Recombinant human HBEGF/DTR protein (Animal Free)
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(1 Publication)
Recombinant human HBEGF/DTR protein (Animal Free) is a Human Full Length protein, in the 63 to 148 aa range, expressed in Escherichia coli, with >97%, < 0.05 EU/µg endotoxin level, suitable for SDS-PAGE, FuncS.
View Alternative Names
DTR, DTS, HEGFL, HBEGF, Proheparin-binding EGF-like growth factor
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
HBEGF functions as a mitogen and chemotactic agent which means it stimulates cell division and attracts cells to migrate. As part of the EGF family HBEGF activates the EGFR (epidermal growth factor receptor) signaling cascade. This signaling is essential for processes such as wound healing and development. HBEGF also forms complexes with other ligands and receptors enhancing its biological activity in tissues.
Pathways
HBEGF plays a role in the MAPK/ERK signaling pathway and the PI3K/AKT pathway. Both pathways are significant for regulating cell growth survival and differentiation. HBEGF interacts with other proteins like Ras and PI3K in these pathways. By activating these pathways HBEGF influences cellular responses critical for normal physiological processes and recovery mechanisms in cells.
Specifications
Form
Lyophilized
General info
Function
Growth factor that mediates its effects via EGFR, ERBB2 and ERBB4. Required for normal cardiac valve formation and normal heart function. Promotes smooth muscle cell proliferation. May be involved in macrophage-mediated cellular proliferation. It is mitogenic for fibroblasts, but not endothelial cells. It is able to bind EGF receptor/EGFR with higher affinity than EGF itself and is a far more potent mitogen for smooth muscle cells than EGF. Also acts as a diphtheria toxin receptor.
Post-translational modifications
Several N-termini have been identified by direct sequencing. The forms with N-termini 63, 73 and 74 have been tested and found to be biologically active.. O-glycosylated with core 1 or possibly core 8 glycans. Thr-47 is a minor glycosylation site compared to Thr-44.
Target data
Publications (1)
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Cell research 30:779-793 PubMed32296111
2020
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
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