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Citations & References (6)
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Tetramethylrhodamine Cadaverine, 5-(and-6)-((N-(5-Aminopentyl) Amino) Carbonyl) Tetramethylrhodamine, mixed isomers
The primary aliphatic amine of tetramethylrhodamine cadaverine can be reversibly coupled to aldehydes and ketones to form a Schiff baseRead more
| Catalog Number | Quantity |
|---|---|
| A1318 also known as A-1318 | 10 mg |
Catalog number A1318
also known as A-1318
Price (BRL)
-
Quantity:
10 mg
The primary aliphatic amine of tetramethylrhodamine cadaverine can be reversibly coupled to aldehydes and ketones to form a Schiff base - which can be reduced to a generate stable amine derivative by sodium borohydride (NaBH4) or sodium cyanoborohydride (NaCNH3). Carboxylic acids of proteins and other water-soluble biopolymers can be coupled to this molecule in aqueous solution using water-soluble carbodiimides such as EDAC (E2247). This material consists of the 5- and 6- isomer. Please see the structure for additional details.
For Research Use Only. Not for use in diagnostic procedures.
Specifications
Chemical ReactivityCarboxylic Acid, Ketone, Aldehyde
Label or DyeTMR (Tetramethylrhodamine)
Product TypeTetramethylrhodamine Cadaverine
Quantity10 mg
Reactive MoietyAmine, Cadaverine
Shipping ConditionRoom Temperature
Label TypeClassic Dyes
Unit SizeEach
Contents & Storage
Store in freezer (-5 to -30°C) and protect from light.
Citations & References (6)
Citations & References
Abstract
Antagonistic effects of cofilin, beryllium fluoride complex, and phalloidin on subdomain 2 and nucleotide-binding cleft in F-actin.
Journal:Biophys J
PubMed ID:16997870
'Cofilin/ADF, beryllium fluoride complex (BeFx), and phalloidin have opposing effects on actin filament structure and dynamics. Cofilin/ADF decreases the stability of F-actin by enhancing disorder in subdomain 2, and by severing and accelerating the depolymerization of the filament. BeFx and phalloidin stabilize the subdomain 2 structure and decrease the critical
Dynamic polymorphism of single actin molecules in the actin filament.
Journal:Nat Chem Biol
PubMed ID:16415860
'Actin filament dynamics are critical in cell motility. The structure of actin filament changes spontaneously and can also be regulated by actin-binding proteins, allowing actin to readily function in response to external stimuli. The interaction with the motor protein myosin changes the dynamic nature of actin filaments. However, the molecular
Synthesis and characterization of conjugates formed between periodate-oxidized ribonucleotides and amine-containing fluorophores.
Journal:Bioconjug Chem
PubMed ID:7849074
The synthesis and purification of new fluorescently labeled derivatives of GDP and ATP are described. The fluorescent groups are coupled initially through amine-containing linker arms to periodate-oxidized nucleotides. Reduction of the initial product yields primarily a six-membered morpholine-like ring. Fluorescein-labeled GDP, rhodamine-labeled GDP, and fluorescein-labeled ATP were characterized by absorbance
The mitogen-activated protein kinase kinase kinase dual leucine zipper-bearing kinase (DLK) acts as a key regulator of keratinocyte terminal differentiation.
Journal:J Biol Chem
PubMed ID:15695824
In the skin, epithelial cells undergo a terminal differentiation program leading to the formation of the stratum corneum. Although it is expected that the last phases of this process must be tightly regulated since it results in cell death, the signaling pathways involved in this induction remain ill defined. We
Orientation of actin monomer in the F-actin filament: radial coordinate of glutamine-41 and effect of myosin subfragment 1 binding on the monomer orientation.
Journal:Biochemistry
PubMed ID:3166995
We have employed the method of radial distance measurements in order to orient the actin monomer in the F-actin filament. This method utilizes fluorescence resonance energy transfer measurements of the distance between two equivalent chemical points located on two different monomers. The interprobe distance obtained this way is used to