You Searched For: SAFE AND SURE NEDERLAND B.V.

Catalog Number: (10135-964)

Supplier: Enzo Life Sciences

Description: Rapid, reliable method to isolate nucleic acid-free nuclear proteins in mammalian cells and tissues.

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Catalog Number: (10033-760)

Supplier: Enzo Life Sciences

Description: 32238807

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Catalog Number: (10014-642)

Supplier: Enzo Life Sciences

Description: 0.44

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Catalog Number: (10051-968)

Supplier: Enzo Life Sciences

Description: BID is an approximately 22 kDa protein belonging to the Bcl-2 family. BID is a cytosolic protein that is cleaved by caspase-8 in response to death receptor stimulation. Proteolytic cleavage of BID results in the formation of a 15 kDa fragment, referred to as tBID. tBID migrates to the mitochondria where it aids in the release of cytochrome c and the subsequent activation of the apoptosome. tBID serves as a link between death receptor dependent and mitochondrial mediated apoptosis.

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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.

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: 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.

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Catalog Number: (200061-588)

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.

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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: 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.

Catalog Number: (200063-284)

Supplier: Enzo Life Sciences

Description: Used in Immunoprecipitation, Western blot with species reactivity to Human.

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Catalog Number: (101410-452)

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.

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Catalog Number: (95043-776)

Supplier: Enzo Life Sciences

Description: Glucose-regulated protein 94 (Grp94, gp96), an abundant resident endoplasmic reticulum (ER) lumenal stress protein, belongs to the Hsp90 family of molecular chaperones along with cytosolic Hsp90. Grp94 and such other resident soluble proteins of the ER as the Ca 2+ binding protein subfamily (CaBP, CaBPI, CaBP2 and calreticulin) possess the C-terminal tetrapeptide Lys-Asp-Glu-Leu (KDEL), a sorting signal considered responsible for the retention of these proteins in the pre-Golgi compartments. Stress conditions such as glucose starvation and heat shock which promote protein misfolding or unfolding increase Grp94 expression. In addition to a homeostatic role in protein folding and assembly, Grp94 can function in the intracellular trafficking of peptides from the extracellular space to the MHC class I antigen processing pathway of antigen presentation cells. Grp94 and Hsp90 share high sequence identity and apparently identical adenosine nucleotide dependent modes of regulation, although previous data suggests that Hsp90 and Grp94 may differ in their nucleotide binding properties. The N-terminal domain of eukaryotic Hsp90 proteins contains a conserved adenosine nucleotide binding pocket which also serves as the binding site for the Hsp90 inhibitors geldanamycin and radicicol. However, the molecular basis for adenosine nucleotide-dependent regulation of Grp94 remains unclear. Data supports a ligand dependent regulation of Grp94 function, and suggests a model whereby Grp94 function is regulated through a ligand -dependent conversion of Grp94 from an inactive to an active conformation.

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Catalog Number: (76285-038)

Supplier: Enzo Life Sciences

Description: Recombinant monclonal antibody (Human IgG1κ).

Recommended Applications: Flow Cytometry, WB, FUNC

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Catalog Number: (76002-744)

Supplier: Enzo Life Sciences

Description: Recommended Applications: WB

Species reactivity: Human

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Catalog Number: (10049-568)

Supplier: Enzo Life Sciences

Description: Primary Antibody, Used in WB with species reactivity to Mouse, Rat, Host: Rabbit, Immunogen: Synthetic peptide corresponding to aa 643-654 (T643GEEDTSEKDEL654) of rat BiP (GRP78; glucose regulated protein 78kDa)

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