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HBEGF

Products

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All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

Background

HBEGF is a 208-amino acid single-pass type I transmembrane glycoprotein of the epidermal growth factor (EGF) family whose full length precursor weighs approximately 23.4 kDa and with the soluble mature form. HBEGF is synthesized as a membrane-bound precursor (proHB-EGF) that undergoes proteolytic processing at the juxtamembrane domain mainly by metalloproteinases: ADAM17 and matrixmetalloproteinases (MMPs), which release the soluble mature form of HBEGF (sHB-EGF). Ectodomain shedding is tightly controlled via a cascade of signaling pathways including PKC, calcium influx and GPCR activation. ProHB-EGF possesses the longest residence time at cell-cell contacts when compared to other EGFR ligands, enabling it to serve dual roles as a precursor of soluble growth factor and a biologically active juxtacrine signaling molecule capable of non-diffusible activation of adjacent cells. Abstract ProHB-EGF tetraspanin CD9 integrin α3β1 heparan sulfate proteoglycans (HSPGs) cell–cell contact sites signaling microdomains What is especially unique about the transmembrane form of HBEGF is it being a receptor for diphtheria toxin (DTx) enabling DTx to enter human and monkey cells, an entry property used to create conditional cell ablation models. Certainly, HBEGF is above all in their (mainly) human tissues such as gall bladder, esophagus, lung, heart, kidneys and macrophages, emphasizing its central roles in epithelial.

Fig.1 Regulation of HBEGF by downstream signaling. (OA Literature)Fig.1 Regulation of HBEGF by downstream signaling in human TB cells.1

HBEGF Protein Function: A Dual-Mode Regulator of Cell Proliferation and Tissue Remodeling

The functional versatility of HBEGF can be attributed to its ability to signal by both membrane-anchored and soluble forms:

  • Juxtacrine Signaling and Cell-Cell Communication: As a non-diffusible signaling molecule, the membrane-bound proHB-EGF will stimulate EGFR on adjacent cells via direct cell-cell contact. Such juxtacrine mode is mediated through complexes with CD9, integrin α3β1, and HSPGs at cell-cell contact sites.
  • Paracrine Mitogenesis and Chemotaxis: sHBEGF is a potent mitogenic and chemoattractant factor for vascular smooth muscle cells, fibroblasts, and keratinocytes. Another molecule, which has a stronger affinity to EGFR (ErbB1) and ErbB4 than EGF, activates ErbB2 and ErbB3 indirectly via heterodimerization.
  • GPCR-Mediated EGFR Transactivation: Unique requirement of HBEGF for G protein-coupled receptor ligands-mediated transactivation of EGFR. In this way, GPCR ligands could activate metalloproteinases (ADAM17) to release HBEGF and subsequently activated EGFR.

HBEGF Membrane Protein Product

Creative Biolabs provides high-quality HBEGF membrane protein products designed to support research in cell signaling, vascular biology, and cancer biology. HBEGF is synthesized as a membrane-associated precursor, proHB-EGF, which can participate in receptor interactions and can be proteolytically processed to release soluble HB-EGF. Our HBEGF membrane protein products are intended to support studies of the membrane-associated form, including structural studies, receptor-binding research, antibody development and characterization, and mechanistic investigations of EGFR-related signaling. Available product formats and applicable research uses should be determined according to the corresponding product information.

HBEGF Membrane Protein Product

Not finding the membrane protein product you need? Contact us to start your one-stop custom service!

HBEGF Stable Cell Line Product

The generation of reliable cell line models is important for the study of HBEGF. Custom-engineered HBEGF stable cell lines that stably express high levels of target HBEGF protein are offered for Creative Biolabs. This will provide stable cell lines suitable for drug screening, ligand binding, ectodomain shedding assays and GPCR transactivation studies together with stable high-throughput screening to enable accurate analysis of HBEGF biology and pharmacology. We optimize expression and maintain cell viability to maximize your pipeline. We present lines with or without HBEGF overexpression for studies of juxtacrine signaling and ADAM17-mediated shedding, and loss-of-function studies with validated expression including flow cytometry, Western blotting, and functional EGFR activation assays. Here we describe specialized reporter cell lines that incorporate either EGFR-dependent luciferase or ERK phosphorylation readouts, allowing for real-time monitoring of HBEGF-mediated signaling and application to therapeutic screening in cardiovascular and wound healing models.

HBEGF Stable Cell Line Product

Not finding the stable cell line product you need? Contact us to start your one-stop custom service!

