You Searched For: Methyl+3-ethoxythiophene-2-carboxylate

Supplier: Peprotech

Description: IL-6 is a pleiotropic cytokine that plays an important role in host defense by regulating immune and inflammatory responses. Produced by T cells, monocytes, fibroblasts, endothelial cells and keratinocytes, IL-6 has diverse biological functions. It stimulates B cell differentiation and antibody production, synergizes with IL-3 in megakaryocyte development and platelet production, induces expression of hepatic acute-phase proteins, and regulates bone metabolism. IL-6 signals through the IL-6 receptor system that consists of two chains, IL-6Rα and gp130. Murine IL-6 is inactive on human cells, while both human and murine are equally active on murine cells. Recombinant Rat IL-6 is a 21.7 kDa protein containing 188 amino acid residues.

Catalog Number: (10088-020)

Supplier: Proteintech

Description: HABP2 is also named as HGFAL, PHBP and belongs to the peptidase S1 family. It can activate coagulation factor VII and prourokinase and release the vasoactive peptide bradykinin by cleaving kininogen and is an important role in the regulation of the haemostasis system as well as fibroproliferative inflammatory processes . HABP2 is present as the 70 kDa inactive single chain precursor in human plasma and transforms to the active two chain form, 50 kDa heavy chain and 27 kDa light chain,and the 50 kDa heavy chain changes to two 26 kDa fragments, and 27 kDa light chain to 17 kDa and 8 kDa fragments, which are all bridged by disulfide linkages, by autocleavage.

Catalog Number: (10477-950)

Supplier: Bioss

Description: FAM50A, also known as DXS9928E, HXC26, XAP5 or 9F, is a 339 amino acid nuclear protein that belongs to the FAM50 family. Expressed ubiquitously with highest expression in fetal kidney, liver and brain, as well as adult heart, spleen, skeletal muscle, prostate and small intestine, FAM50A is thought to function as a transcription factor that may bind to DNA. FAM50A contains an SV40 large T antigen nuclear localization signal and a polymorphic CCG repeat region in its 5’-UTR. Defects in the gene encoding FAM50A may be associated with acute lymphoblastic leukemia, suggesting a possible role for FAM50A in carcinogenesis.

Catalog Number: (89162-330)

Supplier: Enzo Life Sciences

Description: Studies have demonstrated that PR39, a proline/arginine rich 39 amino acid antibacterial peptide originally derived from porcine bone marrow, exhibits a broad spectrum of biological activities, including the ability to induce angiogenesis and to limit inflammatory damage in a variety of animal models. The angiogenic effect is in part explained by the ability of PR39 to inhibit proteasome-dependent degradation of the transcription factor HIF-1a, while anti-inflammatory activity is associated with inhibition of IκBα degradation that in turn prevents activation of NFκB-dependent gene expression. The activities of PR39 reside in the N-terminal portion of the molecule encompassed by PR11. The most recent findings have demonstrated that PR39 is a non-competitive and reversible inhibitor of the proteasome function, which is achieved by a unique allosteric mechanism allowing for specific inhibition of degradation of selected proteins without affecting total proteasome-dependent proteolysis. A proline-arginine-rich 11 amino acid peptide derived from the naturally occurring peptide antibiotic PR39. PR39 has been shown to act as an inhibitor of both 20S and 26S proteasomes with proposed selectivity for the inhibition of the degradation of IκBα, HIF-1a and certain other proteins. PR39 has been reported to inhibit the proteasomal degradation of IκBα without effecting overall proteasome activity, or degradation of p21Cip1/Waf1 and c-fos, cell-cycle genes regulated by proteasome-dependent degradation. In vitro studies have demonstrated PR39 to be an efficient inhibitor of all three activities of the 20S proteasome. Unlike MG132 and lactacystin, long-term exposure to PR39 shows little toxicity or induction of HSP-70. In mouse models of myocardial infarction it has been shown that infusion with PR11 results in a significant reduction of myocardial infarct size. PR39, PR11 and related peptides may therefore provide novel means to regulate cellular function and the control of NF-κB-dependent gene expression for therapeutic purposes.

Catalog Number: (10085-876)

Supplier: Proteintech

Description: DKK1, also named a SK and Dickkopf-1, belongs to the dickkopf family. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease. SDS-PAGE and Western blot analysis demonstrated that DKK1 is expressed as a 35-kD doublet protein, which is larger than the deduced molecular mass of 26 kD. Sometime DKK1 is expressed as a 42- to 50-kD secreted protein, with little change observed after glycanase treatment.

Catalog Number: (10095-280)

Supplier: Proteintech

Description: STBD1 may have the capability to bind to carbohydrates. It functions as a glycogen receptor that tethers glycogen to autophagic membranes for delivery and breakdown in lysosomes. STBD1 appears molecular mass of 35-38 kDa band in mouse/rat tissues and 38-43 kDa in human tissue.

