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Merck

A9460

Sigma-Aldrich

Annexin V from human placenta

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

Sinónimos:

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

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About This Item

UNSPSC Code:
41106305
NACRES:
NA.32

biological source

human placenta

Quality Level

assay

≥90% (SDS-PAGE)

form

buffered aqueous solution

mol wt

33 kDa (four subunits)

technique(s)

cell based assay: suitable

impurities

Human Source(HCV), tested negative

solubility

water: soluble

suitability

suitable for molecular biology

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... ANXA5(308)

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Categorías relacionadas

General description

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

Biochem/physiol Actions

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.

Packaging

Package size based on protein content

Physical form

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

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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Visite la Librería de documentos

Multi-virion infectious units arise from free viral particles in an enveloped virus
Cuevas JM, et al.
Nature microbiology, 2, 17078-17078 (2017)
PHOSPHATIDYLSERINE-POSITIVE ERYTHROCYTES BIND TO IMMOBILIZED AND SOLUBLE THROMBOSPONDIN-1 VIA ITS HEPARIN BINDING DOMAIN
Betal SG and Setty BNY
Translational Research, 152(4), 165?177-165?177 (2008)
A novel assay for apoptosis. Flow cytometric detection of phosphatidylserine expression on early apoptotic cells using fluorescein labelled Annexin V
Vermes I, et al.
Journal of Immunological Methods, 184(1), 39-51 (1995)
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.
Imaging biomarkers to predict response to anti-HER2 (ErbB2) therapy in preclinical models of breast cancer
Shah C, et el.
Clinical Cancer Research, 15(14), 4712?4721- 4712?4721 (2009)

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