生物来源
mouse
质量水平
偶联物
unconjugated
抗体形式
ascites fluid
抗体产品类型
primary antibodies
克隆
BA-4, monoclonal
分子量
antigen 67.5 kDa
包含
15 mM sodium azide
种属反应性
human, goat, sheep, guinea pig, pig, canine, feline, bovine
包装
antibody small pack of 25 μL
技术
immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:5,000 using sheep arterial tissue
microarray: suitable
同位素/亚型
IgG1
UniProt登记号
运输
dry ice
储存温度
−20°C
靶向翻译后修饰
unmodified
基因信息
human ... ELN(2006)
相关类别
一般描述
Monoclonal Anti-Elastin (mouse IgG1 isotype) is derived from the hybridoma produced by the fusion of mouse myeloma cells and splenocytes from an immunized mouse. Elastin is an important polymeric protein of connective tissue. It is synthesized and secreted as a soluble single-chain protein (tropoelastin) that undergoes numerous post-ribosomal modifications prior to the organization of the elastic fiber in the extracellular space.
特异性
The antibody binds to insoluble elastin, α-elastin, tropoelastin (the soluble non-cross linked precursor of elastin) and to peptide fragments generated by proteolytic digestion of insoluble elastin. In tropoelastin preparations, three immunoreactive bands have been observed at 67.5 kDa, 65 kDa and 62 kDa corresponding to the three elastin isoforms. The antibody is specific for an epitope composed of the repeated sequence in elastin: Val-Gly-Val-Ala-Pro-Gly. This epitope has been shown to be a chemoattractant for fibroblasts and monocytes.
免疫原
bovine α-elastin.
应用
Monoclonal Anti-Elastin antibody produced in mouse has been used in:
- immunohistochemistry
- immunostaining
- immunoblotting
生化/生理作用
Elastin is encoded by the ELN gene in humans. It is a polymeric protein in connective tissue that has exceptional properties of extension, elastic recoil to the extracellular matrix and allows many tissues in the body to resume their shape after stretching or contracting. Elastin is a self-assembling, extracellular-matrix protein providing tissue elasticity and is predominantly comprised of cross-linked tropoelastin. It plays an important role in the atherosclerotic process. The conformational disorder is caused due to a constitutive feature of elastin structure and function.
Elastin undergoes changes of morphology with aging and in many disease states. For example, abnormal accumulation of connective tissue in blood vessels contributes to alterations in vascular physiology associated with diseases such as hypertension and atherosclerosis. Several heritable diseases such as Marfan syndrome, pseudoxanthoma elasticum and the Buschke-Ollendorf syndrome may result from molecular defects of elastin.
免责声明
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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WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
法规信息
常规特殊物品
Exercise training enhances elastin, fibrillin and nitric oxide in the aorta wall of spontaneously hypertensive rats
Experimental and Molecular Pathology, 89(3), 351-357 (2010)
International journal of molecular sciences, 21(6) (2020-03-28)
An adenoviral vector (Ad) expressing a Wnt decoy receptor (sLRP6E1E2) is known to induce an anti-fibrotic effect by inhibiting Wnt signaling. We evaluated its effects in vivo using pig models and attempted to introduce an alginate gel-matrix system to prolong
The Journal of biological chemistry, 289(14), 10057-10068 (2014-02-20)
Elastin is the intrinsically disordered polymeric protein imparting the exceptional properties of extension and elastic recoil to the extracellular matrix of most vertebrates. The monomeric precursor of elastin, tropoelastin, as well as polypeptides containing smaller subsets of the tropoelastin sequence
Fabricated elastin
Advanced Helathcare Materials, 4(16), 2530-2530 (2015)
Investigative ophthalmology & visual science, 59(1), 322-329 (2018-01-19)
We examined the pattern and extent of connective tissue distribution in the extraocular muscles (EOMs) and determined the ability of the interconnected connective tissues to disseminate force laterally. Human EOMs were examined for collagens I, III, IV, and VI; fibronectin;
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