A9460
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
Código UNSPSC:
41106305
NACRES:
NA.32
Productos recomendados
origen biológico
human placenta
Nivel de calidad
Análisis
≥90% (SDS-PAGE)
formulario
buffered aqueous solution
mol peso
33 kDa (four subunits)
técnicas
cell based assay: suitable
impurezas
Human Source(HCV), tested negative
solubilidad
water: soluble
idoneidad
suitable for molecular biology
Nº de acceso UniProt
Condiciones de envío
dry ice
temp. de almacenamiento
−70°C
Información sobre el gen
human ... ANXA5(308)
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Descripción general
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.
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.
Aplicación
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
Acciones bioquímicas o fisiológicas
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.
Envase
Package size based on protein content
Forma física
Solution in 40 mM Tris-HCl, pH 7.5, containing 150 mM NaCl, 1 mM DTT and 0.05% sodium azide.
Código de clase de almacenamiento
12 - Non Combustible Liquids
Clase de riesgo para el agua (WGK)
WGK 2
Punto de inflamabilidad (°F)
Not applicable
Punto de inflamabilidad (°C)
Not applicable
Certificados de análisis (COA)
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Los clientes también vieron
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
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