Immunophilins are a family of soluble cytosolic receptors capable of binding to one of two major immunosuppressant agents - cyclosporin A (CsA) or FK506. Proteins that bind FK506 are termed FK506 Binding Proteins (FKBPs) and those that bind cyclosporin A are called cyclophilins (CyP).
Both CyP:CsA and FKBP:FK506 complexes have been shown to inhibit calcineurin, a calcium and calmodulin dependent protein phosphatase which has been implicated as an important signalling enzyme in T-cell activation, providing a possible mechanism of immunosuppression by CsA and FK506. Immunophilins function as peptidyl prolyl cis-trans-isomerases (PPIase) whose activity is inhibited by their respective immunosuppressant compounds. As PPIase's, immunophilins accelerate folding of some proteins both in vivo and in vitro by catalyzing slow steps in the initial folding and rearrangement of proline containing proteins.
Within the cyclophilin family, there are several different proteins which show a high degree of homology including CyPA, CyPB and CyPC. CyPA, also termed CyP-18, is the most abundant and ubiquitous cyclophilin found in all vertebrate tissues and is present in T-cells.

• For Western Blot

Recognizes overexpressed human cyclophilin A. Detects a prominent band of ~18kDa representing recombinant human cyclophilin A by Western blot. Does not detect endogenous levels of cyclophilin A. Also detects hamster cyclophilin A in CHO cells.

Type: Primary
Antigen: PPIA
Clonality: Polyclonal
Clone:
Conjugation:
Epitope:
Host: Rabbit
Isotype:
Reactivity: Human