Streptavidin (Cy3) Reference: GTX85902 Streptavidin is a 52,8 dalton tetrameric protein purified from the bacterium Streptomyces avidinii. It has an extraordinarily high affinity for biotin and is one of the strongest non-covalent interactions known in nature. It is used extensively in biotechnology as, in addition to the high affinity, biotin-binding is resistant to extremes of pH, temperature, organic solvents, denaturants (e.g. guanidinium chloride), detergents (e.g. SDS, Triton) and proteolytic enzymes.Streptavidin conjugated to enzymes or fluorescent molecules is useful for the detection of biotinylated antibodies or proteins in immunological assays. For the detection of biotinylated molecules, streptavidin is superior to egg white avidin (avidin has a lower binding affinity for biotin conjugates, despite avidin having the higher affinity for free, unconjugated biotin).
Streptavidin (TxRd) Reference: GTX85907 Streptavidin is a 55 kDa (subunit MW 14 kDa) biotin-binding protein isolated from Streptomyces avidini. Streptavidin is superior to avidin, because it does not contain carbohydrate like avidin and has no net charge at neutral pH. Streptavidin~biotin system is routinely used in Immunohistochemistry (IHC). Extinction Coefficient 1% A28=32.; Purity: Streptavidin used is 99% pure by HPLC; Eletrophoretically homogenous, single band, Protein content: > 95%; Activity 14.8 units/ mg, one unit bunds 1. microgram of d-biotin; Protease activity: .18 units/mg; Isoelectric point: 7. +/- determined by Isoelectric focusing. Texas Red: A max. 596 nm; E max. 62 nm. Fluorochrome / protein Absorbance ratio: A596 nm/ A28 nm.
Streptavidin (APC) Reference: GTX85908 Streptavidin is a 55 kDa (subunit MW 14 kDa) biotin-binding protein isolated from Streptomyces avidini. Streptavidin is superior to avidin, because it does not contain carbohydrate like avidin and has no net charge at neutral pH. Streptavidin~biotin system is routinely used in Immunohistochemistry (IHC). Extinction Coefficient 1% A28=32.; Purity: Streptavidin used is 99% pure by HPLC; Eletrophoretically homogenous, single band, Protein content: > 95%; Activity 14.8 units/ mg, one unit bunds 1. microgram of d-biotin; Protease activity: .18 units/mg; Isoelectric point: 7. +/- determined by Isoelectric focusing. Allophycocyanin is a protein from the light-harvesting phycobiliprotein family, along with phycocyanin, phycoerythrin and phycoerythrocyanin. It is an accessory pigment to chlorophyll. Allophycocyanin absorbs and emits red light (65 & 66?nm max, respectively), and is readily found in Cyanobacteria (also called blue-green algae), and red algae. Phycobilin pigments have fluorescent properties that are used in immunoassay kits. Allophycocyanin can be isolated from various species of red or blue-green algae, each producing slightly different forms of the molecule. It is composed of two different subunits (α and β) in which each subunit has one phycocyanobilin (PCB) chromophore. The subunit structure for APC has been determined as (αβ)3. The molecular weight of APC is 15, Daltons. Absorption max: 652 nm, additional adsorption 625 nm, Emission max. 657.5 nm, Extinction Coefficient: 2.4 1 (mg/ml), A65/A28=4, A65/A62=1.25.
Streptavidin (AP) Reference: GTX85909 Streptavidin is a 55 kDa (subunit MW 14 kDa) biotin-binding protein isolated from Streptomyces avidini. Streptavidin is superior to avidin, because it does not contain carbohydrate like avidin and has no net charge at neutral pH. Streptavidin~biotin system is routinely used in Immunohistochemistry (IHC). Extinction Coefficient 1% A28=32.; Purity: > 99% pure by HPLC; Eletrophoretically homogenous, single band;Protein content: > 95%; Activity 14.8 units/ mg, one unit bunds 1. microgram of d-biotin; Protease activity: .18 units/mg; Isoelectric point: 7. +/- determined by Isoelectric focusing. Alkaline Phosphatase (ALP) used in this conjugation is 14 KDa enzyme purified from calf intestine.
Streptavidin (PE) Reference: GTX85910 Streptavidin is a 55 kDa (subunit MW 14 kDa) biotin-binding protein isolated from Streptomyces avidini. Streptavidin is superior to avidin, because it does not contain carbohydrate like avidin and has no net charge at neutral pH. Streptavidin~biotin system is routinely used in Immunohistochemistry (IHC). Extinction Coefficient 1% A28=32.. Purity: > 99% pure by HPLC; Eletrophoretically homogenous, single band. Protein content: > 95%; Activity 14.8 units/ mg, one unit bunds 1. microgram of d-biotin; Protease activity: .18 units/mg; Isoelectric point: 7. +/- determined by Isoelectric focusing. Phycoethyrin (R-PE) is a 24 kDa phycobilliprotein found in red, macrophytic algae (seaweed). R-PE can be used with Fluorescein (FITC) for double labeling in flow cytometry using argon laser, since both R-PE and FITC can be excited at 488 nm, and R-PE fluoresces at a longer wavelength (58 nm) than FITC (52 nm). Phycoethyrin: R-PE purified from Poryhyra tenera; A565/A28 >5.; A 1% 565 nm=82; Amax = 49, 545 and 566 nm; E max = 58 nm.
Streptavidin (FITC) Reference: GTX85911 Streptavidin is a 55 kDa (subunit MW 14 kDa) biotin-binding protein isolated from Streptomyces avidini. Streptavidin is superior to avidin, because it does not contain carbohydrate like avidin and has no net charge at neutral pH. Streptavidin~biotin system is routinely used in Immunohistochemistry (IHC). Extinction Coefficient 1% A28=32.. Purity: > 99% pure by HPLC; Eletrophoretically homogenous, single band. Protein content: > 95%; Activity 14.8 units/ mg, one unit bunds 1. microgram of d-biotin; Protease activity: .18 units/mg; Isoelectric point: 7. +/- determined by Isoelectric focusing. One mg of Streptavidin is conjugated with FITC, unconjugated Streptavidin is removed. This conjugate of streptavidin is recommended for use with Biotin~conjugated antibodies. Avidin~Biotin conjugated reagents are stable, sensitive and give less background. Fluorophore: Fluorescein isothiocyanate A max=492nm; E=52nm; Fluorophore/Protein: A492nm/A28nm=~1