| Description | Background informationAnnexins are a family of calcium-dependent phospholipid-binding proteins that preferentially bind phosphatidylserine (PS). Under normal physiologic conditions, PS is predominantly located in the inner leaflet of the plasma membrane. Upon initiation of apoptosis, PS loses its Background informationAnnexins are a family of calcium-dependent phospholipid-binding proteins that preferentially bind phosphatidylserine (PS). Under normal physiologic conditions, PS is predominantly located in the inner leaflet of the plasma membrane. Upon initiation of apoptosis, PS loses its asymmetric distribution across the phospholipid bilayer and is translocated to the extracellular membrane leaflet marking cells as targets of phagocytosis. Once on the outer surface of the membrane, PS can be detected by fluorescently labeled Annexin V in a calcium-dependent manner.In early-stage apoptosis, the plasma membrane excludes viability dyes such as propidium iodide (PI), 7-AAD. These cells will stain with Annexin V but not a viability dye, thus distinguishing cells in early apoptosis. However, in late stage apoptosis, the cell membrane loses integrity thereby allowing Annexin V to also access PS in the interior of the cell. A viability dye can be used to resolve these late-stage apoptotic and necrotic cells (Annexin V, viability dye-positive) from the early-stage apoptotic cells (Annexin V positive, viability dye-negative).We offer recombinant Annexin V conjugated to a numerous fluorophores, as well as an Annexin V biotin conjugate which can be detected with fluorophore-labeled streptavidin. By binding to PS, fluorophores labeled Annexin V can be used to detect and quantify apoptotic cells via flow cytometry or fluorescence microscopy. The excitation and emission maxima of the Annexin V conjugates are summarized in the following table. The excitation and emission maxima of the Annexin V conjugates are summarized in the following table.Cat.No.Ex/Em (nm)Formatrp226056NABiotinrp225999401/422AF405rp226057490/525AF488rp226060650/668AF647rp226002681/704AF680rp226003752/776AF750rp226053498/517FITCrp226004410/455Pacific Bluerp226006647/665Cy5rp226054650/660APCrp226055565/575PErp226058565/670PE-Cy5rp226059565/774PE-Cy7Precautions1. Please try to avoid light when using to slow down the quenching of fluorescence.2. Propidium Iodide Solution is toxigenic and mutagenic; handle with care.3. Due to the calcium dependence of the Annexin V:PS interaction, it is critical to avoid buffers containing EDTA or other calcium chelators during Annexin V experiments.Instruction for use1. Dilute 10X Binding Buffer (A1372288) to 1X using distilled water (1 mL 10X Binding Buffer + 9 mL ddH2O).2. Wash cells twice with cold PBS and then resuspend the desired amounts of cells in Annexin V Binding Buffer at a concentration of 1.0-5.0 x 106 cells/mL.3. Add 5 µL of Annexin V-PE-Cy7 to 100 µL of the cell suspension. Stain with a viability dye, such as PI (P1373641; P1372285), 7-AAD (A1372406), or DAPI (D1372407) dyes, if desired.4. Gently vortex the cells and incubate for 10 min at RT (25°C) in the dark.5. Add 100 µL of 1X Binding Buffer to each assay. Analyze by flow cytometry within 1 hr... Read More | Inquire | Purity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：CNN1 is a member of the calponin family. CNN1 is a thin filament-associated protein which is involved in the regulation and modulation of smooth muscle contraction. CNN1 is able to bind to actin, calmodulinPurity: >90%, by SDS-PAGE visualized with Coomassie® Blue Staining.Description：CNN1 is a member of the calponin family. CNN1 is a thin filament-associated protein which is involved in the regulation and modulation of smooth muscle contraction. CNN1 is able to bind to actin, calmodulin, troponin C and tropomyosin. Prevention of actomyosin Mg-ATPase activity is a result of interaction between calponin and actin... Read More | Purity≥ 92% SDS-PAGEActual molecular weight 15&17kDaFunctionChemotactic factor that attracts monocytes and basophils but not neutrophils or eosinophils. Augments monocyte anti-tumor activity. Has been implicated in the pathogenesis of diseases characterized by monocytic infiltrates, like Purity≥ 92% SDS-PAGEActual molecular weight 15&17kDaFunctionChemotactic factor that attracts monocytes and basophils but not neutrophils or eosinophils. Augments monocyte anti-tumor activity. Has been implicated in the pathogenesis of diseases characterized by monocytic infiltrates, like psoriasis, rheumatoid arthritis or atherosclerosis. May be involved in the recruitment of monocytes into the arterial wall during the disease process of atherosclerosis... Read More | Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： Neuron specific enolase (NSE), also known as ENO2 or gamma-enolase, is a dimeric, Mg2+-dependent enzyme that catalyzes the dehydration of 2-phospho-D glycate (PGA) to phosphoenolpyruvate (PEP) in the Purity:>95%, by SDS-PAGE visualized with Coomassie® Blue Staining. Description： Neuron specific enolase (NSE), also known as ENO2 or gamma-enolase, is a dimeric, Mg2+-dependent enzyme that catalyzes the dehydration of 2-phospho-D glycate (PGA) to phosphoenolpyruvate (PEP) in the glycolytic pathway and catalyzes the reverse reaction in gluconeogenesis. There are three major isozymes of enolase expressed in selective vertebrate tissues from separate genes: alpha (ENO1), beta (ENO3), and gamma (ENO2). NSE is a highly expressed, specific neuron isozyme making it a useful marker for tumors derived from neuronal cells. Neuron-specific enolase is implicated as a diagnostic and prognostic marker in numerous diseases including early small cell lung cancer, prostate cancer, multiple myeloma, traumatic brain injury, acute spinal cord injury, acute ischemic stroke, and post-concussion symptoms. NSE expression and activity are increased in neuronal and glial activation and injury, risk factors implicated in neurodegenerative disease. Elevation of NSE promotes glycolysis, proliferation, activation and migration through its C-terminus to activate PI3K and MAPK signal transduction pathways while inhibition of enolase has been shown to attenuate inflammatory events. NSE can be regulated through cleavage of the C-termini by cathepsin X or inhibited directly by antibiotic SF2312. Inhibition has been proposed as a therapeutic strategy in cancer... Read More |