You Searched For: Enzo Life Sciences

Catalog Number: (CA200063-284)

Supplier: Enzo Life Sciences

Description: Anti-ESR Mouse Monoclonal Antibody [clone: h-151]

Catalog Number: (CA101106-530)

Supplier: Enzo Life Sciences

Description: Metabolism of inositol phospholipids by intracellular signaling mediators is fundamental to signal transduction in eukaryotic cells. PI-4,5-P2 (PIP2) can be synthesized by phosphorylation of PI-4-P by type I phosphatidylinositol phosphate kinase (PIP5K I), or phosphorylation of PI-5-P by type II PIPK (PIP4K II). PI-4,5-P2 regulation of cellular calcium levels involves its hydrolysis by Phospholipase C (PLC) to produce inositol 1,4,5-triphosphate (IP3) and diacylglycerol (DAG), which serve as second messengers in the import of calcium via IP3-sensitive ion channels and in the activation of PKC, respectively.

Supplier: Enzo Life Sciences

Description: Agrin is an essential extracellular matrix component which promotes clustering of nicotinic acetylcholine receptors (nAChRs) and other proteins during development at the neuromuscular junction. Agrin, MuSK and Rapsyn are all essential components for AChR aggregation through an unknown mechanism. The C-terminal region of agrin is released into the medium, interacts with receptors on the muscle surface, and induces AChR aggregation. The central region contains two O-linked glycosylation sites and a domain homologous to domain III of laminin. The N-terminal region anchors agrin to the extracellular matrix via other basal membrane components. This region also contains a protease inhibitor domain and glycosaminoglycan attachment sites, increasing the predicted MW from 200kDa to ~600kDa. The diagram shown indicates the domain structure and functional regions of agrin, as well as domains required for AChR aggregation and alpha-dystroglycan and heparin binding.  Various agrin isoforms are generated by alternative splicing at the X, Y and Z sites, and differ in the presence or absence of small inserts. The isoforms can determine the biological activity of agrin and their expression in specific tissues and stages of development. While no difference in functional activity has been detected between splicing variants at site X, insertion of a 4 aa peptide at site Y modestly increases agrins nAChR clustering activity. Insertion of an 8 aa peptide at splicing site Z increases the clustering activity of soluble rat agrin 10,000 fold.

Catalog Number: (CA200060-568)

Supplier: Enzo Life Sciences

Description: HGF/SF (Hepatocyte growth factor/Scatter factor) is a multifunctional heterodimeric polypeptide. It mediates the growth and scattering of various cell types, epithelial mesenchymal transition, the formation of tubules and lumens, and promotes angiogenesis. The ligand-receptor pair has also shown to be uniquely involved in most human solid tumors and to participate in tumor development, invasion, and metastasis.

Catalog Number: (CA200060-572)

Supplier: Enzo Life Sciences

Description: HGF/SF (Hepatocyte growth factor/Scatter factor) is a multifunctional heterodimeric polypeptide. It mediates the growth and scattering of various cell types, epithelial mesenchymal transition, the formation of tubules and lumens, and promotes angiogenesis. The ligand-receptor pair has also shown to be uniquely involved in most human solid tumors and to participate in tumor development, invasion, and metastasis.

Catalog Number: (CA200061-588)

Supplier: Enzo Life Sciences

Description: The caspases are a family of cysteine proteases that cleave after certain aspartate residues, and are primarily recognized as mediators of apoptosis. caspases are synthesized as inactive zymogens that can be cleaved to form active enzymes following the induction of apoptosis by stress or death receptors. Initiator caspases (e.g. caspase-8 and -10) are activated by dimerization of the zymogen on a dedicated adaptor protein. These activated initiator caspases in-turn cleave downstream effector or executioner caspases (e.g. caspase-3, -6, and -7) in a cascade-like manner, which cleave key cellular proteins that lead to the morphological changes associated with apoptotic cell death.

Supplier: Enzo Life Sciences

Description: Transferrin is a serum glycoprotein involved in iron transport. Transferrin exists in two forms, the iron-free Apotransferrin, which binds two Fe3+ ions to generate Ferrotransferrin. Apotransferrin remains tightly bound to its receptor until the complex is recycled to the cell surface, where Apotransferrin is released into the extracellular space to recruit more Fe3+ ions.

SDS

Supplier: Enzo Life Sciences

Description: The polo-like kinases (PLKs) function in cell-cycle progression and in multiple stages of mitosis. PLK1 is activated by phosphorylation of Thr210 at the G2/M phase boundary. Active PLK1 participates in mitotic entry through activation of Cdc25C and nuclear import of cyclin B1, thereby activating the Cdc2/cyclin B kinase.

Supplier: Enzo Life Sciences

Description: Actin is one of the major proteins (~42 kDa) of the cytoskeleton. It regulates contractile potential in muscle tissues and helps to control the shape as well as the motility of non-muscle cells. Actin is expressed in all eukaryotic cells which makes it a useful loading control in Western blotting experiments. In higher eukaryotes, there are six isoforms of actin: Three alpha-actins (α-skeletal, α-cardiac, α-smooth muscle), one β-actin (β-non-muscle) and two γ-actins (γ-smooth muscle and γ-non-muscle). Actin isoforms show >90% overall sequence homology.

Catalog Number: (CA101410-452)

Supplier: Enzo Life Sciences

Description: The Insulin Receptor (InsR) is a heterodimeric receptor tyrosine kinase with an extracellular alpha-chain, a transmembrane domain and an intracellular beta-chain. InsR is activated upon binding of the peptide hormone insulin, leading to autophosphorylation of tyrosine residues 1146, 1150, and 1151 in the activation loop of the beta-chain. Additional autophosphorylation sites such as tyrosine residues 960, 972, 1316, and 1322 regulate the assembly of signal transduction complexes.

Supplier: Enzo Life Sciences

Description: Hsp27 is one of the most common members of the highly conserved and ubiquitously expressed family of small heat shock proteins (sHsp), which also includes alphaB-crystallin. It is characterized by a conserved C-terminal alpha-crystallin domain consisting of two anti-parallel beta-sheets that promote oligomer formation required for its primary chaperone function as inhibitor of irreversible protein aggregation. Hsp27 oligomerization is modulated by post-translational phosphorylation of Hsp27 at three serine residues, Ser15, Ser78, and Ser82, by a variety of protein kinases including MAPKAPK-3, PKAc-alpha, p70 S6K, PKD I, and PKC-delta. Hsp27 has been shown to inhibit actin polymerization by binding of unphosphorylated Hsp27 monomers to actin intermediate filaments. Anti-apoptotic functions of Hsp27 have also been identified through interactions with DAXX7, activation of Akt, and inhibition of apoptosome formation. Evidence suggests altered expression of Hsp27 is implicated in the pathogenesis of breast, ovarian, and prostate cancer.

Supplier: Enzo Life Sciences

Description: Alpha-crystallins, which are part of the small Heat shock family members, are major water-soluble proteins present in the lens of the mammalian eye. Phosphorylation of serine residues which occurs during development and in response to stress, is intimately linked with its function. Chaperone activity requires, and is modulated by, oligomerization and is limited to binding unfolded intermediates to prevent irreversible aggregation.

Supplier: Enzo Life Sciences

Description: 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.

Supplier: Enzo Life Sciences

Description: Anti-KDEL Mouse Monoclonal Antibody [clone: 10C3]

Supplier: Enzo Life Sciences

Description: 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.

SDS

Catalog Number: (CA95043-696)

Supplier: Enzo Life Sciences

Description: Concentrated lysis buffer for preparation of cell and tissue extracts.