Item no. |
PTM-5908 |
Manufacturer |
PTM Biolabs
|
Amount |
100 ul |
Category |
|
Type |
Antibody Monoclonal |
Format |
Lyophilized powder |
Applications |
WB, ICC, IHC-P |
Clone |
10144 |
Specific against |
Human (Homo sapiens), Rat (Rattus norvegicus) |
Host |
Mouse |
Isotype |
IgG1 |
Conjugate/Tag |
Unconjugated |
Citations |
Piaojian Yu, et al. Pioglitazone-enhanced brown fat whitening contributes to weight gain in diet-induced obese mice. EXPERIMENTAL AND CLINICAL ENDOCRINOLOGY & DIABETES, 2023. https://www.thieme-connect.com/products/ejournals/abstract/10.1055/a-2178-9113. |
ECLASS 10.1 |
42030590 |
ECLASS 11.0 |
42030590 |
UNSPSC |
12352203 |
Alias |
COX4 |
Shipping condition |
Room temperature |
Available |
|
Manufacturer - Type |
Primary Antibodies |
Manufacturer - Applications |
WB, IHC-P, ICC/IF |
Manufacturer - Category |
Loading Control Antibodies |
Manufacturer - Targets |
COX IV |
Shipping Temperature |
Ambient temperature |
Storage Conditions |
Store at -20°C. Avoid freeze/thaw cycles. |
Stability |
Stable for 12 months from date of receipt/reconstitution. |
Manufacturer - Research Area |
Cancer, Metabolism |
Product description |
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunbit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). |
Purification Method |
Protein G purified |
Formula |
PBS, Glycerol, BSA |
PTM |
Unmodified |
Clonality |
Recombinant Monoclonal |
Background |
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunbit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). |
Cellular Localization |
Membrane, Mitochondrion |
Note: The presented information and documents (Manual, Product Datasheet, Safety Datasheet and Certificate of Analysis) correspond to our latest update and should serve for orientational purpose only. We do not guarantee the topicality. We would kindly ask you to make a request for specific requirements, if necessary.
All products are intended for research use only (RUO). Not for human, veterinary or therapeutic use.