产品详情
简单介绍：
重组大鼠表皮生长因子蛋白与其它公司提供的重组蛋白不同，rRtEGF蛋白产品为采用CFS的无细胞麦胚蛋白合成系统表达出来的重组蛋白，可表达出对细胞有毒性、易被蛋白酶降解的蛋白；并获得具有良好的可溶性，并有翻译后修饰、从而部分具有功能的蛋白.同时独有的全自动蛋白纯化技术则简便高效，将蛋白纯化过程中对蛋白的损伤降低到*小程度.重组大鼠表皮生长因子蛋白（全长序列）产品可用于Western Blot验证、抗体制备、蛋白检测、ELISA等试验中.
详情介绍：
重组大鼠表皮生长因子蛋白
| Synonyms | Urogastrone, URG |
| Species | Rat |
| Accession | P07522 |
| GeneID | 25313 |
| Source | Escherichia coli. |
| Molecular Weight | 重组大鼠表皮生长因子蛋白Approximately 6.1 kDa, a single non-glycosylated polypeptide chain containing 53 amino acids, including 3 intramolecular disulfide-bonds. |
| Quantity | 20µg/100µg/1000µg |
| AA Sequence | NSNTGCPPSY DGYCLNGGVC MYVESVDRYV CNCVIGYIGE RCQHRDLRWW KLR |
| Purity | > 97 % by SDS-PAGE and HPLC analyses. |
| Biological Activity | 重组大鼠表皮生长因子蛋白Fully biologically active when compared to standard. The ED50as determined by a cell proliferation assay using murine Balb/c 3T3 cells is less than 0.1 ng/ml, corresponding to a specific activity of > 1.0 × 107IU/mg. |
| Physical Appearance | Sterile Filtered White lyophilized (freeze-dried) powder. |
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS, pH 7.4. |
| Endotoxin | Less than 1 EU/μg of rRtEGF as determined by LAL method. |
| Reconstitution | 重组大鼠表皮生长因子蛋白We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1 % BSA to a concentration of 0.1-1.0 mg/mL. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions. |
| Storage | This lyophilized preparation is stable at 2-8 °C, but should be kept at -20 °C for long term storage, preferably desiccated. Upon reconstitution, the preparation is stable for up to one week at 2-8 °C. For maximal stability, apportion the reconstituted preparation into working aliquots and store at -20 °C to -70 °C. Avoid repeated freeze/thaw cycles. |
| 重组大鼠表皮生长因子蛋白 | |
| SDS-PAGE |  |
| Reference | 1. Chevalier RL, Goyal S, Thornhill BA. 1999. J Urol, 162: 1532-6. 2. Gehm BD, McAndrews JM, Jordan VC, et al. 2000. Mol Cell Endocrinol, 159: 53-62. 3. Yang H, Sun X, Wang Z, et al. 2003. J Membr Biol, 194: 47-58. 4. Cohen S. 2008. J Biol Chem, 283: 33793-7. |
| Background | Epidermal Growth Factor (EGF) was originally discovered in crude preparations of nerve growth factor prepared from mouse submaxillary glands as an activity that induced early eyelid opening, incisor eruption, hair growth inhibition, and stunting of growth when injected into newborn mice. It is prototypic of a family of growth factors that are derived from membrane-anchored precursors. All members of this family are characterized by the presence of at least one EGF structural unit (defined by the presence of a conserved 6 cysteine motif that forms three disulfide bonds) in their extracellular domain. EGF is initially synthesized as a 130 kDa precursor transmembrane protein containing 9 EGF units. The mature soluble EGF sequence corresponds to the EGF unit located proximal to the transmembrane domain. The membrane EGF precursor is capable of binding to the EGF receptor and was reported to be biologically active. Mature rat EGF shares 70 % a.a. sequence identity with mature human EGF. |
