Ziege IgG anti-Alpaka IgG (VHH)-RPE, MinX Bo

Whole IgG antibodies are isolated as intact molecules from antisera by immunoaffinity chromatography. They have an Fc portion and two antigen binding Fab portions joined together by disulfide bonds and therefore they are divalent. The average molecular weight is reported to be about 160 kDa. The whole IgG form of antibodies is suitable for the majority of immunodetection procedures and is the most cost effective.Based on immunoelectrophoresis, Western blot and/or ELISA, the antibody reacts with the VHH domain of heavy chain (HC) alpaca IgG, subclasses 2 and 3, and with the VHH domain of llama IgG, subclasses 2 and 3. It also reacts with whole molecule alpaca and llama IgG1. No antibody was detected against non-immunoglobulin serum proteins. The antibody has been tested by ELISA and/or solid-phase adsorbed to ensure minimal cross-reaction with bovine serum proteins, but it may cross-react with immunoglobulins from other species.

These antibodies react primarily with the Fc region, and are not recommended for detection of VHH antibodies.

Conjugate

Phycoerythrin (R-PE) is among several kinds of light-harvesting phycobiliproteins found in red, blue-green, and cryptomonad algae. We offer R-PE, the form found in red macrophytic algae (seaweed). After phycobiliproteins are conjugated to secondary antibodies, there is little fluorescence quenching, which results in conjugates of high specific fluorescence compared with conventional fluorophore-antibody conjugates. R-PE can be excited by light over a wide range of the visible spectrum is highly water soluble, has a relatively low isoelectric point, and lacks potentially sticky carbohydrates.

It should be noted that the relatively high molecular weight of R-PE may preclude its use in procedures requiring good penetration into cells and tissues. It is predominantly intended for surface labeling of cells for flow cytometry.