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인용 및 참조 문헌 (10)
Invitrogen™
SYPRO™ Ruby Protein Blot Stain
Compatible with immunostaining (Western blotting), microsequencing and mass spectrometry
| 카탈로그 번호 | 수량 |
|---|---|
| S11791 | 200 mL |
카탈로그 번호 S11791
제품 가격(KRW)
333,000
온라인 행사
Ends: 31-Mar-2026
380,000할인액 47,000 (12%)
Each
수량:
200 mL
제품 가격(KRW)
333,000
온라인 행사
Ends: 31-Mar-2026
380,000할인액 47,000 (12%)
Each
SYPRO™ Ruby protein blot stain is a highly sensitive, ready-to-use fluorescent stain for proteins on nitrocellulose or PVDF membranes. Stained proteins can be viewed with a standard UV transilluminator or with a laser scanner.
Protein Gel Electrophoresis, Protein Gel Staining and Imaging, Proteins, Expression, Isolation and Analysis
SYPRO Ruby Protein Blot Stain is a highly sensitive, ready-to-use fluorescent stain for proteins on nitrocellulose or PVDF membranes, making it easy to assess the efficiency of protein transfer to the blot and to determine if lanes are loaded equally. It is compatible with immunostaining (western blotting), microsequencing, and mass spectrometry. Stained proteins can be viewed with blue-LED or UV transilluminator, or with imaging equipment with appropriate filters or laser.
For Research Use Only. Not for use in diagnostic procedures.
사양
검출 위치In-Blot Detection
검출 방법Fluorescence
수량200 mL
배송 조건Room Temperature
타겟 분자Protein
라벨 또는 염료SYPRO Ruby
제품라인SYPRO
제품 유형Protein Blot Stain
Unit SizeEach
구성 및 보관
Store at room temperature and protect from light.
자주 묻는 질문(FAQ)
I have stained my blot with Pro-Q Diamond Phosphoprotein Blot Stain. Can I also stain the blot with SYPRO Ruby Blot Stain for total protein detection?
인용 및 참조 문헌 (10)
인용 및 참조 문헌
Abstract
Laser capture microdissection and protein microarray analysis of human non-small cell lung cancer: differential epidermal growth factor receptor (EGPR) phosphorylation events associated with mutated EGFR compared with wild type.
Journal:Mol Cell Proteomics
PubMed ID:18687633
'Little is known about lung carcinoma epidermal growth factor (EGF) kinase pathway signaling within the context of the tissue microenvironment. We quantitatively profiled the phosphorylation and abundance of signal pathway proteins relevant to the EGF receptor within laser capture microdissected untreated, human non-small cell lung cancer (NSCLC) (n = 25)
Novel observations of Thiobacterium, a sulfur-storing Gammaproteobacterium producing gelatinous mats.
Journal:ISME J
PubMed ID:20220790
The genus Thiobacterium includes uncultivated rod-shaped microbes containing several spherical grains of elemental sulfur and forming conspicuous gelatinous mats. Owing to the fragility of mats and cells, their 16S ribosomal RNA genes have not been phylogenetically classified. This study examined the occurrence of Thiobacterium mats in three different sulfidic marine
Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress.
Journal:J Biol Chem
PubMed ID:10922362
Hyperhomocysteinemia, a risk factor for vascular disease, injures endothelial cells through undefined mechanisms. We previously identified several homocysteine-responsive genes in cultured human vascular endothelial cells, including the endoplasmic reticulum (ER)-resident molecular chaperone GRP78/BiP. Here, we demonstrate that homocysteine induces the ER stress response and leads to the expression of a
TrkB has a cell-autonomous role in the establishment of hippocampal Schaffer collateral synapses.
Journal:J Neurosci
PubMed ID:15829629
Neurotrophin signaling has been implicated in the processes of synapse formation and plasticity. To gain additional insight into the mechanism of BDNF and TrkB influence on synapse formation and synaptic plasticity, we generated a conditional knock-out for TrkB using the cre/loxp system. Using three different cre-expressing transgenic mice, three unique
A thousand points of light: the application of fluorescence detection technologies to two-dimensional gel electrophoresis and proteomics.
Journal:Electrophoresis
PubMed ID:10786886
As proteomics evolves into a high-throughput technology for the study of global protein regulation, new demands are continually being placed upon protein visualization and quantitation methods. Chief among these are increased detection sensitivity, broad linear dynamic range and compatibility with modern methods of microchemical analyses. The limitations of conventional protein