Catalog Number: (10090-914)

Supplier: Proteintech

Description: NQO1, also named as DIA4, NMOR1, DTD and QR1, belongs to the NAD(P)H dehydrogenase (quinone) family. This enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinons involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. It is known to be involved in benzene metabolism. In human studies of ozone exposure, polymorphisms in oxidative stress genes (NQO1, GSTM1, GSTP1) modify respiratory symptoms, lung function, biomarkers and risk of asthma. This antibody recognizes all the three isoforms (26-27 kDa and 31 kDa) of NQO1 and the homo-dimer form (66-70 kDa) of NQO1.

Catalog Number: (10092-856)

Supplier: Proteintech

Description: PRSS8(protease, serine, 8) displays trypsin-like enzymatic activities by hydrolyzing peptidyl fluorogenic substrates such as D-Pro-Phe-Arg-AMC. This trypsinlike enzymatic activity can be inhibited by aprotinin, antipain, leupeptin, and benzamidine. It is a heterodimer of two chains, light and heavy, which are held by a disulfide bond. PRSS8 is also named as CAP1 and belongs to the peptidase S1 family.

Supplier: Enzo Life Sciences

Description: The 70 kDa heat shock protein Hsp70 belongs to the Hsp70 family of highly-related protein isoforms ranging in size from 66 kDa to 78 kDa. Hsc70 shares close biochemical and biological ties to Hsp70, and also belongs to the Hsp70 family. These proteins include cognate members found within major intracellular compartments and highly inducible isoforms predominantly cytoplasmic or nuclear in distribution. Members of the Hsp70 family function as molecular chaperones involved in such cellular functions as protein folding, transport, maturation and degradation, operating in an ATP-dependent manner. The molecular chaperones of the Hsp70 family recognize and bind to nascent polypeptide chains or partially folded intermediates of proteins, preventing their aggregation and misfolding, and the binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein. Data demonstrates that with a ubiquitin-like domain at its amino terminus and its association with the 26S proteosome in HeLa cells, Bag-1 modulates the chaperone activity of Hsc70 and Hsp70. These findings reveal Bag-1's role as a physical link between the Hsc70/Hsp70 chaperone system and the proteasome. Experimental data also shows that the ATPase domain and the substrate-binding domain of Hsp70 (or Hsc70) cooperate to form a co-chaperone-chaperone complex with the synaptic vesicle cysteine string protein (csp), essential for normal neurotransmitter release.

Catalog Number: (10082-232)

Supplier: Proteintech

Description: Ubiquitin is most famous for its function in targeting proteins for degradation by the 26S proteasome, ubiquitin needs to be attached to a substrate in chains (polyubiquitylation) before being recognized by proteasome. Similarly, SUMO (small ubiquitin-related modifier) can be linked to substrates in chains (polysumoylation), SUMO modification has been implicated in many important cellular processes including the control of genome stability, signal transduction, targeting to and formation of nuclear compartments, cell cycle and meiosis. There are 4 confirmed SUMO isoforms in human, SUMO-1, SUMO-2, SUMO-3 and SUMO-4. SUMO-2 and SUMO-3 are nearly identical but are distinct from SUMO-1. SUMO2/3 conjugation was recently widely involved in neuroprotective activities. A substitution (M55V) of SUMO4 was strongly associated with the pathogenesis of type 1 diabetes (T1D) involving NF kappa B related mechanisms.

Catalog Number: (10750-172)

Supplier: Prosci

Description: CSN8 Antibody: The COP9 signalosome (CSN) is an evolutionarily conserved protein complex of the eight subunits that interacts with deubiquitinating enzymes and protein kinases and is highly homologous to the lid sub-complex of 26S proteasome. The CSN complex is an essential regulator of the ubiquitin conjugation pathway by mediating the deneddylation of the SCF-type E3 ligase complexes, which leads to a decrease in ubiquitin ligase activity of SCF-comlpexes such as SCF, CSA or DDB2. It is also involved in phosphorylation of p53, c-jun/JUN, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN8 encodes the smallest and the least conserved but first identified subunit of CSN. Recent studies show CSN8 is essential for Drosophila development and is essential for peripheral T cell homeostasis and antigen receptor-induced entry into the cell cycle from quiescence.

Catalog Number: (10084-298)

Supplier: Proteintech

Description: CD22, also known as Siglec-2 (sialic acid binding Ig-like lectin 2) or BL-CAM (B-lymphocyte cell adhesion molecule), is a 130-140 kDa, B-cell restricted, type I transmembrane glycoprotein belonging to the immunoglobulin gene superfamily. The expression of CD22 is developmentally regulated. It is expressed at low levels in the cytoplasm of pro-B and pre-B cells and present on the cell surface only at mature stages of B-cell differentiation. Cell surface expression is lost during terminal differentiation into plasma cell and after B-cell activation. CD22 is an inhibitory receptor for B-cell receptor (BCR) signalling, preferentially binds to alpha-2,6-linked sialic acid and mediates B-cell B-cell interactions. It plays a crucial role in activation and differentiation of the B-cell.

