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인용 및 참조 문헌 (14)
Invitrogen™
Alexa Fluor™ 488 Hydroxylamine
Alexa Fluor™ 488 Hydroxylamine is useful as a cell tracer and as a reactive dye for labeling aldehydes or ketones자세히 알아보기
| 카탈로그 번호 | 수량 |
|---|---|
| A30629 A-30629으로도 사용됨 | 1 mg |
카탈로그 번호 A30629
A-30629으로도 사용됨
제품 가격(KRW)견적 요청하기
-
수량:
1 mg
Alexa Fluor™ 488 Hydroxylamine is useful as a cell tracer and as a reactive dye for labeling aldehydes or ketones in polysaccharides or glycoproteins. Alexa Fluor™ 488 is a bright, green fluorescent dye with excitation ideally suited to the 488 nn laser line. Used for stable signal generation in imaging and flow cytometry, Alexa Fluor™ 488 dye is water soluble and pH-insensitive from pH 4 to pH 10. In addition to reactive dye formulations, we offer Alexa Fluor™ 488 dye conjugated to a variety of antibodies, peptides, proteins, tracers, and amplification substrates optimized for cellular labeling and detection.
Detailed information about this AlexaFluor™ Hydroxylamine:
- Fluorophore label: Alexa Fluor™ 488 dye
- Reactive group: Hydroxylamine
- Reactivity: Aldehydes or ketones
- Ex/Em of the conjugate: 494/518 nm
- Extinction coefficient: 77,000 cm-1M-1
- Spectrally similar dyes: FITC, GFP
- Molecular weight: 895.07
Cell Tracking and Tracing Applications
Alexa Fluor™ hydrazides and Hydroxylamines are useful as low molecular weight, membrane-impermeant, aldehyde-fixable cell tracers, exhibiting brighter fluorescence and greater photostability than cell tracers derived from other spectrally similar fluorophores. They are easily loaded into cells by microinjection, infusion from patch pipette, or uptake induced by our Influx™ Pinocytic Cell-Loading Reagent (Cat. No. I14402).
Glycoprotein and Polysaccharide Labeling Applications
The Alexa Fluor™ hydrazides and Hydroxylamines are reactive molecules that can be used to add a fluorescent label to biomolecules containing aldehydes or ketones. Aldehydes and ketones can be introduced into polysaccharides and glycoproteins by periodate-mediated oxidation of vicinal diols. Galactose oxidase can also be used to oxidize terminal galactose residues of glycoproteins to aldehydes.
Hydrazide vs Hydroxylamine
Hydrazine derivatives react with ketones and aldehydes to yield relatively stable hydrazones. Hydroxylamine derivatives (aminooxy compounds) react with aldehydes and ketones to yield oximes. Oximes are superior to hydrazones with respect to hydrolytic stability. Both hydrazones and oximes can be reduced with sodium borohydride (NaBH4) to further increase the stability of the linkage.
Learn More About Protein and Antibody Labeling
We offer a wide selection of Molecular Probes™ antibody and protein labeling kits to fit your starting material and your experimental setup. See our Antibody Labeling kits or use our Labeling Chemistry Selection Tool for other choices. To learn more about our labeling kits, read Kits for Labeling Proteins and Nucleic Acids—Section 1.2 in The Molecular Probes™ Handbook.
We'll Make a Custom Conjugate for You
If you can't find what you're looking for in our online catalog, we'll prepare a custom antibody or protein conjugate for you. Our custom conjugation service is efficient and confidential, and we stand by the quality of our work. We are ISO 13485:2000 certified.
Related Products
- DMSO (dimethylsulfoxide) (Cat. No. D12345)
- Antibody Conjugate Purification Kit for 0.5-1 mg (A33086)
- Antibody Conjugate Purification Kit for 20-50 μg (A33087)
- Antibody Conjugate Purification kit for 50-100 μg (A33088)
For Research Use Only. Not for use in diagnostic procedures.
사양
화학물질 반응성Carboxylic Acid, Ketone, Aldehyde
여기494 nm
라벨 또는 염료Alexa Fluor™ 488
제품 유형Hydroxylamine
수량1 mg
반응성 부분Amine, Hydroxylamine
배송 조건Room Temperature
라벨 유형Alexa Fluor
제품라인Alexa Fluor
Unit SizeEach
구성 및 보관
Store in freezer (-5°C to -30°C) and protect from light.
인용 및 참조 문헌 (14)
인용 및 참조 문헌
Abstract
Optical properties of Alexa 488 and Cy5 immobilized on a glass surface.
Journal:Biotechniques
PubMed ID:15679095
'The absorption and emission spectra were measured for Cy5 and Alexa 488 fluorophores confined on a glass surface. The data were obtained using fluorometry and spectroscopic ellipsometry. Red shifts of the surface-immobilized fluorophore absorption spectra relative to the fluorophore spectra in aqueous solution were observed using both methods. We interpret
Multiple site-specific in vitro labeling of single-chain antibody.
Journal:Bioconjug Chem
PubMed ID:19507852
'For multiple site-specific conjugations of bioactive molecules to a single-chain antibody (scFv) molecule, we have constructed a human anti HER2 receptor, scFv, with a C-terminal fusion polypeptide containing 1, 3, or 17 threonine (Thr) residues. The C-terminal extended fusion polypeptides of these recombinant scFv fusion proteins are used as the
A general and efficient method for the site-specific dual-labeling of proteins for single molecule fluorescence resonance energy transfer.
Journal:J Am Chem Soc
PubMed ID:19108697
'A general strategy for the site-specific dual-labeling of proteins for single-molecule fluorescence resonance energy transfer is presented. A genetically encoded unnatural ketone amino acid was labeled with a hydroxylamine-containing fluorophore with high yield (>95%) and specificity. This methodology was used to construct dual-labeled T4 lysozyme variants, allowing the study of
Site-specific chemical modification of recombinant proteins produced in mammalian cells by using the genetically encoded aldehyde tag.
Journal:Proc Natl Acad Sci U S A
PubMed ID:19202059
'The properties of therapeutic proteins can be enhanced by chemical modification. Methods for site-specific protein conjugation are critical to such efforts. Here, we demonstrate that recombinant proteins expressed in mammalian cells can be site-specifically modified by using a genetically encoded aldehyde tag. We introduced the peptide sequence recognized by the
Detection of labeled abasic sites in damaged DNA by capillary electrophoresis with laser-induced fluorescence.
Journal:Anal Bioanal Chem
PubMed ID:17206410
'Removal of nucleobases from the DNA backbone leads to the formation of abasic sites. The rate of abasic site formation is significantly increased for chemically damaged nucleobases. Thus, abasic sites serve as general biomarkers for the quantification of DNA damage. Herein, we show that capillary electrophoresis with laser-induced fluorescence (CE-LIF)