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- 文献和实验
- 技术资料
- 保存条件：
−20°C
- 保质期：
根据瓶身LOT号查询
- 英文名：
Human EGF, Animal-Free Recombinant Protein
- 库存：
有现货
- 供应商：
浙江羽翔生物科技有限公司
- 规格：
100ug
产品信息
应用 建议稀释比
对照试剂 (Ctrl) Assay-dependent
体外检测 (In vitro)
其他PubMed (Misc)
Western blot control (WB Ctrl) Assay-dependent
ELISA standard (ELISA Std) Assay-dependent
Bioactivity (Bioactivity) Assay-dependent
Cell culture (Cell Clt)
Cell differentiation (Cell Diff)
Cell stimulation (Cell Stm)
Cell induction (Cell Ind)
Cell expansion (Cell Exp)
PSC/iPSC (PSC/iPSC)
产品规格
种属
Human
已发表种属
Amphibian, Bat, Bovine, Cat, Chicken, Chordate, Dog, Hamster, Horse, Human, Mollusc, Mouse, Non-human primate, Panda, Pig, Rabbit, Rat, Reptile, Sheep, Zebrafish
Expression System
E. coli
氨基酸序列
NSDSECPLSH DGYCLHDGVC MYIEALDKYA CNCVVGYIGE RCQYRDLKWW ELR
分子量
6.2 kDa
分类
Recombinant
类型
Protein
纯度
≥ 98% by SDS-PAGE gel and HPLC analyses.
内毒素浓度
<0.1 EU/µg
活性
The ED50 was determined by a cell proliferation assay using balb/c 3T3 cells is ≤ 0.1 ng/ml, corresponding to a specific activity of ≥ 1 x 10^7 units/mg.
偶联物
Unconjugated
形式
Lyophilized
Amount
100 µg
纯化类型
purified
内含物
no preservative
保存条件
-20°C
运输条件
Ambient
产品详细信息
Recombinant Human EGF is a 6.2 kDa globular protein containing 53 amino acid residues, including 3 intramolecular disulfide bonds.
This product is shipped at ambient temperature. For storage, handling and reconstitution information, please see the lot-specific Certificate of Analysis
靶标信息
EGF (Epidermal growth factor) exerts its actions by binding to the EGF Receptor, a 170 kDa protein kinase. Activation of EGFR initiates diverse cellular pathways in response to toxic environmental stimuli, or to EGF binding to the receptor, the EGFR forms homo- or heterodimers with other family members. Each dimeric receptor complex initiates a distinct signaling pathway by recruiting different Src homology 2 (SH2) containing effector proteins. EGF is far and wide expressed in kidney, cerebrum, prostrate and salivary glands. EGF acts as a potent mitogenic factor and the phosphorylated receptor recruits adapter proteins like GRB2 that activates complex downstream signaling cascades. EGF activates at least 4 major downstream signaling cascades including the RAS-RAF-MEK-ERK, PI3 kinase-AKT, PLCgamma-PKC and STAT modules. Research studies suggest the protein may also play important role in activating the NF-kappa-B signaling cascade. Defects in the EGGF gene are the cause of hypomagnesemia type 4 and dysregulation has been associated with the growth and progression of certain cancers.
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文献和实验A comparative pharmaco-metabolomic study of glutaminase inhibitors in glioma stem-like cells confirms biological effectiveness but reveals differences in target-specificity
Katharina Koch 1, Rudolf Hartmann 2, Julia Tsiampali 1, Constanze Uhlmann 1, Ann-Christin Nickel 1, Xiaoling He 3, Marcel A Kamp 1, Michael Sabel 1, Roger A Barker 3, Hans-Jakob Steiger 1, Daniel Hänggi 1, Dieter Willbold 2 4, Jaroslaw Maciaczyk # 1 5, Ulf D Kahlert # 1 6
Affiliations Expand
PMID: 32337072 PMCID: PMC7162917 DOI: 10.1038/s41420-020-0258-3
Abstract
Cancer cells upregulate anabolic processes to maintain high rates of cellular turnover. Limiting the supply of macromolecular precursors by targeting enzymes involved in biosynthesis is a promising strategy in cancer therapy. Several tumors excessively metabolize glutamine to generate precursors for nonessential amino acids, nucleotides, and lipids, in a process called glutaminolysis. Here we show that pharmacological inhibition of glutaminase (GLS) eradicates glioblastoma stem-like cells (GSCs), a small cell subpopulation in glioblastoma (GBM) responsible for therapy resistance and tumor recurrence. Treatment with small molecule inhibitors compound 968 and CB839 effectively diminished cell growth and in vitro clonogenicity of GSC neurosphere cultures. However, our pharmaco-metabolic studies revealed that only CB839 inhibited GLS enzymatic activity thereby limiting the influx of glutamine derivates into the TCA cycle. Nevertheless, the effects of both inhibitors were highly GLS specific, since treatment sensitivity markedly correlated with GLS protein expression. Strikingly, we found GLS overexpressed in in vitro GSC models as compared with neural stem cells (NSC). Moreover, our study demonstrates the usefulness of in vitro pharmaco-metabolomics to score target specificity of compounds thereby refining drug development and risk assessment.
Keywords: CNS cancer; Cancer metabolism; Cancer stem cells; Predictive markers; Translational research.
Cell-Free Protein Synthesis as a Promising Expression System for Recombinant Proteins
Cell-free protein synthesis (CFPS) has major advantages over traditional cell-based methods in the capability of high-throughput protein synthesis and special protein production. During recent decades, CFPS has become an alternative protein
An Insect Cell-Free System for Recombinant Protein Expression Using cDNA Resources
results in protein productivity of about 50 μg per mL of the translation reaction mixture. This is the highest protein productivity yet noted among commercialized cell-free protein synthesis systems based on animal extracts.
Methods for Producing Recombinant Human Cellular Retinaldehyde-Binding Protein
The cellular retinaldehyde-binding protein (CRALBP) is expressed at high levels in vertebrate visual trssue, where it may serve to modulate the interaction of 11-cis -retinol with visual-cycle enzymes in the retinal pigment epithelium (RPE
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