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Myoglobin is associated with larger hematoma volume and growth after adjusting potential confounding factors in intracerebral hemorrhage.
Electroanalysis of myoglobin as a marker of acute myocardial infarction by means of screenprinted electrodes modified with multiwalled carbon nanotubes and polymeric artificial antibodies is developed. Plastic antibodies to myoglobin (molecularly imprinted polymers, MIPs) based on o-phenylenediamine were produced by electropolymerization. Molecular imprinting technology in biosensor analysis was used.
In the absence of Mb, the Y-shape structure remains intact. So, a weak electrochemical signal is observed. Upon addition of target, the DApt leave the CS and bind to Mb, leading to disassembly of Y-shape structure and following the addition of Exo I, a strong electrochemical signal could be recorded.
analysis of myoglobin gene regulatory networks in breast and prostate cancer
Data show that with the myoglobin (MYO (show SYNPO2 ELISA Kits)) monoclonal antibody of high specificity and affinity, a one-step sandwich ELISA for detecting MYO (show SYNPO2 ELISA Kits) has been established successfully, which provides a basis for the development of domestic ELISA kit.
A non-ischemic serum myoglobin release is rare, but could be associated in subgroups of patients.
Data show that chimeric neuroglobin (show NGB ELISA Kits) and myoglobin were generated by swapping a regulatory segment.
Findings indicate that myoglobin (Mb) and neuroglobin (Ngb (show NGB ELISA Kits)) can be expressed in nonmuscle and non-neural contexts.
Blood myoglobin could serve as a valuable early predictor and marker of rhabdomyolysis and acute myoglobinuric kidney injury
High myoglobin expression is associated with renal cell carcinoma.
Myoglobin overexpression inhibits reperfusion in the ischemic mouse hindlimb through impaired angiogenesis but not arteriogenesis
Chronic exercise downregulates myocardial myoglobin and attenuates nitrite reductase capacity during ischemia-reperfusion.
Show a high capacity of myoglobin-deficient mice to adapt to catecholamine induced cardiac stress which is associated with activation of a distinct cardiac gene expression program.
Endogenous nitrite reduction to NO. via the heme globin myoglobin enhances blood flow and matches O(2) supply to increased metabolic demands under hypoxic conditions.
Myoglobin is present in the murine vasculature and contributes significantly to nitrite-induced vasodilation
myoglobin constitutes the important barrier that efficiently protects the heart from nitrosative stress
Findings demonstrate that myoglobin serves as an important cytoplasmic buffer of iNOS (show NOS2 ELISA Kits)-derived NO, which determines the functional consequences of iNOS (show NOS2 ELISA Kits) overexpression.
myoglobin is an important cytoplasmic cardiac hemoprotein that functions in regulating NO homeostasis within cardiomyocytes.
The role of myoglobin as intracellular nitric oxide(NO) scavenger is small, and increase in mitochondrial superoxide in SOD heterozygous mice may cause decrease NO bioavailability and alter control of myocardial O2 consumption by NO.
importance of oxygen supply and nitric oxide scavenging by myoglobin is clearly demonstrated at the conscious animal level
Similar conclusions are obtained both for pig cyano-myoglobin and for horse cyano-myoglobin, the structural deformation being in the former of minor entity
Glycine at E14 in myoglobin enhances autoxidation and hemin loss rates.
Methylglyoxal interacts with myoglobin by Maillard reaction. Methylglyoxal-modification leads to amyloid-like aggregation of Mb at longer incubation time.
The study applies hydrogen/deuterium exchange (HDX) mass spectrometry (MS) for probing the conformational dynamics of the model protein myoglobin (Mb) in the presence of N(2) bubbles.
Using a coarse-grained symmetrized Go model, study performed a series of folding simulations of two apo (show C9orf3 ELISA Kits)-myoglobin molecules restrained at a high density, addressing competition of formation of a domain-swapped dimer with folding to two monomer structures.
This work presents a thorough investigation of the hydration dependence of myoglobin dynamics.
Equine carbonmonoxy Mb contains 4.5 +/- 1.0 ordered internal water molecules with a mean survival time of 5.6 +/- 0.5 mus (show TRPV6 ELISA Kits) at 25 degrees C.
The stretching mode of nitric oxide (NO) in ferric MB(III)NO consists of a major band at 1922 cm(-1) (97.7%) and a minor band at 1902 cm(-1) (2.3%), suggesting that ferric MB(III)NO in room temperature solution has two conformational substates.
The study computes electron transfer rates for the [myoglobin(wt), cytochrome b5 (show CYB5A ELISA Kits)] complex.
The ultrafast equilibrium fluctuations of the Fe(III)-NO complex of a single point mutation of Myoglobin (H64Q) have been studied using Fourier Transform 2D-IR spectroscopy.
Various structural models for the first stable HNO heme protein complex, MbHNO (Mb, myoglobin), were examined by quantum chemical calculations.
Results describe a correlation between glycation-induced structural and functional modifications of the heme protein myoglobin.
myoglobin plays a crucial role in zebrafish development and is important for angiogenesis and gut (show GUSB ELISA Kits) development
This gene encodes a member of the globin superfamily and is expressed in skeletal and cardiac muscles. The encoded protein is a haemoprotein contributing to intracellular oxygen storage and transcellular facilitated diffusion of oxygen. At least three alternatively spliced transcript variants encoding the same protein have been reported.