epitope corresponding to amino acids 1-300 mapping at the N-terminus of IgA1 of human origin
Modification Notes
Immunoglobulins are four-chain, Y-shaped, monomeric structures comprised of two identical heavy chains and two identical light chains held together through interchain disulfide bonds. The chains form two domains, the Fab (antigen binding) fragment and the Fc (constant) fragment. Immunoglobulin A (IgA) is the main protein of the mucosal immune system. It is generated by B cells in gut-associated lymphoid tissues. Daily production of IgA exceeds that of any of the other immunoglobulins. The IgA heavy chain is an å-chain, and the light chains are either ˚- or ¬- chains. IgA exists mainly in dimers but can also exist as polymers or as monomers. Dimers and polymers contain a joining (J) chain that can be bound by the polymeric immunoglobulin receptor (pIgR) for transportation of the molecule to mucosal surfaces.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of IgA1 and IgA2 of human origin by WB, IP, IF and ELISA: WB:1:100~1:200 IF:1:20~1:100 IP:1:20~1:100
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to amino acids 1-300 mapping at the N-terminus of IgA1 of human origin
Tissue Specificity
epitope corresponding to amino acids 1-300 mapping at the N-terminus of IgA1 of human origin