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MB encodes a member of the globin superfamily and is expressed in skeletal and cardiac muscles. Additionally we are shipping Myoglobin Antibodies (320) and Myoglobin Kits (89) and many more products for this protein.
Showing 10 out of 159 products:
Human MB Protein expressed in Escherichia coli (E. coli) - ABIN667863
Qiu, Sutton, Riggs: Identification of myoglobin in human smooth muscle. in The Journal of biological chemistry 1998
Show all 2 references for ABIN667863
analysis of myoglobin gene regulatory networks in breast and prostate cancer
Data show that with the myoglobin (MYO) monoclonal antibody of high specificity and affinity, a one-step sandwich ELISA for detecting MYO 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 Proteins) and myoglobin were generated by swapping a regulatory segment.
Findings indicate that myoglobin (Mb) and neuroglobin (Ngb (show NGB Proteins)) 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 (show MOK Proteins).
Our LFIA performance was additionally compared with electrochemiluminescence immunoassay (ECLI) detection for simultaneous determination of hs-cTnI (show TNNI3 Proteins) and myoglobin in patients with suggestive of acute myocardial infarction .
Hydrophobic effect drives oxygen uptake in myoglobin via histidine E7.
Water entry into the heme pockets of isolated hemoglobin subunits was detected by optical methods.
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 Proteins)-derived NO, which determines the functional consequences of iNOS (show NOS2 Proteins) 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.
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 Proteins)-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 Proteins) 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 Proteins)] 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.
Electrospray ionization mass spectrometry (ESI-MS) was employed to monitor the heme release and the conformational changes of myoglobin (Mb) under different solvent conditions, and to observe ligand bindings of Mb.
myoglobin plays a crucial role in zebrafish development and is important for angiogenesis and gut (show GUSB Proteins) 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.