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Expression levels of myoglobin in muscle and non-muscle tissues of rainbow trout Oncorhynchus mykiss
The results showed that the MI-based bio-sensing system had high selectivity and sensitivity for detection of Cardiac biomarkers . Compared with the control region, ultrasensitive detections of CRP (zeige CRP Proteine) and Mb were accomplished with the detection limits of 1.0 pg/mL and 0.1 pg/mL, respectively.
Report morphology of myoglobin casts in renal biopsies with acute kidney injury.
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 (zeige SYNPO2 Proteine)) monoclonal antibody of high specificity and affinity, a one-step sandwich ELISA for detecting MYO (zeige SYNPO2 Proteine) 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 (zeige NGB Proteine) and myoglobin were generated by swapping a regulatory segment.
Findings indicate that myoglobin (Mb) and neuroglobin (Ngb (zeige NGB Proteine)) can be expressed in nonmuscle and non-neural contexts.
Inhibition of mammalian target of rapamycin (mTOR (zeige FRAP1 Proteine)) activation using rapamycin restored Mb mRNA expression to control levels. Lipid supplementation had no effect on Mb gene expression. Thus, IGF-1 (zeige IGF1 Proteine)-induced anabolic signaling can be a strategy to improve muscle size under mild hypoxia, but lowers Mb gene expression
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 (zeige NOS2 Proteine)-derived NO, which determines the functional consequences of iNOS (zeige NOS2 Proteine) 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.
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.
A spectroscopic study involving apomyoglobin (Apo (zeige C9orf3 Proteine)-Mb) and cyclodextrin (CyD (zeige CYBB Proteine)) of various cavity sizes as model globular protein and synthetic receptors, respectively, using steady-state and picosecond-resolved techniques, is detailed here.
Determination of a representative formal redox potentials of the Fe(II)/Fe(III) redox couple cyanhaemoglobin/cyanmethaemoglobin and the myoglobin/metmyoglobin , at pH=7 and related to the state in solution, was the objective of this work.
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 (zeige C9orf3 Proteine)-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 (zeige TRPV6 Proteine) 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 (zeige CYB5A Proteine)] 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.
myoglobin plays a crucial role in zebrafish development and is important for angiogenesis and gut (zeige GUSB Proteine) 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.