You Searched For: Antibodies

Catalog Number: (CA200062-766)

Supplier: Enzo Life Sciences

Description: The 90kDa molecular chaperone family includes 90 kDa heat shock protein Hsp90 and 94 kDa glucose-regulated protein grp94, both major molecular chaperones of the cytosol and the endoplasmic reticulum. Mammalian cells contain isoforms Hsp90α and Hsp90β, encoded by separate genes. The amino acid sequences of human and yeast Hsp90-alpha are 85% and 90% homologous to those of Hsp90β , respectively. All known members of the Hsp90 protein family are highly conserved, especially in the N-terminal and C-terminal regions containing independent chaperone sites with different substrate specificity. These ubiquitous and highly conserved proteins account for 1-2% of all cellular proteins in most cells. Hsp90 functions as part of the cell’s powerful network of chaperones to fight the deleterious consequences of protein unfolding caused by non-physiological conditions. In the absence of stress, however, Hsp90 provides a necessary component of such fundamental cellular processes as hormone signaling and cell cycle control. In this context, researchers identified key regulatory proteins as substrates of Hsp90, including steroid receptors, cell cycle kinases involved in signal transduction, and p53. Hsp90 may act as a capacitor for morphological evolution by buffering widespread variation, potentially affecting morphogenic pathways. When temperature and other stress factors compromise Drosophila Hsp90 buffering, cryptic variant expression occurs, and selection can lead to the continued expression of these traits even after Hsp90 function is restored.

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: 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.

Supplier: Enzo Life Sciences

Description: Hsp70-Hsp90 Organizing Protein (HOP, p60) is an ~60kDa protein that is a critical intermediate component for the efficient maturation of steroid receptor complexes, serving to recruit Hsp90 to Hsp70-containing complexes. HOP contains three tetratricopeptide repeat (TPR) domains, TPR1, TPR2a, and TPR2b.

Catalog Number: (CA200062-418)

Supplier: Enzo Life Sciences

Description: Cleavage of heme b (Fe-protoporphyrin IX) at the a-methene carbon bridge to form the open tetrapyrrole, biliverdin IXa and carbon monoxide (CO) is catalyzed by heme oxygenase (HO) isozymes HO-1 and HO-2 (heme hydrogen-donor: oxygen oxidoreductase; EC 1.14.99.3). In mammalian species, biliverdin reductase (BVR; bilirubin: NAD(P)+ oxidoreductase; EC 1.3.1.24) converts the open tetrapyrrole to bilirubin. This pathway represents the only efficient way of making bilirubin and thereby deterring activation of oxygen by the heme molecule. HO-1 belongs to the heat shock protein family (Hsp32), while HO-2 takes a constitutive form expressed at exceedingly high levels in the brain and testes. The end products of the heme degradation process carry out important physiological activities. CO may act as a messenger in the brain and systemic organs stimulating cGMP-production through interactions with the heme-dependent form of guanylate cyclase. Bile pigments display potent antioxidant activity as well as effective antiviral activity against HIV and herpes virus. BVR is unique among all enzymes characterized to date in having two pH optima (6.8 and 8.7), using a different cofactor at each pH range (NADH at pH 7.0 and NADPH at pH 8.7). The enzyme displays pI and molecular mass microheterogeneity, apparently a result of post translational modifications. In rat, the enzyme also shows a tissue specific developmental pattern. BVR is not inactivated by heat shock, and its preexisting message is not sequestered from translation subsequent to thermal stress. Furthermore, reductase preserves microheterogeneity under thermal stress. BVR expression occurs not only in cells and brain regions that already display HO-1 and HO-2, but also in regions and cell types with potential to induce stress proteins. Rat cDNA for BVR has been isolated and characterized. The deduced protein contains 3 cysteine residues (Cys73, Cys281, and Cys290) involved in cofactor and substrate binding. Human BVR consists of a substantially longer polypeptide than the rat enzyme (41-42 kDa vs. 33 kDa), but also is dual cofactor and dual pH dependent, requires free SH groups for activity, and displays pI and molecular mass microheterogeneity. The human and rat BVR share some antigenic epitopes and show immunochemical cross reactivity.

Catalog Number: (CA200062-334)

Supplier: Enzo Life Sciences

Description: TAK1 (TGF-beta-activated kinase-1) is a 65 kDa serine/threonine kinase that is a member of the MAPKKK family. TAK1 is involved in the regulation of transcription by the TGF-beta super family, as its kinase activity is stimulated by TGF-beta and bone morphogenetic protein (BMP).

Supplier: Enzo Life Sciences

Description: Calreticulin (CRT) is a multifunctional, multi-compartmental protein most abundant in the ER lumen. CRT contains the ER-retrieval sequence, KDEL, and has been best characterized as a soluble molecular chaperone of new or misfolded proteins and a Ca2+- binding protein. Both CRT and its membrane bound homolog, Calnexin (CNX) interact with proteins and glycoproteins that have monoglucosylated N-glycans. The CRT/CNX cycle promotes correct folding, inhibits aggregation of folding intermediates, blocks premature oligimerization, regulates ER degradation, and provides quality control by preventing incompletely folded glycoproteins from exiting to the Golgi complex.

Supplier: Enzo Life Sciences

Description: Ubiquitin (Ub) plays a very important role in regulated non-lysosomal ATP dependent protein degradation. The protein to be degraded is conjugated to Ub and the ubiquinated protein is then selectively degraded by the 26S complex, a multicatalytic cytosolic and nuclear protease. The Ub-proteasome proteolytic pathway, which is a complex process, is implicated to be of great importance for regulating numerous cellular processes.

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.

SDS

Supplier: Enzo Life Sciences

Description: The tetrapeptide KDEL, located at the carboxy-terminal sequences of luminal proteins, is a retrieval motif essential for the precise sorting of these proteins along the secretory pathway. KDEL proteins perform essential functions in the endoplasmic reticulum (ER) related to protein folding as well as assembly. The localization of chaperones and other soluble proteins to the ER is achieved by their continuous retrieval from post-ER compartments by the KDEL receptor (Erd2p), which is a membrane protein localized in the Golgi apparatus.

Catalog Number: (89154-086)

Supplier: Enzo Life Sciences

Description: Host: Rat, Isotype: IgG2a

Catalog Number: (89154-094)

Supplier: Enzo Life Sciences

Description: Host: Rat, Isotype: IgG2a

Catalog Number: (89154-332)

Supplier: Enzo Life Sciences

Description: Host: Mouse, Isotype: IgG1

Catalog Number: (89154-288)

Supplier: Enzo Life Sciences

Description: Host: Mouse, Isotype: IgG2b

Catalog Number: (89154-348)

Supplier: Enzo Life Sciences

Description: Host: Rat, Isotype: IgG

Catalog Number: (89154-340)

Supplier: Enzo Life Sciences

Description: Host: Mouse, Isotype: IgG1