Recombinant Mouse TGF-beta RI/ALK-5 Fc Chimera Protein, CF Summary
Additional Information
This item is in process of being discontinued.
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Rat Endoglin/CD105 Fc Chimera (Catalog # 6440-EN) or Recombinant Mouse Endoglin/CD105 Fc Chimera (Catalog # 1320-EN) is immobilized at 2 μg/mL (100 μL/well), the concentration of Recombinant Mouse TGF-beta RI/ALK-5 Fc Chimera that produces 50% of the optimal binding response is found to be approximately 0.25-1.25 μg/mL.
Source
Spodoptera frugiperda, Sf 21 (baculovirus)-derived mouse TGF-beta RI/ALK-5 protein
Mouse TGF-beta RI (Ala21-Glu121) & (Thr22-Glu121) Accession # BAA05023
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.1 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
37.5 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
40-50 kDa, reducing conditions
Publications
Read Publications using 587-RI in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain
Reconstitution Instructions
Reconstitute at 500 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse TGF-beta RI/ALK-5 Fc Chimera Protein, CF
AAT5
activin A receptor type II-like kinase, 53kD
activin A receptor type II-like kinase, 53kDa
Activin receptor-like kinase 5
ACVRLK4
ALK-5
ALK-5ALK5
EC 2.7.11
EC 2.7.11.30
LDS1A
LDS2A
Serine/threonine-protein kinase receptor R4
SKR4
tbetaR-I
TGFB1R1
TGF-beta receptor type I
TGF-beta receptor type-1
TGF-beta RI
TGF-beta type I receptor
TGFbetaRI
TGFBR1
TGF-bRI
TGFR-1
transforming growth factor beta receptor I
transforming growth factor, beta receptor 1
transforming growth factor, beta receptor I (activin A receptor type II-likekinase, 53kD)
Transforming growth factor-beta receptor type I
Background
TGF-beta RI, also called ALK-5, is an approximately 55 kDa type I transmembrane serine/threonine receptor kinase (1, 2). It contains a cysteine-rich extracellular domain (ECD), a transmembrane helix, and a C-terminal cytoplasmic kinase domain (3). Within the cytoplasmic domain there is also a short, conserved regulatory sequence known as the GS region that is N-terminal to the kinase domain (1). Within the ECD, mouse TGF-beta RI shares 98% and 90% amino acid sequence identity with rat and human TGF-beta RI, respectively. In the presence of TGF-beta , TGF-beta RI forms a complex with, and is phosphorylated by, TGF-beta RII (1). Phosphorylated TGF-beta RI can then transiently bind and phosphorylate Smad2 and Smad3 (2, 4-6). These phosphorylated Smads form heteromeric complexes with Smad4, translocate to the nucleus, and regulate target gene transcription (2, 4-6). TGF-beta RI is likely important during development, since mice deficient for TGF-beta RI die at midgestation with severe defects in vascular development of the yolk sac and placenta, and an absence of circulating red blood cells (7). Furthermore, TGF-beta RI appears to be involved in proper lymphatic network development (8). Mutations in TGF-beta RI have been identified in pancreatic, colorectal, ovarian, and head and neck cancers (9).
Wrana, J.L. et al. (1994) Nature 370:341.
Massagué, J. (2012) Nat. Rev. Mol. Cell Biol. 13:616.
Huse, M. et al. (1999) Cell 96:425.
Marcías-Silva, M. et al. (1996) Cell 87:1215.
Zhang, Y. et al. (1996) Nature 383:168.
Huse, M. et al. (2001) Mol. Cell 8:671.
Larsson, J. et al. (2001) EMBO J. 20:1663.
James, J.M. et al. (2013) Development 140:3903.
Sheen, Y.Y. et al. (2013) Biomol. Ther. (Seoul) 21:323.
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