Supplier: Enzo Life Sciences

Description: The 70 kDa heat shock protein Hsp70 belongs to the Hsp70 family of highly-related protein isoforms ranging in size from 66 kDa to 78 kDa. Hsc70 shares close biochemical and biological ties to Hsp70, and also belongs to the Hsp70 family. These proteins include cognate members found within major intracellular compartments and highly inducible isoforms predominantly cytoplasmic or nuclear in distribution. Members of the Hsp70 family function as molecular chaperones involved in such cellular functions as protein folding, transport, maturation and degradation, operating in an ATP-dependent manner. The molecular chaperones of the Hsp70 family recognize and bind to nascent polypeptide chains or partially folded intermediates of proteins, preventing their aggregation and misfolding, and the binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein. Data demonstrates that with a ubiquitin-like domain at its amino terminus and its association with the 26S proteosome in HeLa cells, Bag-1 modulates the chaperone activity of Hsc70 and Hsp70. These findings reveal Bag-1's role as a physical link between the Hsc70/Hsp70 chaperone system and the proteasome. Experimental data also shows that the ATPase domain and the substrate-binding domain of Hsp70 (or Hsc70) cooperate to form a co-chaperone-chaperone complex with the synaptic vesicle cysteine string protein (csp), essential for normal neurotransmitter release.

Catalog Number: (CAPIPA5-18324)

Supplier: Thermo Scientific

Description: This antibody is predicted to react with bovine, canine, mouse and rat based on sequence homology. The 26S proteasome is a multicatalytic proteinase complex with a highly ordered structure composed of 2 complexes, a 20S core and a 19S regulator. The 20S core is composed of 4 rings of 28 non-identical subunits; 2 rings are composed of 7 alpha subunits and 2 rings are composed of 7 beta subunits. The 19S regulator is composed of a base, which contains 6 ATPase subunits and 2 non-ATPase subunits, and a lid, which contains up to 10 non-ATPase subunits. Proteasomes are distributed throughout eukaryotic cells at a high concentration and cleave peptides in an ATP/ubiquitin-dependent process in a non-lysosomal pathway. An essential function of a modified proteasome, the immunoproteasome, is the processing of class I MHC peptides. This gene encodes one of the non-ATPase subunits of the 19S regulator lid. In addition to participation in proteasome function, this subunit may also participate in the TNF signalling pathway since it interacts with the tumor necrosis factor type 1 receptor. A pseudogene has been identified on chromosome 1.

Supplier: Peprotech

Description: IL-6 is a pleiotropic cytokine that plays an important role in host defense by regulating immune and inflammatory responses. Produced by T cells, monocytes, fibroblasts, endothelial cells and keratinocytes, IL-6 has diverse biological functions. It stimulates B cell differentiation and antibody production, synergizes with IL-3 in megakaryocyte development and platelet production, induces expression of hepatic acute-phase proteins, and regulates bone metabolism. IL-6 signals through the IL-6 receptor system that consists of two chains, IL-6Rα and gp130. Murine IL-6 is inactive on human cells, while both human and murine are equally active on murine cells. Recombinant Murine IL-6 is a 21.7 kDa protein containing 188 amino acid residues.

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Supplier: Enzo Life Sciences

Description: The 70 kDa heat shock protein Hsp70 belongs to the Hsp70 family of highly-related protein isoforms ranging in size from 66 kDa to 78 kDa. Hsc70 shares close biochemical and biological ties to Hsp70, and also belongs to the Hsp70 family. These proteins include cognate members found within major intracellular compartments and highly inducible isoforms predominantly cytoplasmic or nuclear in distribution. Members of the Hsp70 family function as molecular chaperones involved in such cellular functions as protein folding, transport, maturation and degradation, operating in an ATP-dependent manner. The molecular chaperones of the Hsp70 family recognize and bind to nascent polypeptide chains or partially folded intermediates of proteins, preventing their aggregation and misfolding, and the binding of ATP triggers a critical conformational change leading to the release of the bound substrate protein. Data demonstrates that with a ubiquitin-like domain at its amino terminus and its association with the 26S proteosome in HeLa cells, Bag-1 modulates the chaperone activity of Hsc70 and Hsp70. These findings reveal Bag-1's role as a physical link between the Hsc70/Hsp70 chaperone system and the proteasome. Experimental data also shows that the ATPase domain and the substrate-binding domain of Hsp70 (or Hsc70) cooperate to form a co-chaperone-chaperone complex with the synaptic vesicle cysteine string protein (csp), essential for normal neurotransmitter release.