A9460
Annexin V from human placenta
≥90% (SDS-PAGE), buffered aqueous solution
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Synonym(s):
Annexin V, Calphosbindin I, Lipocortin V, PAP-1
UNSPSC Code:
41106305
NACRES:
NA.32
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Quality Level
Assay
≥90% (SDS-PAGE)
form
buffered aqueous solution
mol wt
33 kDa (four subunits)
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... ANXA5(308)
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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.
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.
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Regulatory Information
常规特殊物品
Certificates of Analysis (COA)
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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
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.
Barbara Schmidinger et al.
PLoS pathogens, 18(2), e1010326-e1010326 (2022-02-18)
Helicobacter pylori colonizes half of the global population and causes gastritis, peptic ulcer disease or gastric cancer. In this study, we were interested in human annexin (ANX), which comprises a protein family with diverse and partly unknown physiological functions, but
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)
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