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Catalog Number: (89139-158)
Supplier: Biotium
Description: BAPTA and its derivatives are calcium chelators that are commonly used to form calcium buffers with well-defined calcium concentrations. By injecting the chelators into cells or by incubating cells with the AM ester form of the chelators, one can control the cytosolic calcium concentration, an important means to study the roles of calcium. Key advantages of these calcium chelators include relative insensitivity toward intracellular pH change and fast release of calcium.


Catalog Number: (76085-290)
Supplier: Bioss
Description: Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit. The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain. SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways. SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.


Catalog Number: (CA24470-00)
Supplier: Hach
Description: Reagent set for the determination of Calcium Hardness by EDTA Buret Titration Method (Hach method 8222)

SDS


Catalog Number: (10389-500)
Supplier: Bioss
Description: Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3). SOD1 is found in all eukaryotic species as a homodimeric 32 kDa enzyme containing one each of Cu and Zn ion per subunit. The manganese containing 80 kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain. SOD3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways. SOD4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.


Catalog Number: (76714-584)
Supplier: AFG Bioscience
Description: Rat Calcium Binding Protein B (S100B) ELISA Kit


Catalog Number: (10481-416)
Supplier: Bioss
Description: Peroxiredoxin (Prx) is an antioxidant enzyme detoxifying reactive oxygen species and has a cysteine at the active site. Prx enzymes modulate various receptor signaling pathways and protect cells from oxidatively induced death. Peroxiredoxin 1 to 4 have two conserved Cys residues corresponding to Cys51 and Cys172 of mammalian Peroxiredoxin 1. The active site cysteine(Cys51) is oxidized to cysteine sulfenic acid(Cys51-SOH) when a peroxide is reduced. Because Cys51-SOH is unstable, it forms a disulfide with Cys172-SH which comes from the other subunit of the homodimer. The disulfide is then reduced back to the Prx active thiol form by the thioredoxin-thioredoxin reductase system. However, the formation of the disulfide is a slow process. Thus under oxidative stress conditions, the sulfenic intermediate(Cys51-SOH) can be easily over oxidized to cysteine sulfinic acid(Cys-SO2H) or cysteine sulfonic acid(Cys-SO3H) before it is able to form a disulfide. Recent studies suggest that over oxidized Prx can be reduced back to the active form during recovery after oxidative stress.


Catalog Number: (76715-404)
Supplier: AFG Bioscience
Description: Human Calcium Independent Phospholipase A2 (iPLA2) ELISA Kit


Catalog Number: (89139-296)
Supplier: Biotium
Description: Kit provides a range of calibration buffers with accurate calcium concentrations and is useful for the calibration of fluorescent Ca² indicators (1,2).


Catalog Number: (10099-794)
Supplier: Prosci
Description: SLC24A6 belongs to a family of potassium-dependent sodium/calcium exchangers that maintain cellular calcium homeostasis through the electrogenic countertransport of 4 sodium ions for 1 calcium ion and 1 potassium ion.SLC24A6 belongs to a family of potassium-dependent sodium/calcium exchangers that maintain cellular calcium homeostasis through the electrogenic countertransport of 4 sodium ions for 1 calcium ion and 1 potassium ion (Cai and Lytton, 2004 [PubMed 14625281]).


Catalog Number: (10390-184)
Supplier: Bioss
Description: Cav2.1 is a voltage-sensitive calcium channels (VSCC) which belongs to the calcium channel alpha-1 subunit family. Cav2.1 mediates the entry of calcium ions into excitable cells and is also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. Cav2.1 (isoform alpha-1A) gives rise to P and/or Q-type calcium currents. Voltage-dependent calcium channels are multisubunit complexes, consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1 ratio. The channel activity is directed by the pore-forming and voltage-sensitive alpha-1 subunit. In many cases, this subunit is sufficient to generate voltage-sensitive calcium channel activity. The auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge regulate the channel activity.


Catalog Number: (10390-172)
Supplier: Bioss
Description: Cav2.1 is a voltage-sensitive calcium channels (VSCC) which belongs to the calcium channel alpha-1 subunit family. Cav2.1 mediates the entry of calcium ions into excitable cells and is also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. Cav2.1 (isoform alpha-1A) gives rise to P and/or Q-type calcium currents. Voltage-dependent calcium channels are multisubunit complexes, consisting of alpha-1, alpha-2, beta and delta subunits in a 1:1:1:1 ratio. The channel activity is directed by the pore-forming and voltage-sensitive alpha-1 subunit. In many cases, this subunit is sufficient to generate voltage-sensitive calcium channel activity. The auxiliary subunits beta and alpha-2/delta linked by a disulfide bridge regulate the channel activity.


Catalog Number: (ABCA_AB2783-100UG)
Supplier: Abcam
Description: Mouse monoclonal [JA9] to Calcium Pump PMCA4 ATPase.

New Product


Catalog Number: (ABCA_AB238110-100U)
Supplier: Abcam
Description: Rabbit polyclonal to Calcium channel L type DHPR alpha 2 subunit/CACNA2D1.

New Product


Catalog Number: (76711-978)
Supplier: AFG Bioscience
Description: Human Calcium/Calmodulin-Dependent Protein Kinase type II Subunit beta (CAMK2B) ELISA Kit


Catalog Number: (76705-828)
Supplier: AFG Bioscience
Description: Rat S100 Calcium Binding Protein B(S100-B) ELISA Kit


Catalog Number: (10349-080)
Supplier: Bioss
Description: The sarcoplasmic reticulum (SR) is, in part, responsible for maintaining the level of intracellular calcium in cardiac and skeletal muscle by storing and releasing calcium. Several intralumenal SR calcium binding proteins have been identified, the most prominent of these is calsequestrin. Calsequstrin is a calcium binding protein known to sequester calcium accumulated in the sarcoplasmic reticulum of muscle cells during relaxation and is found discretely localized to the junctional and corbular (terminal cisternae) SR. Calsequestrin functions to localize calcium near the junctional face of the terminal cisternae from which calcium can be released into the cytosol via the ryanodine receptor. This protein is highly acidic and has a large capacity and moderate to low affinity for calcium.


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