HBEGF Recombinant Antibody Product

We offer a wide range of high-affinity recombinant antibodies for HBEGF to satisfy the requirements of different research areas. In comparison to conventional polyclonal antibodies, these antibodies produced via modern recombinant technologies exhibit improved specificity, sensitivity and batch-to-batch reproducibility. Validated in Western Blotting (WB), ELISA, Flow Cytometry (FCM), Immunofluorescence (IF), Immunocytochemistry (ICC) and Immunohistochemistry (IHC) and your choice for detecting the HBEGF from the wound tissue homogenates, atherosclerotic plaques, cardiac tissues, serum and cell culture supernatants with our specifically developed recombinant antibodies. We provide sHB-EGF/proHB-EGF–specific antibodies that can be utilized to accurately define the shedding state and signaling mode in various physiological or pathological settings. New probes directed against the heparin-binding domain, the EGF-like domain and cytoplasmic tail allow for more precise studies of HBEGF functional roles and regulation by pharmacological means.

HBEGF Recombinant Antibody Product

Not finding the recombinant antibody product you need? Contact us to start your one-stop custom service!

Product Features

  • High Purity & Activity: High purity and verified integrity for dependable downstream work.
  • Diverse Expression Systems: Choice of expression formats to match routine or specialized projects.
  • Species Reactivity: Products available for human, mouse, pig, and other species.
  • Validated Applications: Application-tested to deliver consistent signals across common lab workflows.
  • Exceptional Lot-to-Lot Consistency: Tight lot-to-lot control for reproducible performance.
  • Customization Options: Flexible customization of tags, labels, or packaging upon request.

Custom HBEGF Membrane Protein and Antibody Discovery Services

In addition to our vast catalogue items, Creative Biolabs has the capacity for custom protein engineering and antibody discovery solutions tailored to your specific needs for HBEGF-related research programs. We offer an integrated service platform that fuses premium structure biology expertise with next generation molecular engineering to deliver best-in-class solutions beyond the off-the-self paradigm:

  • Custom HBEGF Receptor Production: Tailored expression, purification, and characterization of challenging multi-domain receptor constructs.
  • Custom Antibody Development: From antigen design to antibody engineering (monoclonal, polyclonal, recombinant) for specific research applications.
  • Stable Cell Line Development: Generation of bespoke stable cell lines expressing your target of interest.
  • Functional Assay Development: Designing and executing assays to assess receptor activation and ligand.

Frequently Asked Questions (FAQ)

  1. Is the field of Creative Biolabs capable of expressing HBEGF variants that shed differently or have different receptor specificity compared to wild-type?

    Absolutely. We offer a variety of protein engineering services based on custom modifications, which are designed with shedding-resistant juxtamembrane mutants (ADAM17 cleavage site substitutions), heparin-binding domain deletions and EGF-like domain point mutations, diphtheria toxin-binding site mutants, tag fusions (His, Fc, GST and biotin) and formulations prepared to meet your requirements. Our scientific team works with our clients to develop constructs for juxtacrine signaling researchers, structural biologists, therapeutic screeners and conditional cell ablation model developers.

  2. What types of HBEGF products does Creative Biolabs offer?

    We provide extensive products including recombinant HBEGF soluble proteins (wild-type mature form, heparin-binding domain-containing mutants, shedding-resistant mutations), stable cell lines expressing recombinant HBEGF (overexpressing and reporter cell lines), high-affinity antibodies to recombinant human HBEGF(proHB-EGF-specific,sHB-EGF-specific, neutralizing), and fully customized protein engineering and antibody discovery services. This means you can obtain products for different species and expression systems.

  3. Is your recombinant soluble HBEGF provided in a carrier-free formulation maintaining the heparin-binding competence to be used instantly in cell proliferation, receptor binding & wound healing scratch assays?

    Yes, protein is purified reagent-free in a buffer without carrier protein or denaturing agents and supplied at physiological pH in endotoxin-monitored buffer. It enables direct dilution into serum-free culture media or assay buffers without dialysis and preserves both disulfide-linked EGF-like fold as well as the heparin-binding surface necessary for in vitro biological activity.

  4. Can Creative Biolabs'HBEGF products be used in clinical or diagnostic applications?

    Clinical diagnosis, therapeutic intervention, prophylaxis or human application is not intended. Researchers are within the remit of adhering to all appropriate institutional and personal regulatory requirements.

Reference
  1. Jain, Chandni V., et al. "Regulation of HBEGF by micro-RNA for survival of developing human trophoblast cells." PloS one 11.10 (2016): e0163913. Under Open Access license CC BY 4.0, without modification. https://doi.org/10.1371/journal.pone.0163913
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