VSA34, SAA19, SAA21, SAA11, VSA31, VSA38, VSA2, VSA43Hybridoma clones have been derived from hybridization of Sp2/0 myeloma cells with spleen cells of Balb/c mice immunized with either human SAA (SAA19, SAA21, SAA11), or canine SAA (VSA34, VSA31, VSA38), or synthetic peptides derived from the region 79-104 a.a.r. of canine SAA (VSA2, VSA43).

Canine SAA (all MAbs)Feline SAA (VSA34, SAA19, VSA31, VSA38, SAA21, SAA11)Equine SAA (all MAbs)

IgG1 for MAb VSA2IgG2a for MAbs SAA19, VSA31, VSA38IgG2b for MAbs VSA34, SAA21, VSA43, SAA11

Recommended pairs for sandwich immunoassay (capture – detection):SAA19 – VSA34: canine, feline, equineSAA21 – VSA34: canine, feline, equineVSA2 – VSA38: canine, equineVSA2 – VSA31: canine, equineVSA38 – VSA43: canine, equineAll MAbs react with SAA in Western blotting.

Chromatography on protein G Sepharose

PBS, pH 7.4, 0.1 % sodium azide (NaN3)

+ 4 °C

We recommend to avoid using bovine serum albumin (BSA) as a buffer component or blocking agent for SAA immunoassay. In buffers, BSA can be replaced with 1% casein.Immunoassay plates blocking with casein is needed to prevent non-specific binding of SAA to the wells of an immunoassay plate.For pairs SAA19 – VSA34 and SAA21 – VSA34, we recommend to start assay optimization using 0.01% CHAPS in antigen dilution and washing buffers. According to our data, Tween 20 lowered the signal in the wells when it was used in concentration 0.05-0.1% in antigen dilution buffer. When lower concentration of Tween 20 was used (0.005-0.025%), non-specific binding of SAA to the wells of an immunoassay plate was observed.For pairs VSA2 – VSA38, VSA2 – VSA31 and VSA38 – VSA43, we recommend to use antigen dilution buffer containing 1% casein and 0.05-0.1% Tween 20.

This product is sold as an antibody preparation for research use only. Standard Laboratory Practices should be followed when handling this material.Contains sodium azide (0.1 %) as preservative. Although the amount of sodium azide is very small appropriate care must be taken when handling this product.