Thermo Scientific Pierce AMAS is an amine-to-sulfhydryl crosslinker that contains NHS-ester and maleimide reactive groups at opposite ends of aLeia mais
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Número do catálogo
Quantity
22295
50 mg
Número do catálogo 22295
Preço (BRL)
-
Quantity:
50 mg
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Thermo Scientific Pierce AMAS is an amine-to-sulfhydryl crosslinker that contains NHS-ester and maleimide reactive groups at opposite ends of a very short spacer arm (4.4 angstroms).
Features of AMAS:
• Reactive groups: NHS ester and maleimide • Reactive towards: amino and sulfhydryl groups • Shortest of aliphatic spacer series which includes AMAS, BMPS, GMBS and EMCS • NHS ester end couples with primary amines at pH 7-9, forming stable amide bonds • Maleimide reacts with -SH groups at pH 6.5-7.5, forming stable thioether linkages • Non-cleavable • Water-insoluble (dissolve first in DMF or DMSO) • Very short aliphatic spacer has low potential for eliciting an immune response
For Research Use Only. Not for use in diagnostic procedures.
Especificações
Cell PermeabilityYes
DescriptionAMAS
FormPowder
Labeling MethodChemical Labeling
Molecular Weight (g/mol)252.18
PEGylatedNo
Product LinePierce
Quantity50 mg
Reactive MoietyMaleimide, NHS Ester
Shipping ConditionAmbient
SolubilityDMF, DMSO
Spacer Arm Length4.4 Å
Water SolubleNo
Chemical ReactivityAmine-Sulfhydryl
CleavableNo
Crosslinker TypeHeterobifunctional
FormatStandard
Product TypeCrosslinker
SpacerShort (<10 Å)
Unit SizeEach
Conteúdo e armazenamento
Upon receipt store desiccated at 4°C.
Frequently asked questions (FAQs)
Can you provide the shelf-life for AMAS (N-α-maleimidoacet-oxysuccinimide ester)?
AMAS (N-α-maleimidoacet-oxysuccinimide ester is covered under our general 1-year warranty and is guaranteed to be fully functional for 12 months from the date of shipment, if stored as recommended. Please see section 8.1 of our Terms & Conditions of Sale (https://www.thermofisher.com/content/dam/LifeTech/Documents/PDFs/Terms-and-Conditions-of-Sale.pdf) for more details.
Dual binding mode of the nascent polypeptide-associated complex reveals a novel universal adapter site on the ribosome.
Authors:Pech M, Spreter T, Beckmann R, Beatrix B
Journal:J Biol Chem
PubMed ID:20410297
'Nascent polypeptide-associated complex (NAC) was identified in eukaryotes as the first cytosolic factor that contacts the nascent polypeptide chain emerging from the ribosome. NAC is present as a homodimer in archaea and as a highly conserved heterodimer in eukaryotes. Mutations in NAC cause severe embryonically lethal phenotypes in mice, Drosophila ... More
Analysis of RovA, a transcriptional regulator of Yersinia pseudotuberculosis virulence that acts through antirepression and direct transcriptional activation.
'The transcription factor RovA of Yersinia pseudotuberculosis and analogous proteins in other Enterobacteriaceae activate the expression of virulence genes that play a crucial role in stress adaptation and pathogenesis. In this study, we demonstrate that the RovA protein forms dimers independent of DNA binding, stimulates RNA polymerase, most likely via ... More
A central role for the T1 domain in voltage-gated potassium channel formation and function.
To interpret the recent atomic structures of the Kv (voltage-dependent potassium) channel T1 domain in a functional context, we must understand both how the T1 domain is integrated into the full-length functional channel protein and what functional roles the T1 domain governs. The T1 domain clearly plays a role in ... More
Spatial and dynamic interactions between phospholamban and the canine cardiac Ca2+ pump revealed with use of heterobifunctional cross-linking agents.
Authors:Chen Z, Stokes DL, Rice WJ, Jones LR
Journal:J Biol Chem
PubMed ID:12972413
Heterobifunctional thiol to amine cross-linking agents were used to gain new insights on the dynamics and conformational factors governing the interaction between the cardiac Ca2+ pump (SERCA2a) and phospholamban (PLB). PLB is a small protein inhibitor of SERCA2a that reduces enzyme affinity for Ca2+ and thereby regulates cardiac contractility. We ... More