TGF-beta 1 PLUS activity is determined using the firefly luciferase reporter assay (*) in transiently transfected HEK293T cells. Cells are treated in triplicate with a serial dilution of TGF-beta 1. Firefly luciferase ...read more
TGF-beta 1 PLUS (Qk010) dimer migrates as a single band at 24 kDa in non-reducing (NR) and 13 kDa as a single monomeric species upon reduction (R). High purity yield of dimeric protein (bioactive form).Purified ...read more
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
24 kDa (dimer). 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
Dimeric TGF- beta 1 PLUS protein only
Publications
Read Publication using Qk010 in the following applications:
Store lyophilized protein between -20 and -80 °C until the date of expiry. Avoid freeze-thaw cycles.
Buffer
Lyophilized from acetonitrile/TFA
Reconstitution Instructions
Resuspend in 10mM HCl at >100 µg/ml, prepare single use aliquots, add carrier protein if desired.
Notes
The above product was manufactured, tested and released by R&D System's contract manufacturer, Qkine Ltd, at 1 Murdoch House, Cambridge, UK, CB5 8HW. The product is for research use only and not for the diagnostic or theraputic use.
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human TGF-beta 1 PLUS, Animal-Free Protein
CEDLAP
DPD1
latency-associated peptide
TGF beta
TGF beta1
TGFB
TGFB1
TGF-beta 1 protein
TGFbeta 1
TGF-beta 1
TGFbeta
TGF-beta-1
transforming growth factor beta-1
transforming growth factor, beta 1
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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