Recombinant Human TGF-beta 1 Biotinylated Protein, CF Summary
Additional Information |
Human Cell-expressed, Biotinylated |
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant
Human TGF-beta RII Fc Chimera
(Catalog #
341-BR)
is immobilized at 0.1 µg/mL (100 µL/well), Biotinylated Recombinant Human TGF-beta 1 (Catalog # BT7754) binds with an ED 50 of 1.50-15.0 ng/mL. |
Source |
Human embryonic kidney cell, HEK293-derived human TGF-beta 1 protein Ala279-Ser390 |
Accession # |
|
N-terminal Sequence |
Ala279 |
Structure / Form |
Disulfide-linked homodimer Biotinylated via amines |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
12.8 kDa. 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 |
8-14 kDa, under reducing conditions. |
Packaging, Storage & Formulations
Storage |
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 Acetonitrile and TFA with Trehalose. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 250 μg/mL in 4mM HCl. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human TGF-beta 1 Biotinylated Protein, CF
Background
TGF‑ beta 1 (transforming growth factor
beta 1) is one of three closely related mammalian members of the large TGF‑
beta superfamily that share a characteristic cystine knot structure (1‑7). TGF‑beta
1, 2 and 3 are highly pleiotropic cytokines that are proposed to act
as cellular switches that regulate processes such as immune function,
proliferation and epithelial‑mesenchymal transition (1‑4). Each TGF‑ beta
isoform has some non‑redundant functions; for TGF‑beta 1, mice with targeted
deletion show defects in hematopoiesis and endothelial differentiation, and die
of overwhelming inflammation (2). Human TGF‑beta 1 cDNA encodes a
390 amino acid (aa) precursor that contains a 29 aa signal peptide
and a 361 aa proprotein (8). A furin-like convertase processes the proprotein
to generate an N‑terminal 249 aa latency‑associated peptide (LAP) and a C‑terminal
112 aa mature TGF‑beta 1 (8, 9). Disulfide-linked homodimers of LAP
and TGF‑beta 1 remain non‑covalently associated after secretion, forming the
small latent TGF‑beta 1 complex (8‑10). Covalent linkage of LAP to one of three
latent TGF‑beta binding proteins (LTBPs) creates a large latent complex that
may interact with the extracellular matrix (9, 10). TGF‑beta is activated
from latency by pathways that include actions of the protease plasmin, matrix
metalloproteases, thrombospondin 1 and a subset of integrins (10).
Mature human TGF‑beta 1 shares 100% aa identity with pig, dog and cow TGF‑beta
1, and 99% aa identity with mouse, rat and horse TGF‑beta 1. It
demonstrates cross‑species activity (1). TGF‑beta 1 signaling begins with high‑affinity
binding to a type II ser/thr kinase receptor termed TGF‑beta RII. This
receptor then phosphorylates and activates a second ser/thr kinase receptor,
TGF‑beta RI (also called activin receptor‑like kinase (ALK) ‑5), or
alternatively, ALK‑1. This complex phosphorylates and activates Smad proteins
that regulate transcription (3, 11, 12). Contributions of the
accessory receptors betaglycan (also known as TGF-beta RIII) and
endoglin, or use of Smad-independent signaling pathways, allow for disparate
actions observed in response to TGF‑beta in different contexts (11).
- Derynck, R. and K. Miyazono (2008) Cold Spring Harbor Laboratory Press p. 29.
- Dunker, N. and K. Krieglstein (2000) Eur. J. Biochem. 267:6982.
- Wahl, S.M. (2006) Immunol. Rev. 213:213.
- Chang, H. et al. (2002) Endocr. Rev. 23:787.
- Lin, J.S. et al. (2006) Reproduction 132:179.
- Hinck, A.P. et al. (1996) Biochemistry 35:8517.
- Mittl, P.R.E. et al. (1996) Protein Sci. 5:1261.
- Derynck, R. et al. (1985) Nature 316:701.
- Miyazono, K. et al. (1988) J. Biol. Chem. 263:6407.
- Oklu, R. and R. Hesketh (2000) Biochem. J. 352:601.
- de Caestecker, M. et al. (2004) Cytokine Growth Factor Rev. 15:1.
- Zuniga, J.E. et al. (2005) J. Mol. Biol. 354:1052.
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