You Searched For: Chromium+(III)+nitrate


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Catalog Number: (PRSI30-095)
Supplier: ProSci Inc.
Description: Kininogens are inhibitors of thiol proteases. HMW-kininogen plays an important role in blood coagulation by helping to position optimally prekallikrein and factor XI next to factor XII and inhibits the thrombin- and plasmin-induced aggregation of thrombocytes. The active peptide bradykinin that is released from HMW-kininogen shows a variety of physiological effects such as influence in smooth muscle contraction, induction of hypotension, natriuresis and diuresis, etc.
UOM: 1 * 50 µG


Catalog Number: (PRSI91-168)
Supplier: ProSci Inc.
Description: Ubiquitin Carboxyl-Terminal Hydrolase Isozyme L1 (UCHL1) belongs to the Peptidase C12 family. UCHL1 is specifically expressed in the neurons and in cells of the diffuse neuroendocrine system. UCHL1 is a component of the ubiquitin system, which has a fundamental role in regulating various biological activities. UCHL1 is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. UCHL1 also binds to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer of UCHL1 may have ATP-independent ubiquitin ligase activity.
UOM: 1 * 50 µG


Catalog Number: (PRSI91-269)
Supplier: ProSci Inc.
Description: Ubiquitin-Conjugating Enzyme E2 S (UBE2S) is a member of the Ubiquitin-Conjugating Enzyme family. UBE2S interacts with CDC20, FZR1/CDH1 and VHL. UBE2S can form a thiol ester linkage with Ubiquitin in an Ubiquitin Activating Enzyme-Dependent manner, a characteristic property of Ubiquitin Carrier Proteins. UBE2S acts as an essential factor of the Anaphase Promoting Complex/Cyclosome, a cell cycle-regulated Ubiquitin ligase that controls progression through mitosis. UBE2S is also involved in ubiquitination and subsequent degradation of VHL, resulting in an accumulation of HIF1A.
UOM: 1 * 50 µG


Catalog Number: (AATB4530)
Supplier: AAT BIOQUEST
Description: Cu-free click reaction, i.e., the strain-promoted alkyne-azide cycloaddition (SPAAC) is a bioorthogonal reaction utilizing a pair of reagents, cyclooctynes and azides that exclusively and efficiently react with each other while remain inert to naturally occurring functional groups such as hydroxy, amino and thiol groups.
UOM: 1 * 1 mg


Supplier: ENZO LIFE SCIENCES
Description: The multifunctional, multi -compartmental protein Calreticulin (Crt) functions as a soluble molecular chaperone of new or misfolded proteins, as well as a Ca2+-binding protein. Most abundant in the ER lumen, Crt expression also occurs in other membrane-bound organelles, the cell surface, and extracellularly. Also known as CRP-55, calregulin and HACBP (high affinity calcium-binding protein), Crt contains the ER-retrieval sequence, KDEL, and is the solub le paralog of the ER membrane protein Calnexin (Cnx). Crt's three domains include a 180 residue N-terminal domain, a proline-rich Pdomainresidues 189 -288) that binds Ca2+ with high affinity and shares homology with Cnx and calmegin, and a 110 residue C-terminal domain that binds Ca2+ with low affinity but high capacity. The P-domain may interact with the co-chaperone ERp57 (Grp58), a thiol reductase. The NMR structure of the P -domain consists of an extended hairpin that appears to form a curved protrusion from the Crt core domain. Both Crt and its membrane bound homolog CNX interact with proteins and glycoproteins possessing monoglucosylated N -glycans. The Crt/Cnx cycle promotes correct folding, inhibits aggregation of folding intermediates, blocks premature oligomerization, regulates ER degradation, and prevents incompletely folded glycoproteins from exiting to the Golgi complex. Crt also appears to function as an auto-antigen in systemic lupus erythematosus, rheumatoid arthritis, celiac disease, complete congenital heart block, and halothane hepatitis. A diversity of additional functions attributed to Crt includes adhesion, blood function, and cardiac and neuronal development gene expression.

