| 产品名称: Fascin1 蛋白 |
| 货号 10150 |
| 产品全名: Fascin1 蛋白 |
| 基因符号 Fascin homolog 1, actin-bundling protein, FSCN1, SNL, p55 |
| Source: Human, recombinant full length, his-tag |
| Expression 种属反应性: E. coli |
| 分子量: 55 kDa |
| 纯化: >95% by SDS-PAGE |
| Introduction: Fascin is an ~58 kDa monomeric actin filament bundling protein. It is required to maximally cross-link the actin filaments into straight, compact, and rigid bundles, and contributes to the formation of filopodia that are critical for cell migration. Elevated levels of fascin have been found in metastatic tumors and are correlated with clinically aggressive phenotypes, poor prognosis, and shorter survival. |
| Amino Acid Sequence (1-493) |
MTANGTAEAVQIQFGLINCGNKYLTAEAFGFKVNASASSLKKKQIWTLEQPPDEAGSAAVCLRSHLG
RYLAADKDGNVTCEREVPGPDCRFLIVAHDDGRWSLQSEAHRRYFGGTEDRLSCFAQTVSPAEKWSV
HIAMHPQVNIYSVTRKRYAHLSARPADEIAVDRDVPWGVDSLITLAFQDQRYSVQTADHRFLRHDGRLVA
RPEPATGYTLEFRSGKVAFRDCEGRYLAPSGPSGTLKAGKATKVGKDELFALEQSCAQVVLQAANERNV
STRQGMDLSANQDEETDQETFQLEIDRDTKKCAFRTHTGKYWTLTATGGVQSTASSKNASCYFDIEWRD
RRITLRASNGKFVTSKKNGQLAASVETAGDSELFLMKLINRPIIVFRGEHGFIGCRKVTGTLDANRSSYD
VFQLEFNDGAYNIKDSTGKYWTVGSDSAVTSSGDTPVDFFFEFCDYNKVAIKVGGRYLKGDHAGVLKA
SAETVDPASLWEY |
Properties
|
| Physical Appearance (form): Dissolved in 20mM Tris-HCl, pH8.0, 150mM NaCl. |
| Physical Appearance (form): White or clear. |
| Concentration: 1 mg/mL |
| Storage: -80°C |
Preparation Instructions:
Centrifuge the vial before open the cap and reconstitute in water. Adding of 10 mM β-mercaptoethanol or 1 mM DTT into the solution to protect the protein is recommended and using of non-ionic detergents such as n-Dodecyl β-D-maltoside(DoDM) or polyethylene detergents (e.g. C12E10) also help to stabilize the protein. Avoid repeated freezing and thawing after reconstitution. The purity of His6-tagged. Fascin was determined by SDS-PAGE and Coomassie Brilliant Blue Staining |
References:
1. Mosialos, G. et al., Am. J. Path. 148: 593-600, 1996.
2. Ono, S. et al., J. Biol. Chem. 272: 2527-2533, 1997.
3. Pinkus, G. S. et al., Am. J. Path. 150: 543-562, 1997.
