M7773
Monoclonal Anti-Myoglobin antibody produced in mouse
clone MG-1, ascites fluid
別名:
Anti-PVALB
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すべての画像(2)
About This Item
結合体:
unconjugated
application:
ELISA (i)
IHC (p)
IHC (p)
クローン:
MG-1, monoclonal
化学種の反応性:
human
citations:
10
テクニック:
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:400 using human skeletal muscle tissue
indirect ELISA: 1:10,000
indirect ELISA: 1:10,000
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由来生物
mouse
品質水準
結合体
unconjugated
抗体製品の状態
ascites fluid
抗体製品タイプ
primary antibodies
クローン
MG-1, monoclonal
含みます
15 mM sodium azide
化学種の反応性
human
テクニック
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:400 using human skeletal muscle tissue
indirect ELISA: 1:10,000
アイソタイプ
IgG1
UniProtアクセッション番号
輸送温度
dry ice
保管温度
−20°C
ターゲットの翻訳後修飾
unmodified
遺伝子情報
human ... MB(4151)
詳細
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.
免疫原
Purified human skeletal muscle myoglobin.
アプリケーション
Monoclonal Anti-Myoglobin antibody is suitable for use in western blot and protein arrays.
生物化学的／生理学的作用
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.
免責事項
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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保管分類コード
10 - Combustible liquids
WGK
nwg
引火点(°F)
Not applicable
引火点(℃)
Not applicable
適用法令
試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。
Jan Code
M7773-.2ML:
M7773-.5ML:
M7773-100UL:
M7773-BULK:
M7773-VAR:
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
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
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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