Catalog #RP106
Recombinant human activin AB protein
Reactivities
Human
Applications
Drug discovery in metabolism
Wound healing and fibrosis
Wound healing and fibrosis
Product Description
Recombinant human activin AB protein is a disulfide-linked heterodimer of one inhibinβA and one inhibinβB chain and a secreted member of the transforming growth factor-beta (TGF-β) family, whose activin class spans activins A, B, C and E and extends to GDF-8 (myostatin) and GDF-11 (BMP-11). The inhibinβ chains are homologous, with 63% identity between A and B and 50% with C, and combine as homodimers or heterodimers to form functional ligands that regulate growth, differentiation and proliferation in a wide range of cell types. Activins signal through the type 1 activin receptor-like kinases ALK4 and ALK7 to activate the SMAD2/3 pathway, as distinct from the SMAD1/5/8 pathway engaged via ALK1, ALK2, ALK3 and ALK6. Activins A and B mediate activation or expression of JNK, iNOS and PARP1 and activation of hepatic stellate cells, driving liver fibrosis, activin overexpression improves insulin sensitivity and reduces fat via FGF-21 and PDE4B in diabetes models, and activin B promotes JNK/ERK-driven migration of adipose-derived stem cells in wound healing, making activin AB a valuable reagent for TGF-β signaling, fibrosis and metabolic research.
This protein is optimized for in vivo and functional applications: low-endotoxin, tag-free, and carrier-free, supporting reproducible performance in demanding preclinical and bioactivity studies.
Species reactivity: human.
This protein is optimized for in vivo and functional applications: low-endotoxin, tag-free, and carrier-free, supporting reproducible performance in demanding preclinical and bioactivity studies.
Species reactivity: human.
Specifications
| Reported Applications |
Drug discovery in metabolism Wound healing and fibrosis |
|---|---|
| Formulation | Lyophilized, white powder |
| Endotoxin |
≤0.5 EU/mg LAL assay |
| Purity |
≥95% Determined by SDS-PAGE |
| Sterility | Sterile |
| Production | Microbial. Expressed in E. coli |
| Molecular Weight | 25.7 kDa (dimer) |
| Storage | Store lyophilized protein between -20 °C and -80 °C until the date of expiry. Avoid freeze-thaw cycles |
| Mycoplasma | Negative |
| Bioactivity Assay | No significant difference between EC50 of reference and test lots |
| Reconstitution | Resuspend in 10 mM HCl (Reconstitution Buffer A) at >50 µg/ml. Once reconstituted, store in single-use aliquots to avoid freeze-thaw cycles. Store reconstituted protein at -20 °C to -80 °C for a maximum of 12 months or until the expiry date if sooner. |
| Shelf Life | This product has a guaranteed shelf-life of one year from the date of customer receipt when stored as recommended. |