Catalog Number: (PRSI25-651)
Supplier: ProSci Inc.
Description: Electron transport pathways are generally associated with mitochondrial membranes, but non-mitochondrial pathways are also biologically significant. Plasma membrane electron transport pathways are involved in functions as diverse as cellular defense, intracellular redox homeostasis, and control of cell growth and survival. Members of the ecto-NOX family, such as CNOX, or ENOX1, are involved in plasma membrane transport pathways. These enzymes exhibit both a hydroquinone (NADH) oxidase activity and a protein disulfide-thiol interchange activity in series, with each activity cycling every 22 to 26 minutes.Electron transport pathways are generally associated with mitochondrial membranes, but non-mitochondrial pathways are also biologically significant. Plasma membrane electron transport pathways are involved in functions as diverse as cellular defense, intracellular redox homeostasis, and control of cell growth and survival. Members of the ecto-NOX family, such as CNOX, or ENOX1, are involved in plasma membrane transport pathways. These enzymes exhibit both a hydroquinone (NADH) oxidase activity and a protein disulfide-thiol interchange activity in series, with each activity cycling every 22 to 26 minutes (Scarlett et al., 2005 [PubMed 15882838]).[supplied by OMIM].
UOM: 1 * 50 µG


Catalog Number: (PRSI96-762)
Supplier: ProSci Inc.
Description: Ubiquitin carboxyl-terminal hydrolase isozyme L1 (UCHL1) ,a member of the peptidase C12 family, is also known as neuron cytoplasmic protein 9.5 (PGP 9.5) and ubiquitin thioesterase L1.About 30% of total UCHL1 is associated with membranes in brain. UCHL1 is involved both in the processing of ubiquitin precursors and of ubiquitinated proteins. This enzyme is a thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of ubiquitin. Also,UCHL1 can bind to free monoubiquitin and may prevent its degradation in lysosomes. The homodimer of UCHL1 may have ATP-independent ubiquitin ligase activity. Furthermore, the mutations of UCHL1 gene can result in parkinson disease 5.
UOM: 1 * 50 µG


Catalog Number: (PRSI91-365)
Supplier: ProSci Inc.
Description: Cathepsin B is an enzymatic protein belonging to the peptidase (or protease) families. The protein encoded by this gene is a lysosomal cysteine protease composed of a dimer of disulfide-linked heavy and light chains, both produced from a single protein precursor. It is a member of the peptidase C1 family. At least five transcript variants encoding the same protein have been found for this gene. Cystatin-B / CSTB is an intracellular thiol proteinase inhibitor. Tightly binding reversible inhibitor of cathepsins L, H and B. Cystatin-B / CSTB is able to form a dimer stabilized by noncovalent forces, inhibiting papain and cathepsins l, h and b. Cystatin-B / CSTB is also thought to play a role in protecting against the proteases leaking from lysosomes
UOM: 1 * 50 µG


Catalog Number: (PIER20408)
Supplier: Thermo Fisher Scientific
Description: Thermo Scientific Pierce 2-Mercaptoethylamine-HCl, commonly abbreviated 2-MEA, is a mild reductant that is often used to selectively reduce hinge-region disulfide bonds in antibody.
UOM: 1 * 1 SET


Supplier: MP Biomedicals
Description: β-Mercaptoethylamine (Cysteamine hydrochloride) is useful antioxidant. It is experimentally used as a radioprotective agent. It is also used to produce acute and chronic duodenal ulcers in rats and as an antidote to acetaminophen.

Catalog Number: (17-0480-01)
Supplier: Cytiva
Description: Epoxy-activated Sepharose™ 6B is a pre-activated medium for immobilisation of various ligands including sugars through coupling of hydroxy, amino or thiol groups on the ligand to Sepharose™ 6B via a 12-atom hydrophilic spacer arm. Medium is formed by reacting Sepharose™ 6B with 1,4-bis (2,3- epoxy-propoxy-) butane. It can be used to couple sugars and other carbohydrates via stable ether linkages to hydroxyl groups.
UOM: 1 * 15 g


