Összes fotó(2)
Fontos dokumentumok
M7773
Monoclonal Anti-Myoglobin antibody produced in mouse
clone MG-1, ascites fluid
Szinonimák:
Anti-PVALB
Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(2)
About This Item
konjugátum:
unconjugated
application:
ELISA (i)
IHC (p)
IHC (p)
klón:
MG-1, monoclonal
faj reaktivitás:
human
citations:
10
technika/technikák:
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:400 using human skeletal muscle tissue
indirect ELISA: 1:10,000
indirect ELISA: 1:10,000
Javasolt termékek
biológiai forrás
mouse
Minőségi szint
konjugátum
unconjugated
antitest forma
ascites fluid
antitest terméktípus
primary antibodies
klón
MG-1, monoclonal
tartalmaz
15 mM sodium azide
faj reaktivitás
human
technika/technikák
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:400 using human skeletal muscle tissue
indirect ELISA: 1:10,000
izotípus
IgG1
UniProt elérési szám
kiszállítva
dry ice
tárolási hőmérséklet
−20°C
célzott transzláció utáni módosítás
unmodified
Géninformáció
human ... MB(4151)
Related Categories
Általános leírás
Myoglobin is a hemoprotein that regulates the storage and diffusion of oxygen in heart and skeletal muscles. Additionally, this protein also protects the tissues from oxidative damage by controlling the levels of reactive oxygen species and nitric oxide. Thus, myoglobin has been implicated in regulating nitric oxide and oxygen levels in the mitochondrial compartments of skeletal muscle and cardiac cells. Monoclonal Anti-Myoglobin antibody is specific for myoglobin and stains human skeletal muscles. The product does not cross-react with hemoglobin.
Myoglobin is composed of a 153 amino acid long polypeptide and heme group. This protein is encoded by the gene MB mapped to human chromosome 22q12.3. It is a unit of 20S core proteasome complex. Myoglobin is localized to the skeletal and cardiac muscle.
Immunogén
Purified human skeletal muscle myoglobin.
Alkalmazás
Monoclonal Anti-Myoglobin antibody is suitable for use in western blot and protein arrays.
Biokémiai/fiziológiai hatások
Myoglobin participates in proteases mediated degradation of intracellular proteins Upon damage to the muscle cell due to infarction of a coronary artery, neurological trauma, infection or tumor processes, myoglobin escapes to the environment and can be found in plasma using sensitive assays.
Jogi nyilatkozat
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Tárolási osztály kódja
10 - Combustible liquids
WGK
nwg
Lobbanási pont (F)
Not applicable
Lobbanási pont (C)
Not applicable
Válasszon a legfrissebb verziók közül:
Analitikai tanúsítványok (COA)
Lot/Batch Number
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D J Marcinek et al.
American journal of physiology. Regulatory, integrative and comparative physiology, 280(4), R1123-R1133 (2001-03-15)
Myoglobin (Mb) buffers intracellular O2 and facilitates diffusion of O2 through the cell. These functions of Mb will be most effective when intracellular PO2 is near the partial pressure of oxygen at which Mb is half saturated (P50) of the
Proteomics analysis indicated the protein expression pattern related to the development of fetal conotruncal defects
Wu Y, et al.
Journal of Cellular Physiology, 234(8), 13544-13556 (2019)
George A Ordway et al.
The Journal of experimental biology, 207(Pt 20), 3441-3446 (2004-09-02)
Myoglobin is a cytoplasmic hemoprotein, expressed solely in cardiac myocytes and oxidative skeletal muscle fibers, that reversibly binds O2 by its heme residue, a porphyrin ring:iron ion complex. Since the initial discovery of its structure over 40 years ago, wide-ranging
Joy G Ghosh et al.
Protein science : a publication of the Protein Society, 14(3), 684-695 (2005-02-22)
Protein pin array technology was used to identify subunit-subunit interaction sites in the small heat shock protein (sHSP) alphaB crystallin. Subunit-subunit interaction sites were defined as consensus sequences that interacted with both human alphaA crystallin and alphaB crystallin. The human
U B Hendgen-Cotta et al.
The Journal of experimental biology, 213(Pt 16), 2734-2740 (2010-08-03)
For more than 100 years, myoglobin has been among the most extensively studied proteins. Since the first comprehensive review on myoglobin function as a dioxygen store by Millikan in 1939 and the discovery of its structure 50 years ago, multiple
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