biological source
mouse
Quality Level
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
AN5, monoclonal
form
buffered aqueous solution
mol wt
antigen ~35 kDa
species reactivity
human
technique(s)
immunocytochemistry: suitable
indirect ELISA: suitable
microarray: suitable
western blot: 0.5-1 μg/mL using HeLa total cell extract
isotype
IgG1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... ANXA5(308)
General description
Monoclonal Anti-Annexin V (mouse IgG1 isotype) is derived from the hybridoma AN5 produced by the fusion of mouse myeloma cells (NS1 cells) and splenocytes from BALB/c mice immunized with purified human Annexin V. Annexin V belongs to a class of Ca2+-dependent binding proteins. the amino acid sequence of the annexin V protein consists of a core of four repeats of a highly conserved 70 amino acid residue motif and a unique N-terminal tail. Within each repeat, there is a 17 amino acid residue consensus sequence, which is postulated to form part of the Ca2+ and/or phospholipid binding site.
Immunogen
purified human annexin V.
Application
Monoclonal Anti-Annexin V antibody produced in mouse has been used in:
- immunocytochemistry
- indirect immunofluorescence
- immunohistochemistry
- western blotting
- enzyme linked immunosorbent assay (ELISA)
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Storage Class Code
10 - Combustible liquids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
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Clustering seems to be employed by many receptors for transmembrane signaling. Here, we show that acid sphingomyelinase (ASM)-released ceramide is essential for clustering of CD95. In vitro and in vivo, extracellularly orientated ceramide, released upon CD95-triggered translocation of ASM to
Domain IV of Annexin A5 Is Critical for Binding Calcium and Guarantees Its Maximum Binding to the Phosphatidylserine Membrane
Wang J, et al.
Molecules (Basel), 22(12), 2256-2256 (2017)
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Bregano LC, et al.
Brazilian Journal of Veterinary Pathology, 3(2), 16-16 (2010)
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