TGF α (1-50) (rat)
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TGF α (1-50) (rat)

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TGF α (1-50) (rat) was originally identified as an agent that can reversibly confer a transformed phenotype on normal non-tumor cells, such as normal rat renal fibroblasts. This activity requires the presence of transforming growth factor-β (TGF-β), which enhances the effects of TGF-α through a separate receptor. TGF-α is synthesized by monocytes, keratinocytes and a variety of tissues and tumors. (approx. ED50 = 0.2 ng/mL)

Category
Peptide Inhibitors
Catalog number
BAT-015210
CAS number
89899-53-6
Molecular Formula
C244H361N71O71S6
Molecular Weight
5617.38
Synonyms
H-Val-Val-Ser-His-Phe-Asn-Lys-Cys-Pro-Asp-Ser-His-Thr-Gln-Tyr-Cys-Phe-His-Gly-Thr-Cys-Arg-Phe-Leu-Val-Gln-Glu-Glu-Lys-Pro-Ala-Cys-Val-Cys-His-Ser-Gly-Tyr-Val-Gly-Val-Arg-Cys-Glu-His-Ala-Asp-Leu-Leu-Ala-OH (Disulfide bridge: Cys8-Cys21, Cys16-Cys32, Cys34-Cys43); Transforming Growth Factor-α (1-50) from rat
Appearance
White or Off-white Lyophilized Powder
Sequence
VVSHFNKCPDSHTQYCFHGTCRFLVQEEKPACVCHSGYVGVRCEHADLLA (Disulfide bridge: Cys8-Cys21, Cys16-Cys32, Cys34-Cys43)
Storage
Store at -20°C
Solubility
Soluble in Water
1. Human transforming growth factor alpha (TGF-alpha) is digested to a smaller (1-43), less biologically active, form in acidic gastric juice
T Marchbank, H Hansen, R Boulton, R J Playford Gut . 2002 Dec;51(6):787-92. doi: 10.1136/gut.51.6.787.
Background:Transforming growth factor alpha (TGF-alpha) is a 50 amino acid peptide with potent proliferative and cytoprotective activity present in gastric mucosa and juice.Aims:To determine the forms and biological activity of natural and recombinant TGF-alpha following incubation with acid pepsin.Patients:Human gastric juice was obtained under basal conditions from patients taking acid suppressants and from volunteers undergoing intragastric neutralisation.Methods:Samples were analysed using mass spectroscopy and/or high pressure liquid chromatography with radioimmunoassay. Biological activity was determined using thymidine incorporation into rat hepatocytes and an indomethacin/restraint induced gastric damage rat model.Results:TGF-alpha(1-50) is cleaved to TGF-alpha(1-43) by acid pepsin and this is the predominant form in normal gastric juice. However, intragastric neutralisation or taking acid suppressants caused the predominant form to be TGF-alpha(1-50). TGF-alpha(1-43) had only half of the ability to maximally stimulate [(3)H]thymidine incorporation into primary rat hepatocytes (28 177 (1130) DPM/well for 2.16 nM TGF-alpha(1-43) v 63 184 (3536) DPM/well for TGF-alpha(1-50); p<0.001). A similar reduced potency was seen when used in an indomethacin induced rat gastric damage model (0.18 micro mol/kg/h of TGF-alpha(1-43) reduced ulcer area by 19% whereas TGF-alpha(1-50) reduced area by 62%; p<0.001).Conclusions:TGF-alpha(1-50) is cleaved to the TGF-alpha(1-43) form by acid pepsin, causing 2-5-fold loss of biological activity. Such changes may have relevance to the actions of acid suppressants and the importance of this peptide in both normal and abnormal growth.
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