containing proteins.

Supplier: ENZO LIFE SCIENCES

Produced in baculovirus system

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For use in deubiquitinylating enzyme assays and linear polyubiquitin binding studies.

Supplier: ENZO LIFE SCIENCES

Produced in E. coli.

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DKK1 inhibitor

Supplier: ENZO LIFE SCIENCES

Produced in E. coli.

Supplier: ENZO LIFE SCIENCES

A potent and selective vanilloid receptor (TRPV1) antagonist. An effective antagonist of hTRPV1 when stimulated by capsaicin, acid, or noxious heat.

Supplier: ENZO LIFE SCIENCES

Disrupts Wnt signaling

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Probenecid

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Host: Hamster, Isotype: IgG1

Supplier: ENZO LIFE SCIENCES

Host: Mouse, Isotype: IgM

Supplier: ENZO LIFE SCIENCES

Host: Mouse, Isotype: IgG1

Supplier: ENZO LIFE SCIENCES

Host: Mouse, Isotype: IgG1

Supplier: ENZO LIFE SCIENCES

Synuclein was originally identified in Torpedo californica as a small neuroprotein that localized to the nuclear envelope of neurons and to presynaptic nerve termini. The human homolog was initially termed NACP, a precursor protein to NAC (Non-Ab Component), because of its prevalence in amyloid plaques in Alzheimer’s patients. Later, NACP was recognized as being alpha-Synuclein (alpha-SYN), a 14kDa protein, belonging to the synuclein family of phosphoproteins that also includes: betalpha-SYNuclein, gammalpha-SYNuclein, and synoretin.
alpha-SYN is recognized as a key component in the development and diagnosis of neurodegenerative synucleinopathic diseases (NSDs), such as Alzheimer’s and Parkinson’s disease. In the past five years, several genetic and post-translational modifications to alpha-SYN have been elucidated that have been linked to its collaboration in the formation of the classical Lewy bodies (LBs) or Lewy neurites that are associated with neurodegeneration. A study that shed more light on the neurogenesis of autorecessive synucleinopathies (ARSs) was the finding that alpha-SYN accumulation can occur due to mutations in the E3 ubiquitin ligase.
ARSs only account for a small percentage of NSD. Thus the illustration that alpha-SYN has a high susceptibility to tyrosine nitration may be the key component in understanding the formation of LBs. Due to the chemical structure of alpha-SYN, tyrosine nitration readily leads to the formation of oligomers via covalent O,O’-dityrosine bonds (cross-linking). Nitrosylated, wild-type, alpha-SYN products thus form SDS-insoluble, heat-stable aggregates in vitro that may account for alpha-SYN inclusions in all forms of NSDs.

Supplier: ENZO LIFE SCIENCES

Certain serine/threonine protein kinases, such as ASK1, RIP, DAP, and ZIP kinases, are mediators of apoptosis. Receptor interacting proteins including RIP and RIP2/RICK mediate apoptosis induced by TNF-R1 and Fas, two prototype members in the death receptor family. A member in the RIP kinase family was identified and designated RIP3. RIP3 contains an N-terminal kinase domain but, unlike RIP or RIP2, lacks the C-terminal death or CARD domain. RIP3 binds to RIP and TNF-R1, mediates TNF-R1 induced apoptosis, and attenuates RIP and TNF-R1 induced NF-κB activation. Overexpression of RIP3 induces apoptosis and NF-κB activation. The messenger RNA of RIP3 is expressed in a subset of adult tissues. Meanwhile RIP4 has been identified and initially characterized. These data suggest that RIP4 is involved in NF-κB and JNK signalling and that caspase-dependent processing of RIP4 may negatively regulate NF-κB-dependent pro-survival or pro-inflammatory signals.

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Mycotoxin.

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From herpes simplex virus type 1. Inactivated by 0.1% Triton X-100.

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From adenovirus type 40. Inactivated by 2 hours at 54°C.

Supplier: ENZO LIFE SCIENCES

Chemerin (tazarotene-induced gene 2; TIG2) is a chemotactic agent that was identified as the ligand for the orphan G protein-coupled receptor ChemR23. Chemerin has been shown to be expressed abundantly in adipose tissue and to function as a adipokine. Chemerin potentiates insulin-stimulated glucose uptake and regulates adipogenesis and adipocyte metabolism.

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Host: Mouse, Isotype: IgG1

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Host: Rat, Isotype: IgG2a

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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.