Animal Free,Carrier Free,Bioactive,ActiBioPure™,Azide Free,High Performance,His-Tag,≥95%(SDS-PAGE) ActiBioPure™,Animal Free,Azide Free,Bioactive,Carrier Free,High Performance,His Tag for sensitive chromatographic and analytical workflows requiring minimal baseline interference.
Store at -20°C,Avoid repeated freezing and thawing Ships Ice chest + Ice pads Check lot-specific COA for exact specifications.
SDS, COA, datasheet, and spec sheet available for download. Lot-specific COA accessible via lot number lookup.
Cited in 0 peer-reviewed publications across chromatography, organic synthesis, and cross-coupling reactions.
Purity
≥95% (SDS-PAGE)
Endotoxin level
＜0.1 EU/μg
Function
Activin and Inhibin are members of the TGF-beta superfamily of cytokines and are involved in a wide range of biological processes including tissue morphogenesis and repair, fibrosis, inflammation, neural development, hematopoiesis, reproductive system function, and carcinogenesis. Activin and Inhibin are produced as precursor proteins. Their amino terminal propeptides are proteolytically cleaved and facilitate formation of disulfide-linked dimers of the bioactive proteins. Activins are nonglycosylated homodimers or heterodimers of various beta subunits ( beta A, beta B, beta C, and beta E in mammals), while Inhibins are heterodimers of a unique alpha subunit and one of the beta subunits. Activin A is a widely expressed homodimer of two beta A chains. The beta A subunit can also heterodimerize with a beta B or beta C subunit to form Activin AB and Activin AC, respectively. The 14 kDa mature human beta A chain shares 100% amino acid sequence identity with bovine, feline, mouse, porcine, and rat beta A. Activin A exerts its biological activities by binding to the type 2 serine/threonine kinase Activin RIIA which then noncovalently associates with the type 1 serine/threonine kinase Activin RIB/ALK-4. Signaling through this receptor complex leads to Smad activation and regulation of activin-responsive gene transcription. The bioactivity of Activin A is regulated by a variety of mechanisms. BAMBI, Betaglycan, and Cripto are cell‑associated molecules that function as decoy receptors or limit the ability of Activin A to induce receptor complex assembly. The intracellular formation of Activin A can be prevented by the incorporation of the beta A subunit into Activin AC or Inhibin A. And the bioavailability of Activin A is restricted by its incorporation into inactive complexes with alpha 2-Macroglobulin, Follistatin, and FLRG. Activin A is involved in the differentiation of various cell and tissue types. The induction of definitive endoderm by Activin A is required in differentiation protocols of induced pluripotent stem cells (iPSCs). In vitro models of human gametogenesis use prolonged Activin A supplementation to human embryonic stem cells for differentiation into human primordial germ cell-like cells. Activin A can also be used to maintain cells in vitro, as is the case for iPSC-derived nephron cells that can then be used in disease modeling, drug screening and in regenerative medicine. Activin A is an important factor for tumor cells to evade the immune system as Activin A can act on surrounding immune cells to decrease their antitumor activity. Activin A also promotes migration and growth of tumors, making it a target for cancer therapies. Specifically, research has shown that interfering with Activin A activity can assist in overcoming CD8 T-cell exclusion and immunotherapy resistance. In bone marrow-derived stem cell transplants for treatment of diabetes, Activin A enhances migration and homing of stem cells towards pancreatic lineage.
Recombinant Human Activin A Protein (rp142493) - Protein Bioactivity
Measured by its ability to induce hemoglobin expression in K562 human chronic myelogenous leukemia cells. The ED50 for this effect is 2.87 ng/mL.
Recombinant Human Activin A Protein (rp142493) - SDS-PAGE
3 μg/lane of Recombinant Human Activin A Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing the band at 13 - 16 kDa (mature) and 39 - 46 kDa (precursor) under reducing condition. Under non-reducing conditions, the migration rate of the mature protein is 27 kDa, and the migration rate of the precursor protein is 39 - 46 kDa, and there may also be a migration rate of 55 - 65 kDa (indicating the combination of the precursor and mature forms). These changes in migration rate are mainly due to the effects of glycosylation and interchain disulfide bonds.
Comprehensive hazard, handling, storage, and regulatory compliance document.
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| Lot Number | Certificate Type | Fecha | Articulo |
|---|---|---|---|
 ZJ24F1113619 | Certificate of Analysis | Jun 15, 2026 | rp142493 |
| ZJ24F1113620 | Certificate of Analysis | Jun 15, 2026 | rp142493 |
| ZJ24F1113621 | Certificate of Analysis | Jun 15, 2026 | rp142493 |
Our grade selection guide covers purity, stabilizer status, and application suitability for all variants in our catalog.
View Animal Free grade guide → View Carrier Free grade guide → View Bioactive grade guide → View ActiBioPure™ grade guide → View Azide Free grade guide → View High Performance grade guide → View His Tag grade guide →
