You Searched For: Enzo Life Sciences

Supplier: Enzo Life Sciences

Description: GroEL and GroES are E. coli chaperonins, which are homologs of mitochondrial chaperonins Hsp60 and Hsp10. GroEL is a double toriodal assembly of 14 identical subunits which form two heptameric rings stacked back-to-back, with a cavity at each end. GroEL and its co-chaperonin GroES facilitate protein folding with an ATP-dependent mechanism.

Supplier: Enzo Life Sciences

Description: TCP-1 alpha is a 60 kDa subunit of a cytosolic hetero-oligomer chaperone that is known to be involved in the folding of Actin and Tubulin. This protein is a member of the Chaperonin family, which includes E. coli GroEL, the mitochondrial Heat-shock protein Hsp60, the plastid Rubisco-subunit-binding protein, and the archaebacterial protein TF55. These Chaperonins assist the folding of proteins upon ATP hydrolysis.

Catalog Number: (CA200062-174)

Supplier: Enzo Life Sciences

Description: The casein kinases are serine/threonine protein kinases involved in the regulation of multiple cell signaling pathways. There are at least seven identified mammalian isoforms in the casein kinase I (CKI) family, which are monomeric and function in cell growth and the replication and repair of DNA. Casein kinase II (CK2) is a ubiquitous tetrameric holoenzyme comprised of two catalytic alpha subunits and two regulatory beta subunits. CK2 enzymes are known to regulate metabolic signal transduction, transcription, and translation.

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: (CA200062-088)

Supplier: Enzo Life Sciences

Description: The eukaryotic translation initiation factors (eIFs) regulate translation at the level of messenger RNA engagement by the ribosome. eIF-2alpha promotes the binding of the initiator tRNA to 40S ribosomal subunits, and is a key signaling component of the unfolded protein response (UPR). eIF-4E recruits mRNAs to the eIF4F complex through binding of their 5 N7-methylguanosine cap. eIF-4E binding proteins-1 and -2 are translational repressors, sequestering eIF-4E in conditions of low cellular demand for translation. Their dissociation from eIF-4E is regulated by phosphorylation in response to growth-promoting stimuli.

Catalog Number: (CA200063-162)

Supplier: Enzo Life Sciences

Description: The Rab family of GTP-binding proteins are members of the Ras superfamily of small G proteins, and participate in multiple steps of the membrane trafficking. Rab3A participates in the fusion of synaptic vesicles during neurotransmitter release, a process regulated by GDP/GDP exchange cofactors such as GAP, GDI, GRF, and rabphilin. Rab4 regulates recycling of proteins from the early endosome to the surface of many cell types, regulating glucose transporter and transferrin receptor cell surface localization. Rab5 regulates the fusion of plasma membrane-derived clathrin-coated vesicles with early endosomes and homotypic fusion among early endosomes.

Supplier: Enzo Life Sciences

Description: Calnexin (CNX), an unglycosylated resident ER transmembrane protein, together with Calreticulin (CRT), plays a key role in glycoprotein folding and its control within the ER, by interacting with folding intermediates via their monoglucosylated glycans. Calnexin associates with newly synthesized monomeric glycoproteins and only recognizes glycoproteins when they are incompletely folded. Furthermore, Calnexin has been demonstrated to function as a molecular chaperone capable of interacting with polypeptide segments of folding glycoproteins.

Supplier: Enzo Life Sciences

Description: The Hsp70 family of heat shock proteins contains multiple homologs ranging in size from 66-78 kDa, and are the eukaryotic equivalents of the bacterial DnaK. The most studied Hsp70 members include the cytosolic stress-induced Hsp70 (Hsp72), the constitutive cytosolic Hsc70 (Hsp73), and the ER-localized BiP (Grp78). Hsp70 family members contain highly conserved N-terminal ATP-ase and C-terminal protein binding domains. Binding of peptide to Hsp70 is assisted by Hsp40, and stimulates the inherent ATPase activity of Hsp70, facilitating ATP hydrolysis and enhanced peptide binding. Hsp70 nucleotide exchange and substrate binding coordinates the folding of newly synthesized proteins, the re-folding of misfolded or denatured proteins, coordinates trafficking of proteins across cellular membranes, inhibits protein aggregation, and targets the degradation of proteins via the proteasomal pathway.

