Purity: >95% by SDS-Page
Endotoxin Concentration: <1 EU/mL
Protein Length: 116 aa
Biological Activity: ED50 ≤5 ng/mL
Molecular Weight: 25 kDa
Reconstitution: We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute lyophilized recombinant human Activin A in sterile PBS containing 0.1% human serum albumin. Further dilutions should be made in low endotoxin medium or a buffered solution containing a carrier protein such as heat inactivated FCS or tissue culture grade BSA.
Storage: Store this lyophilized preparation at ≤ -20°C, preferably desiccated. Upon reconstitution, apportion into working aliquots and store at ≤ -20°C. Avoid repeated freeze/thaw cycles.
Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I ( I and IB) and two type II (II and IIB) receptors. These receptors are all transmembrane proteins, composed of a ligand-binding extracellular domain with cysteine-rich region, a transmembrane domain, and a cytoplasmic domain with predicted serine/threonine specificity. Type I receptors are essential for signaling; and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a stable complex after ligand binding, resulting in phosphorylation of type I receptors by type II receptors. Activin A mutations are associated with fibrodysplasia ossificans progressive.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: Activin beta-A chain; EDF; erythroid differentiation factor; Erythroid differentiation protein; follicle-stimulating hormone-releasing protein; FSH-releasing protein; Inhibin beta A chain; inhibin, beta A (activin A, activin AB alpha polypeptide); Inhibin, beta-1
Gene Aliases: EDF; FRP; INHBA