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Key Documents

A9460

Sigma-Aldrich

Annexin V from human placenta

≥90% (SDS-PAGE), buffered aqueous solution

Synonyme(s) :

Annexin V, Calphosbindin I, Lipocortin V, PAP-1

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About This Item

Code UNSPSC :
41106305
Nomenclature NACRES :
NA.32

Source biologique

human placenta

Niveau de qualité

Pureté

≥90% (SDS-PAGE)

Forme

buffered aqueous solution

Poids mol.

33 kDa (four subunits)

Technique(s)

cell based assay: suitable

Impuretés

Human Source(HCV), tested negative

Solubilité

water: soluble

Adéquation

suitable for molecular biology

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−70°C

Informations sur le gène

human ... ANXA5(308)

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Description générale

Research area: Apoptosis

Annexin V is a calcium-dependent phospholipid-binding protein. It is expressed in high concentration in cells with barrier functions, such as vascular endothelium, epithelial cells in bile ducts, placental trophoblasts, mammary ducts, renal tubules, and nasal epithelium.

Application

Annexin V from human placenta has been used:
  • to verify the involvement of phosphatidylserine in adhesion using flow cytometry
  • to test adhesion specificity of phosphatidylserine
  • for synthesis of NIR700-Annexin-V imaging probe
  • in dynamic light scattering (DLS) assay to test the effects of various treatments on virion aggregation

Actions biochimiques/physiologiques

Annexins are ubiquitous homologous proteins that bind phospholipids in the presence of calcium. The cellular changes involved in the apoptotic process include loss of phospholipid asymmetry during the early stages. This phenomenon is universal and is not limited to stimulus or to mammalian cells, but also occurs in insect and plant cells. In living cells, phosphatidylserine is transported to the inside of the lipid bilayer by the Mg2+ATP dependent enzyme, aminophospholipid translocase. At the onset of apoptosis, phosphatidylserine becomes translocated to the external surface of the cell membrane. Since the movement of phosphatidylserine from the internal membrane surface to the external surface is an early indicator of apoptosis, annexin V and its conjugates that interact strongly and specifically with phosphatidylserine may be used to detect apoptosis. Annexin V conjugates can be used to detect apoptotic cells significantly earlier than DNA-based assays. Fluorescent dye labeled annexin V have applications in flow cytometry, fluorescence microscopy, and laser scanning cytometry.
It is a widely used marker for identifying apoptotic cells due to its high affinity for phosphatidylserine, which is normally located on the inner leaflets of membranes but moves to the cell surface during programmed cell death.

Conditionnement

Package size based on protein content

Forme physique

Solution in 40 mM Tris-HCl, pH 7.5, containing 150 mM NaCl, 1 mM DTT and 0.05% sodium azide.

Code de la classe de stockage

12 - Non Combustible Liquids

Classe de danger pour l'eau (WGK)

WGK 2

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Les clients ont également consulté

W J Buhl et al.
European journal of cell biology, 56(2), 381-390 (1991-12-01)
Membranes from human placenta contain proteins which inhibit the activity of phospholipases A2 by binding to phospholipid thus impeding substrate availability. We used unilamellar mixed liposomes and a partially purified cytosolic phospholipase A2 from placenta for characterizing this substrate-depleting activity.
B N Yamaja Setty et al.
Blood, 99(5), 1564-1571 (2002-02-28)
Phosphatidlyserine (PS) exposure on the erythrocyte surface endows the cell with the propensity of adhering to vascular endothelium. Because individuals with sickle cell disease (SCD) manifest loss of erythrocyte membrane asymmetry with PS exposure, we have assessed the contribution of
D D Schlaepfer et al.
Biochemistry, 31(6), 1886-1891 (1992-02-18)
Annexin V is a protein of unknown biological function that undergoes Ca(2+)-dependent binding to phospholipids located on the cytosolic face of the plasma membrane. Preliminary results presented herein suggest that a biological function of annexin V is the inhibition of
Yeast alcohol dehydrogenase: SH groups, disulfide groups, quaternary structure, and reactivation by reductive cleavage of disulfide groups.
M Bühner et al.
European journal of biochemistry, 11(1), 73-79 (1969-11-01)
Ke Chen et al.
Journal of biomedical science, 18, 57-57 (2011-08-17)
High glucose induced lipid synthesis leads to β cell glucolipotoxicity. Sterol regulatory element binding protein-1c (SREBP-1c) is reported to be partially involved in this process. Insulin induced gene-1 (Insig-1) is an important upstream regulator of Insig-1-SREBPs cleavage activating protein (SCAP)-SREBP-1c

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