-
Recombinant Human Myoglobin
Recombinant Human Myoglobin
- 中文名称：
- Recombinant Human Myoglobin
- 英文名称：
- Recombinant Human Myoglobin
- 品牌：
- AAA Biotech
- 品牌介绍：
- AAA Biotech专注于为全球生命科学研究提供高品质的蛋白质研究工具，核心产品包括经严格验证的抗体、重组蛋白及ELISA试剂盒。
- 货号：
- AAA38437
- 规格：
- 0.01 mg|0.05 mg|1 mg|2x1 mg|3x1 mg
- 保存建议：
- Myoglobin should be stored at 4°C.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please do not freeze.
- 货期：
- 6-8周
- 纯度：
- Greater than 95.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
- 产品形式：
- The sterile solution (1.9 mg/mL) contains phosphate-buffered saline (pH 7.4) and 0.05% NaN3.
Sterile Filtered brownish solution.
- 免责声明：
- *本产品仅供科研实验使用，不得用于临床诊断。*
- 说明书：
Description: Myoglobin Human Recombinant produced in E Coli is a non-glycosylated polypeptide chain having a molecular mass of 17.67 kDa.
The Myoglobin is purified by proprietary chromatographic techniques.
Introduction: Myoglobin is a member of the globin superfamily and can be found in skeletal and cardiac muscles. It is a haemoprotein that contributs to intracellular oxygen storage and transcellular facilitated diffusion of oxygen. Myoglobin has a single-chain globular structure of 153 amino acids, containing a heme prosthetic group (iron-containing porphyrin) in the core around which the remaining apoprotein folds. Myoglobin has 8 alpha helices and a hydrophobic core. Myoglobin's molecular weight is 16.7 kDa, and it is the primary oxygen-carrying pigment of muscle tissues. The binding of oxygen in myoglobin is different from the cooperative oxygen binding in hemoglobin, since positive collaboration is a property of multimeric/oligomeric proteins only. Instead, the binding of oxygen by myoglobin is uninfluenced by the oxygen pressure in the surrounding tissue. Myoglobin is frequently referred to as having an "instant binding tenacity" to oxygen given its hyperbolic oxygen dissociation curve. Different organisms are able to hold their breaths longer due to high concentrations of myoglobin in their muscle cells. Myoglobin is responsible for the pigments that make meat red. The color of the meat is partly determined by the charge of the iron atom in myoglobin and the oxygen attached to it. Myoglobin is found in Type I muscle, Type II A and Type II B, but it is mostly deemed that myoglobin is not found in smooth muscle. Myoglobin is discharged from damaged muscle tissue (rhabdomyolysis), which contains very high concentrations of myoglobin. Even though the released myoglobin is filtered by the kidneys, it is toxic to the renal tubular epithelium and thus may cause acute renal failure.
