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Cynomolgus ALK-2 / ACVR1 / ALK2 Protein (Cytokine) PDF Download

Catalog Size (Price) Quantity In Stock Operation Other Information
90058-C02H
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Protein Production & Purification Service

Activin A receptor, type I Protein Datasheet

 

ALK-2 / ACVR1 / ALK2 Protein Price Inquiry ( Available Sizes )

ALK-2 / ACVR1 / ALK2 Protein Product Information

Synonym : ACVR1
Protein Construction:

A DNA sequence encoding the cynomolgus ACVR1 (F7A9J8) (Met1-Glu123) was expressed with the Fc region of human IgG1 at the C-terminus.

Source: Cynomolgus
Expression Host: Human Cells

ALK-2 / ACVR1 / ALK2 Protein QC Testing

Purity: (75.3+22.3)% as determined by SDS-PAGE SDS-PAGE:
SDS-PAGE

ALK-2 / ACVR1 / ALK2 protein

Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
Stability: Samples are stable for up to twelve months from date of receipt at -70℃
Predicted N terminal: Asp 23
Molecular Mass:

The recombinant cynomolgus ACVR1 is a disulfide-linked homodimer. The reduced monomer comprises 342 amino acids and has a calculated molecular mass of 38.2 KDa.The apparent molecular mass of the protein is approximately 44 and 37 KDa respectively in SDS-PAGE.

Formulation: Lyophilized from sterile PBS, pH 7.4.
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.

ALK-2 / ACVR1 / ALK2 Protein Usage Guide

Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

ALK-2 / ACVR1 / ALK2 Protein Related Products & Topics

Related Areas:

Cancer>>Growth Factor & Receptor>>TGF-beta Superfamily>>Activin/Inhibitin>>ALK-2/ACVR1

Immunology>>Cytokine & Receptor>>TGF-beta Superfamily>>TGF-beta Superfamily Receptors>>ALK-2/ACVR1

Proteins:

Molecule Species Description //For Detailed Info. and Price------CLICK! Cat. No
ALK-2/ACVR1 Human ALK-2/ACVR1/Fc Protein, Recombinant 10227-H03H
ALK-2/ACVR1 Human ALK-2 / ACVR1 / ALK2 Protein, Recombinant 10227-H08B
ALK-2/ACVR1 Mouse ALK-2/ACVR1/Fc Protein, Recombinant 50297-M03H
ALK-2/ACVR1 Rat ALK-2 / ACVR1 / ALK2 Protein, Recombinant 80118-R02H
ALK-2/ACVR1 Cynomolgus ALK-2 / ACVR1 / ALK2 Protein, Recombinant 90058-C02H

Antibodies:

ALK-2 / ACVR1 / ALK2 Protein Description

Cytokines and hormones belonging to the transforming growth factor beta (TGFβ) superfamily such as the activin, anti-müllerian hormone (AMH), bone morphogenetic proteins (BMPs), and Nodal, are involved in a variety of physiological processes including growth, cell differentiation, homeostasis, osteogenesis, and apoptosis. They initiate signaling through heteromeric complexes of a type I  and a type I I serine/threonine kinase receptor. The two type receptors are type I transmembrane proteins and are distinguished by the presence of a glycine/serine-rich juxta-membrane domain found in the type I receptors. Type II receptors are required for binding ligands and recruitment of type I receptors which then form stable complexes, and type I receptors are essential for signaling transduction. ALK2, also termed as ACVR1, ActRI, SKR1, was initially identified as an activin type I receptor because of its ability to bind activin in concert with ActRII or IIB. In addition, ALK2 is also identified as a BMP type I receptor. ACVR1 has been demonstrated to form complex with either the BMP-2/7-bound BMPR-II or ACVR2A/ACVR2B and transduce signals to downstream components R-SMADs. Recombinant soluble ALK2 does not bind activin. Mutations in this gene are associated with fibrodysplasia ossificans progressive.

References

  1. Attisano L. et al., 1993, Cell. 75: 671-80.
  2. Ten Dijke P. et al., 1994, Science. 264: 101-4.
  3. Macias-Silva M. et al., 1998, J Biol Chem. 273: 25628-36.
  4. Shore EM. et al., 2006, Nature Genetics. 38: 525-7.
  5. Renlund N. et al., 2007, J Endocrinology. 195: 95-103.