Recombinant Human Activin A Protein, ≥95% (SDS-PAGE), high purity

Features and benefits
  • Expression System: HEK293
  • Accession #: P08476(Human), Q04998 (Mouse), P18331(Rat)
  • Protein Tag: C-His
  • 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.
  • Endotoxin Concentration: <0.1 EU/μg
Item Number
rp142493
Grouped product items
SKUSizeAvailabilityPrice Qty
rp142493-10μg
10μg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$139.90
rp142493-50μg
50μg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$619.90
rp142493-100μg
100μg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$709.90
rp142493-1mg
1mg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$2,599.90

Animal Free, ≥95% (SDS-PAGE), Active, 293F, C-His tag, 21-426 aa

Basic Description

Product NameRecombinant Human Activin A Protein, ≥95% (SDS-PAGE), high purity
SynonymsActivin A | activin AB alpha polypeptide | Activin beta-A chain | erythroid differentiation factor | Erythroid differentiation protein | follicle-stimulating hormone-releasing protein | FSH-releasing protein | inhibin beta A chain | inhibin beta A subunit | Inhibin, beta-1
GradeActiBioPure™, Animal Free, Azide Free, Bioactive, Carrier Free, High Performance
Product Description

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.

Specifications & PurityActiBioPure™, Bioactive, Animal Free, Carrier Free, Azide Free, High performance, ≥95%(SDS-PAGE)
Purity≥95% (SDS-PAGE)
BioactivityMeasured by its ability to induce hemoglobin expression in K562 human chronic myelogenous leukemia cells. The ED50 for this effect is 2.87 ng/mL.
Endotoxin Concentration<0.1 EU/μg
Expression SystemHEK293
SpeciesHuman/ Mouse/ Rat
Amino Acids21-426 aa
SequenceSPTPGSEGHSAAPDCPSCALAALPKDVPNSQPEMVEAVKKHILNMLHLKKRPDVTQPVPKAALLNAIRKLHVGKVGENGYVEIEDDIGRRAEMNELMEQTSEIITFAESGTARKTLHFEISKEGSDLSVVERAEVWLFLKVPKANRTRTKVTIRLFQQQKHPQGSLDTGEEAEEVGLKGERSELLLSEKVVDARKSTWHVFPVSSSIQRLLDQGKSSLDVRIACEQCQESGASLVLLGKKKKKEEEGEGKKKGGGEGGAGADEEKEQSHRPFLMLQARQSEDHPHRRRRRGLECDGKVNICCKKQFFVSFKDIGWNDWIIAPSGYHANYCEGECPSHIAGTSGSSLSFHSTVINHYRMRGHSPFANLKSCCVPTKLRPMSMLYYDDGQNIIKKDIQNMIVEECGCSHHHHHH
Protein TagC-His
ConjugationUnconjugated
Accession #P08476(Human), Q04998 (Mouse), P18331(Rat)
Predicted molecular weight45 kDa
SDS-PAGE13 - 16 kDa (mature) and 39 - 46 kDa (precursor) , under reducing conditions.

Images

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.

Product Specifications

FormLyophilized
ReconstitutionReconstitute in sterile water to a concentration of 0.1-0.5 mg/ml.
Storage TempStore at -20°C,Avoid repeated freezing and thawing
Shipped InIce chest + Ice pads
Stability And StorageStore at -20~-80℃ for more than 1 year. Upon delivery aliquot. Avoid freeze/thaw cycle.

Certificates

Certificate of Analysis(COA)

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Related Documents

References

1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P et al..  (2004)  The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)..  Genome Res,  14  (10B): (2121-7).  [PMID:15489334] [10.1021/op500134e]
2. Wentworth KL, Masharani U, Hsiao EC.  (2019)  Therapeutic advances for blocking heterotopic ossification in fibrodysplasia ossificans progressiva..  Br J Clin Pharmacol,  85  (6): (1180-1187).  [PMID:30501012] [10.1021/op500134e]
3. Zhu J, Mishra RK, Schiltz GE, Makanji Y, Scheidt KA, Mazar AP, Woodruff TK..  (2015)  Virtual High-Throughput Screening To Identify Novel Activin Antagonists..  J Med Chem,  58  (14): (5637-5648).  [PMID:26098096] [10.1021/acs.jmedchem.5b00753]
4. Tanimoto, K K, Handa, S S, Ueno, N N, Murakami, K K and Fukamizu, A A..  (1991)  Structure and sequence analysis of the human activin beta A subunit gene..  DNA sequence : the journal of DNA sequencing and mapping,      [PMID:1777673]
5. Murata, M M, Eto, Y Y, Shibai, H H, Sakai, M M and Muramatsu, M M..  (1988)  Erythroid differentiation factor is encoded by the same mRNA as that of the inhibin beta A chain..  Proceedings of the National Academy of Sciences of the United States of America,      [PMID:3267209]
6. Mason, A J AJ, Niall, H D HD and Seeburg, P H PH..  (1986)  Structure of two human ovarian inhibins..  Biochemical and biophysical research communications,    (28):   [PMID:3754442]
7. Stewart, A G AG, Milborrow, H M HM, Ring, J M JM, Crowther, C E CE and Forage, R G RG..  (1986)  Human inhibin genes. Genomic characterisation and sequencing..  FEBS letters,    (6):   [PMID:3758355]
8. Thompson, Thomas B TB, Woodruff, Teresa K TK and Jardetzky, Theodore S TS..  (2003)  Structures of an ActRIIB:activin A complex reveal a novel binding mode for TGF-beta ligand:receptor interactions..  The EMBO journal,    (1):   [PMID:12660162]
9. Schneyer, Alan A, Schoen, Amy A, Quigg, Alicia A and Sidis, Yisrael Y..  (2003)  Differential binding and neutralization of activins A and B by follistatin and follistatin like-3 (FSTL-3/FSRP/FLRG)..  Endocrinology,      [PMID:12697670]
10. Hillier, Ladeana W LW and 106 more authors..  (2003)  The DNA sequence of human chromosome 7..  Nature,    (10):   [PMID:12853948]
11. Stamler, Robin R and 5 more authors..  (2008)  The structure of FSTL3.activin A complex. Differential binding of N-terminal domains influences follistatin-type antagonist specificity..  The Journal of biological chemistry,    (21):   [PMID:18768470]
12. Tournier, Isabelle I and 20 more authors..  (2014)  Germline mutations of inhibins in early-onset ovarian epithelial tumors..  Human mutation,      [PMID:24302632]
13. Hatsell, Sarah J SJ and 20 more authors..  (2015)  ACVR1R206H receptor mutation causes fibrodysplasia ossificans progressiva by imparting responsiveness to activin A..  Science translational medicine,    (2):   [PMID:26333933]
14. Aykul, Senem and 19 more authors..  (2020)  Activin A forms a non-signaling complex with ACVR1 and type II Activin/BMP receptors via its finger 2 tip loop..  eLife,    (9):   [PMID:32515349]

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