Supplier: ENZO LIFE SCIENCES
Description: The multifunctional, multi-compartmental protein Calreticulin (Crt) functions as a soluble molecular chaperone of new or misfolded proteins as well as a Ca2+-binding protein. Most abundant in the ER lumen, Crt expression also occurs in other membrane-bound organelles, the cell surface, and extracellularly. Also known as CRP-55, calregulin and HACBP (high affinity calcium-binding protein), Crt contains the ER-retrieval sequence, KDEL, and is the soluble paralog of the ER membrane protein Calnexin (Cnx). Crts three domains include a 180 residue N-terminal domain, a proline-rich P-domain (residues 189-288) that binds Ca2+ with high affinity and shares homology with Cnx and calmegin, and a 110 residue C-terminal domain that binds Ca2+ with low affinity but high capacity. The P-domain may interact with the co-chaperone ERp57 (Grp58), a thiol reductase. The NMR structure of the P-domain consists of an extended hairpin that appears to form a curved protrusion from the Crt core domain. Both Crt and its membrane bound homolog CNX interact with proteins and glycoproteins possessing monoglucosylated N-glycans. The Crt/Cnx cycle promotes correct folding, inhibits aggregation of folding intermediates, blocks premature oligomerization, regulates ER degradation, and prevents incompletely folded glycoproteins from exiting to the Golgi complex. Crt also appears to function as an auto-antigen in systemic lupus erythematosus, rheumatoid arthritis, celiac disease, complete congenital heart block, and halothane hepatitis. A diversity of additional functions attributed to Crt includes adhesion, blood function, and cardiac and neuronal development gene expression.

Catalog Number: (PRSI92-668)
Supplier: ProSci Inc.
Description: Tryptophan synthase is a multienzyme alpha2 beta 2 complex composed of two protein subunit. Tryptophan synthase catalyses the last two steps in the synthesis of L-tryptophan (L-Trp). The alpha-subunit catalyses cleavage of 3-indole-d-glycerol 3′-phosphate (IGP) to give indole and D-glyceraldehyde 3′-phosphate (G3P). Indole is then transferred through a 25-Å hydrophobic tunnel to the beta -subunit. The beta 2 subunit contains pyridoxal 5'-phosphate and catalyses several pyridoxal 5'-phosphate-dependent reactions, including/3-elimination reactions 6 and a thiol-dependent transamination reaction. This enzyme is commonly found in Eubacteria, Archaebacteria, Protista, Fungi, and Plantae, but is absent from Animalia. As humans do not have tryptophan synthase, this enzyme has been explored as a potential drug target.
UOM: 1 * 50 µG


Catalog Number: (PRSI91-767)
Supplier: ProSci Inc.
Description: Endoplasmic reticulum resident protein 27, also known as ER protein 27, C12orf46 and ERP27, is an endoplasmic reticulum luminal protein which is a member of the protein disulfide isomerase family. ERP27 contains one thioredoxin domain and does not contain a CXXC active site motif. ERP27 is widely expressed in many tissues; it has highest expression in pancreas, with lower levels in spleen, lung, kidney, thymus, and bone marrow. ERP27 interacts with PDIA3 and binds somatostatin-14 via hydrophobic interactions. ERP27 may act as a protease, protein disulfide isomerase, thiol-disulfide oxidase or phospholipase.
UOM: 1 * 50 µG


Catalog Number: (PRSI91-750)
Supplier: ProSci Inc.
Description: ERO1-Like Protein alpha (ERO1L) is an enzyme that belongs to the EROs family. ERO1L is expressed at high level in esophagus and upper digestive tract. ERO1L is an essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. ERO1L acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. It associates with ERP44, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. ERO1L may be responsible for a significant proportion of reactive oxygen species (ROS) in the cell. ERO1L responses to temperature stimulus, protein thiol-disulfide exchange, protein folding with or without chaperone cofactor and transport.
UOM: 1 * 50 µG


Catalog Number: (PRSI92-667)
Supplier: ProSci Inc.
Description: Tryptophan synthase is a multienzyme alpha2 beta 2 complex composed of two protein subunit. Tryptophan synthase catalyses the last two steps in the synthesis of L-tryptophan (L-Trp). The alpha-subunit catalyses cleavage of 3-indole-d-glycerol 3′-phosphate (IGP) to give indole and D-glyceraldehyde 3′-phosphate (G3P). Indole is then transferred through a 25-Å hydrophobic tunnel to the beta -subunit. The beta 2 subunit contains pyridoxal 5'-phosphate and catalyses several pyridoxal 5'-phosphate-dependent reactions, including/3-elimination reactions 6 and a thiol-dependent transamination reaction. This enzyme is commonly found in Eubacteria, Archaebacteria, Protista, Fungi, and Plantae, but is absent from Animalia. As humans do not have tryptophan synthase, this enzyme has been explored as a potential drug target.
UOM: 1 * 50 µG


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