A 1:2000 dilution of SMC-261 was sufficient for detection of Vimentin in 10 µg of Human, Mouse, Rat, HeLa, Brain cell lysates by ECL immunoblot analysis using Goat Anti-Mouse IgG:HRP as the secondary antibody.
Biological Description
Alternative Names
CTRCT30 Antibody, Epididymis luminal protein 113 Antibody, HEL113 Antibody, VIM Antibody, VIME_HUMAN Antibody, Vimentin Antibody
Cellular Localization
Cytoplasm
Accession Number
NP_003371.2
Gene ID
7431
Swiss Prot
P08670
Scientific Background
Vimentin is a type III intermediate filament (IF) protein. All IF proteins are highly expressed and vimentin is the major cytoskeletal component of mesechymal, and therefore Vimentin is used as a marker of mesenchymally-derived cells or cells undergoing EMT during both normal development and metastic progression. Functionally it also serves a significant role in supporting and anchording the organelles in the cytosol. Clinical significance includes being used as a sarcoma tumor marker, and it has also been used in the diagnosis of rheumatoid arthritis.
References
1. Katsumoto T., Mitsushima A., Kurimura T. (1990). Biol Cell. 68(2): 139–146.
2. Leader M, Collins M, Patel J, Henry K (1987). Histopathology 11(1): 63–72.
3. Immunohistochemistry from the Washington Animal Disease Diagnostic laboratory (WADDL)of the College of Veterinary Medicine, Washington State University. Retrieved 2009-03-14.
Western Blot analysis of Human, Mouse, Rat HeLa, Brain cell lysates showing detection of ~50-57 kDa Vimentin protein using Mouse Anti-Vimentin Monoclonal Antibody, Clone 1A7 (SMC-261). Lane 1: Human HeLa. Lane 2: Mouse Brain. Lane 3: Rat Brain.. Primary Antibody: Mouse Anti-Vimentin Monoclonal Antibody (SMC-261) at 1:2000. Predicted/Observed Size: ~50-57 kDa.
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Biotin
Properties:
Binds tetrameric avidin proteins including Streptavidin and neuravidin with very high affinity
Molar mass: 244.31 g/mol
Formula: C10H16N2O3S
Applications: Western blot, immunohistochemistry, and ELISA
① 电泳分离4种核苷酸时应取pH3.5 的缓冲液,在该pH时,这4种单核苷酸之间所带负电荷差异较大,它们都向正极移动,但移动的速度不同,依次为:UMP>GMP>AMP>CMP; ② 应取pH8.0,这样可使核苷酸带较多负电荷,利于吸附于阴离子交换树脂柱。虽然pH 11.4时核苷酸带有更多的负电荷,但pH过高对分离不利。 ③ 当不考虑树脂的非极性吸附时,根据核苷酸负电荷的多少来决定洗脱速度,则洗脱顺序为CMP>AMP> GMP > UMP,但实际上核苷酸和聚苯乙烯阴离子交换树脂之间存在着非极性吸附,嘌呤碱基的非极性吸附是嘧啶碱基的3倍。静电吸附与非极性吸附共同作用的结果使洗脱顺序为:CMP> AMP > UMP >GMP。