Supplier: Enzo Life Sciences

Description: Synaptotagmins (Syt) are membrane-trafficking proteins characterized by an N-terminal transmembrane region, a variable linker, and two C-terminal C2-domains, C2A and C2B. At least twelve Synaptotagamins are expressed in vertebrates and can be found in both vesicular and plasma membranes.

Catalog Number: (CA200062-876)

Supplier: Enzo Life Sciences

Description: Postsynaptic density protein 95 kDa (PSD-95), also known as Synapse associated protein 90 kDa (SAP90), is a brain specific protein that is highly similar to the Drosophila dlg tumor suppressor protein. PSD-95 is a member of membrane associated proteins that are localized beneath the postsynaptic membrane of synapses in the CNS. PSD-95 interacts with NMDA receptor and Shaker-type K+ channels and contributes to their clustering and localization at the synaptic spines in hippocampal neurons and the pinceau terminal of cerebellar basket cells, respectively.

Catalog Number: (CA200062-934)

Supplier: Enzo Life Sciences

Description: Syntaxins are type II integral membrane proteins localized to membranes that regulate vesicle transport, protein maturation, and exocytosis. Syntaxin 1A resides in the nerve terminals of sensory neurons and nerve fibers reaching small blood vessels. Syntaxin 2 localizes to the apical plasma membrane and regulates epithelial-mesenchymal interactions. Syntaxin 6 is primarily localized to the trans-Golgi network, and partially co-localizes with AP-1 on clathrin-coated membranes. Syntaxin 13 is ubiquitously expressed and localizes to the tubular early and recycling endosomes, as well as endosomal vacuoles.

Catalog Number: (CA95045-894)

Supplier: Enzo Life Sciences

Description: Anti-AGRN Mouse Monoclonal Antibody [clone: Agr-33]

Supplier: Enzo Life Sciences

Description: PKA (Protein Kinase A), also known as cAMP-dependent protein kinase, phosphorylates serine or threonine residues in target protein in response to elevated levels of cAMP. Inactive PKA exists as a tetrameric protein composed of two regulatory (R) subunits and two catalytic (C) subunits. Activation occurs when two cAMP molecules bind to each R subunit which causes a conformational change that releases the active C subunits.

Catalog Number: (CA95045-850)

Supplier: Enzo Life Sciences

Description: Lysine-specific demethylase 1 (LSD1, AOF2, BHC110) is a nuclear amine oxidase homolog, and was the first such protein to display definitive activity in epigenetic modulation as a histone demethylase. LSD1 demethylates histone H3 at mono- or di-methylated lysine residues. Depending on associated co-factors, LSD1-mediated demethylation can lead to transcriptional repression or activation.

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: The Hsp70 family of heat shock protiens contains multiple homologs ranging in size from 66-78 kDa, and are the eukaryotic equivalents of the bacterial DnaK. The most studied Hsp70 members include the cytosolic stress-induced Hsp70 (Hsp72), the constitutive cytosolic Hsc70 (Hsp73), and the ER-localized BiP (Grp78). Hsp70 family members contain highly conserved N-terminal ATP-ase and C-terminal protein binding domains. Binding of peptide to Hsp70 is assisted by Hsp40, and stimulates the inherent ATPase activity of Hsp70, facilitating ATP hydrolysis and enhanced peptide binding. Hsp70 nucleotide exchange and substrate binding coordinates the folding of newly synthesized proteins, the re-folding of misfolded or denatured proteins, coordinates trafficking of proteins across cellular membranes, inhibits protein aggregation, and targets the degradation of proteins via the proteasomal pathway.