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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.

Catalog Number: (95038-978)

Supplier: Enzo Life Sciences

Description: The nucleosome is made up of four core histone proteins (H2A, H2B, H3 and H4) and is the primary building block of chromatin. The core histones form an octamer, which is made up of one H3-H4 tetramer and two H2A-H2B dimers. The N-terminal tail of core histones undergoes different post-transcriptional modifications including acetylation, phosphorylation, methylation and ubiquitination. These modifications occur in response to cell signal stimuli and have a direct effect on gene expression.

Catalog Number: (95042-192)

Supplier: Enzo Life Sciences

Description: 31472488

SDS

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.

Catalog Number: (95053-544)

Supplier: Enzo Life Sciences

Description: Glucagon-like peptide-1 (9-36) amide and GLP-1 (9-37) are the forms of GLP-1 which result from rapid degradation of the active forms of the peptide (GLP-1 (7-36) amide and GLP-1 (7-37)) by the enzyme dipeptidyl peptidase-IV (DPP-IV, also known as CD26 or adenosine deaminase binding protein). GLP-1 is a peptide hormone of the glucagon family, produced by the L cells of the intestinal mucosa from the same prohormone as glucagon. The active forms are potent stimulators of glucose-dependent insulin secretion. The sequence of GLP-1 is fully conserved in all mammalian species examined so far.

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.

Catalog Number: (101106-530)

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: 31472488

Catalog Number: (95038-974)

Supplier: Enzo Life Sciences

Description: Cyclins are a family of proteins which function as the regulatory subunits of cyclin/cyclin-dependent kinase (Cdk) holoenzymes, mediating entry into and progression through the cell cycle. Each cyclin is expressed in a temporal fashion during the cell cycle, partnering with a specific Cdk to activate its protein kinase activity. The most well defined mitotic cyclins are: cyclin D, which partners with cdks 4 and 6 during early G1 phase; cyclin E, which activates Cdk2 in the G1 to S phase transition; cyclin A, which utilizes Cdks 1 and 2 during progression through S phase and into G2; and cyclin B, which activates Cdk1 in M-phase promotion.

Catalog Number: (95043-918)

Supplier: Enzo Life Sciences

Description: Stats (Signal transducers and activators of transcription) are a family of cytoplasmic latent transcription factors that are activated to regulate gene expression in response to a large number of extracellular signaling polypeptides including cytokines, interferons, and growth factors. After phosphorylation by JAK tyrosine kinases, Stats enter the nucleus to regulate transcription of many different genes.

Supplier: Enzo Life Sciences

Description: The Hsp60 of Heliothis viescens belongs to a highly conserved family of molecular chaperones from several species, including plant Hsp60 (known as Rubisco binding protein), GroEL, the E.coli Hsp60, and 65 kDa major antigen of mycobacteria. In eukaryotes, Hsp60 is localized in the mitochondrial matrix, and in plants Hsp60 is localized in the chloroplast. Mitochondria, chloroplasts and bacteria share a common ancestry (>1 billion years), and this coupled with the high degree of homology between the divergent Hsp60s suggests that these proteins perform a primitive but vital function similar to all the different species. The common characteristics shared by the Hsp60s from the divergent species include high abundance; induction with environmental stress such as heat shock; homo-oligomeric structures of either 7 or 14 subunits which reversibly dissociate in the presence of Mg2+ and ATP; ATPase activity; and a role in folding and assembly of oligomeric protein structures. Studies support these similarities, showing expression of the single-ring human mitochondrial homolog Hsp60 with its co-chaperonin Hsp10, in a E. coli strain engineered so that the groE operon remained under strict regulatory control. The findings demonstrate that expression of Hsp60-Hsp10 enabled successful performance of all essential in vivo functions of GroEL and its co-chaperonin, GroES. Consistent with their functions as chaperones, Hsp60 and Hsp10 may act as docking molecules with a passive role in the maturation of caspase processing. Data incidates that recombinant Hsp60 and Hsp10 accelerate the activation of procaspase-3 by cytochrome c and dATP in an ATP-dependent manner. Hsps are intracellular proteins thought to serve protective functions against infection and cellular stress; however, several studies reveal a possible link between members of the Hsp60 and a number of autoimmune diseases, atherosclerosis, and chlamydial disease.

SDS

Catalog Number: (200060-572)

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: (200063-284)

Supplier: Enzo Life Sciences

Description: 31472488

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

Supplier: Enzo Life Sciences

Description: Produced in <i>E. coli.</i> Contains 179 amino acids.