You Searched For: Cyclohexyl+methyl+sulphide

Catalog Number: (10459-176)

Supplier: Bioss

Description: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.Sequence similarities: Belongs to the RuBisCO large chain family. Type I subfamily.Post-translational modifications: The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity). The disulfide bonds reported in 1RBO may be the result of oxidation during crystallization.

Catalog Number: (10464-554)

Supplier: Bioss

Description: EphA3 is a member of the Ephrin (Eph) family. The Ephrins and Eph-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. Based on their structures and sequence relationships, ephrins are divided into the Ephrin A (EphA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the Ephrin B (EphB) class, which are transmembrane proteins. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats.

Catalog Number: (10464-556)

Supplier: Bioss

Description: EphA3 is a member of the Ephrin (Eph) family. The Ephrins and Eph-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, especially in the nervous system and in erythropoiesis. Based on their structures and sequence relationships, ephrins are divided into the Ephrin A (EphA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the Ephrin B (EphB) class, which are transmembrane proteins. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats.

Catalog Number: (75790-470)

Supplier: Prosci

Description: FAS(TNFRSF6) is a receptor and contains three TNFR-Cys repeats and one death domain. It has been shown that FAS is involved in the physiological regulation of programmed cell death, and has been implicated in the pathogenesis of various malignancies and diseases of the immune system. FADD (adapter molecule) recruits caspase-8 to the activated receptor, the resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases mediating apoptosis. FAS-mediated apoptosis may play a role in the induction of peripheral tolerance, in the antigen-stimulated suicide of mature T-cells, or both.

Supplier: Biotium

Description: This conjugate is prepared by labeling F(ab’)2 fragment of goat anti-rabbit IgG (H+L) with CF™680 dye. CF™ dyes offer advantages in brightness, photostability, and specificity compared to other fluorescent dyes. Far-red/near-infrared CF™680 (Ex/Em 681/698 nm) is brighter and provides the best signal-to-noise ratio compared to antibody conjugates of spectrally similar dyes.

Alexa Fluor® is a registered trademark of Thermo Fisher Scientific. Cy®5 is a registered trademark of GE Healthcare.

Catalog Number: (75791-732)

Supplier: Prosci

Description: Peroxisomes are essential organelles that participate in multiple important metabolic processes, including the beta -oxidation of fatty acids, plasmalogen synthesis, and the metabolism of reactive oxygen species (ROS). Peroxiredoxins is overexpressed in breast cancer tissues to a great extent suggesting that they has a proliferative effect and may be related to cancer development or progression. Peroxiredoxin 5 (PRDX5) is a thioredoxin peroxidase that belongs to the atypical 2-Cys class of the TSA/ahpC family of peroxiredoxins. PRDX5 is a widely expressed mitochondrial antioxidant enzyme that reduces hydrogen peroxide, alkyl hydroperoxides, and peroxynitrite. In human cells, this enzyme is present in the cytosol, mitochondria, peroxisomes, and nucleus.

Catalog Number: (76101-388)

Supplier: Bioss

Description: May catalyze the degradation of intercellular cohesive structures in the cornified layer of the skin in the continuous shedding of cells from the skin surface. Specific for amino acid residues with aromatic side chains in the P1 position. Cleaves insulin A chain at '14-Tyr-|-Gln-15' and insulin B chain at '6-Leu-|-Cys-7', '16-Tyr-|-Leu-17', '25-Phe-|-Tyr-26' and '26-Tyr-|-Thr-27'. Could play a role in the activation of precursors to inflammatory cytokines.

Catalog Number: (89358-276)

Supplier: Genetex

Description: This gene encodes a member of the ubiquitin-specific processing (UBP) family of proteases that is a deubiquitinating enzyme (DUB) with His and Cys domains. This protein is located in the cytoplasm and cleaves the ubiquitin moiety from ubiquitin-fused precursors and ubiquitinylated proteins. Mice with a mutation that results in reduced expression of the ortholog of this protein are retarded for growth, develop severe tremors by 2 to 3 weeks of age followed by hindlimb paralysis and death by 6 to 10 weeks of age. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. [provided by RefSeq]

Catalog Number: (76100-144)

Supplier: Bioss

Description: This gene belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. EPH and EPH-related receptors have been implicated in mediating developmental events, particularly in the nervous system. Receptors in the EPH subfamily typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. This gene is expressed in some human cancer cell lines and has been implicated in carcinogenesis.

Catalog Number: (CAAAA44506-AC)

Supplier: Thermo Scientific Chemicals

Description: Liquid

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Supplier: Anaspec Inc

Description: One of the three mammalian Natriuretic peptides, A-type is the Atrial natriuretic peptide (ANP) also called Cardiodilatin (CDD). ANP (1-28) peptide hormone constitutes the first 28 amino acids of the ANP synthesized in the heart of different vertebrates. It plays an important role in the regulation of blood pressure and natriuresis/diuresis. Residues Phe8, Arg14 and the C-terminal sequence of ANP are known to bind to human NPR-A (Natriuretic peptide receptor type A).
Sequence:SLRRSSCFGGRMDRIGAQSGLGCNSFRY (Disulfide bridge: 7-23)
MW:3080.5 Da
%Peak area by HPLC:≥95%
Storage condition: -20°C

Catalog Number: (10096-832)

Supplier: Proteintech

Description: USP1(Ubiquitin carboxyl-terminal hydrolase 1) is a negative regulator of DNA damage repair which specifically deubiquitinates monoubiquitinated FANCD2.It is Also involved in PCNA-mediated translesion synthesis (TLS) by deubiquitinating monoubiquitinated PCNA.This protein, which consists of 785 amino acids with a deduced molecular mass of 88.2 kDa, possesses His and Cys domains that are highly conserved in all members of the ubiquitin-specific processing (UBP) family of proteases. The USP1 enzyme can undergo autocleavage, resulting in a 100 kDa N-terminal fragment and a 14 kDa C-terminal fragment.

Catalog Number: (76117-444)

Supplier: Bioss

Description: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site.Sequence similarities: Belongs to the RuBisCO large chain family. Type I subfamily.Post-translational modifications: The disulfide bond which can form between Cys-247 in the large chain dimeric partners within the hexadecamer appears to be associated with oxidative stress and protein turnover (By similarity). The disulfide bonds reported in 1RBO may be the result of oxidation during crystallization.

Catalog Number: (75790-458)

Supplier: Prosci

Description: Tumor necrosis factor receptor superfamily member 3, also known as Lymphotoxin-beta receptor,Tumor necrosis factor C receptor,Tumor necrosis factor receptor 2-related protein,Tumor necrosis factor receptor type III,LTBR,TNFCR, TNFR3 and TNFRSF3, is a member of the tumor necrosis factor (TNF) family of receptors. LTBR is a single-pass type I membrane protein and contains four TNFR-Cys repeats. It is expressed on the surface of most cell types, but not on T and B lymphocytes. LTBR and its ligand play a role in the development and organization of lymphoid tissue and transformed cells. Activation of LTBR can trigger apoptosis. In addition, LTBR can lead to the release of the cytokine interleukin 8.

Catalog Number: (10349-408)

Supplier: Bioss

Description: Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide, cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Isoform 3 seems to be inactive.

Catalog Number: (76083-154)

Supplier: Bioss

Description: Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide, cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Isoform 3 seems to be inactive.