| Species : |
Human/Cynomolgus |
| Source : |
HEK293 |
| Tag : |
Fc |
| Protein Length : |
20-135 aa |
| Description : |
Activin receptor type-2A (ACVR2A) is also known as Activin receptor type IIA, ACTR-IIA, ACTRIIA and ACVR2, which is single-pass type I membrane protein. ACVR2A belongs to the protein kinase superfamily, TKL Ser/Thr protein kinase family and TGFB receptor subfamily.On ligand binding, ACVR2A can forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators.ACVR2A is Receptor for activin A, activin B and inhibin A as well. Several type I I activin receptors have been identified and bind to different activins with different affinities. |
| Form : |
Lyophilized from 0.22 μm filtered solution in 50 mM Tris, 100 mM Glycine, 25 mM Arginine, 150 mM NaCl, pH7.5 with trehalose as protectant. |
| Bio-activity : |
Immobilized Human Activin A Protein, Tag Free at 5 μg/mL (100 μL/well) can bind Human/Cynomolgus Activin RIIA/ACVR2A Protein, Fc Tag with a linear range of 0.2-8 ng/mL. |
| Molecular Mass : |
The protein has a calculated MW of 39.9 kDa. The protein migrates as 50-60 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation. |
| Endotoxin : |
Less than 1.0 EU/μg by the LAL method/rFC method. |
| Purity : |
>90% as determined by SDS-PAGE. |
| Storage : |
This product is stable after storage at: -20 to -70 centigrade for 12 months in lyophilized state; -70 centigrade for 3 months under sterile conditions after reconstitution. For long term storage, the product should be stored at lyophilized state at -20 centigrade or lower. Please avoid repeated freeze-thaw cycles. |
| Reconstitution : |
It is recommended that sterile water be added to the vial to prepare a stock solution of 0.2 μg/μL. Centrifuge the vial at 4 centigrade before opening to recover the entire contents. |
