Recombinant Human HB-EGF (Heparin Binding EGF) Protein

Name: Recombinant Human HB-EGF (Heparin Binding EGF) Protein
Brand: Beta LifeScience
SKU: BL-1610SG
Availability: InStock

Collections: Buy cytokines, chemokines, and growth factors for research online, Growth factors and receptors for advanced research, High-quality recombinant proteins

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Product Overview

Tag	N/A
Host Species	Human
Accession	Q99075
Synonym	Heparin Binding EGF-like growth factor, HBEGF, Diphtheria toxin receptor, DTR
Background	Human HBEGF (Heparin Binding EGF like growth factor) is a member of the EGF family of peptide growth factors that signal through the EGF receptor, and stimulates the proliferation of smooth muscle cells, fibroblasts, epithelial cells, and keratinocytes. HBEGF is expressed in many cell types and tissues, including bronchial epithelium, visceral and vascular smooth muscle, CD4+ T cells, glomerular podocytes, keratinocytes, macrophages and certain tumor cells. Mature HBEGF is a soluble peptide that arises from the proteolytic processing of the 208 amino acid type-I transmembrane form and exhibits the ability to specifically bind heparin and heparin sulfate proteoglycans.
Description	Recombinant Human HB-EGF (Heparin Binding EGF) was produced in E. coli. This protein is purified with our unique purification methods.
Source	E.coli
Molecular Weight	10.1 kDa
Purity	For specific purity information on a given lot, see related COA.
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Formulation	Recombinant protein is supplied in 50mM Tris-HCl, pH 7.5, 50mM NaCl, 10mM Glutathione, 0.25mM DTT, 0.1mM EDTA, 0.1mM PMSF and 25% glycerol.
Stability	The recombinant protein is stable for up to 12 months at -70°C
Usage	For Research Use Only
Storage	Recombinant Human HB-EGF (Heparin Binding EGF) Protein should be stored should be stored at < -70°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target 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.
Subcellular Location	[Heparin-binding EGF-like growth factor]: Secreted, extracellular space. Note=Mature HB-EGF is released into the extracellular space and probably binds to a receptor.; [Proheparin-binding EGF-like growth factor]: Cell membrane; Single-pass type I membrane protein.
Database References	HGNC: 3059 OMIM: 126150 KEGG: hsa:1839 STRING: 9606.ENSP00000230990 UniGene: PMID: 28746898 HB-EGF plays a pro-inflammatory role in the active skin and lung lesions of systemic sclerosis. PMID: 29044628 HB-EGF expression in serum may be a potential therapeutic indicator for novel HB-EGF-targeted therapy in recurrent ovarian cancer. PMID: 29970572 both HBEGF upregulation and apoptosis were rescued by exogenous MMP2 PMID: 28731464 Results support the idea that excess heparin binding epidermal growth factor-like growth factor (HB-EGF) leads to a significant elevation of vascular endothelial growth factor (VEGF) and ventricular dilatation. These data suggest a potential pathophysiological mechanism that elevated HB-EGF can elicit VEGF induction and hydrocephalus. PMID: 27243144 These results suggest that HBEGF is an important EGFR ligand in cervical cancer and that cervical cancer cells are the predominant source of HBEGF. Therefore, we propose an autocrine EGFR stimulation model in cervical carcinomas. PMID: 28498437 macrophage-secreted MMP-9 released HB-EGF from macrophages, which increased MMP9 in OVCA433, resulting in a positive feedback loop to drive HB-EGF release and increase proliferation in co-culture. PMID: 27888810 Genome-wide significant (GWS) associations in single-nucleotide polymorphism (SNP)-based tests (P < 5 x 10(-8)) were identified for SNPs in PFDN1/HBEGF, USP6NL/ECHDC3, and BZRAP1-AS1. PMID: 28183528 HB-EGF is implicated in DNA double strand breaks repair as silencing of HB-EGF increased gammaH2AX foci half-life as well as USP9X expression, two features that could be linked to the observed effect on Mcl-1. PMID: 28970067 Heparan sulfate proteoglycans and heparin derivatives further enhance HBEGF-induced differentiation by forming a complex with the epidermal growth factor receptor PMID: 28174207 this study suggests that HBEGF promotes the formation of gliomas, is necessary for tumor maintenance and therefore may be a novel therapeutic target. PMID: 28368403 Results show that HBEGF is highly expressed in primary ovarian tumors and increases as the disease progresses. PMID: 28668900 Serous carcinomatous component championed by expression of HB-EGF predisposes to recurrence/metastasis in stage I metastasis and recurrence in stage I uterine malignant mixed mullerian tumor. PMID: 26980026 Annexin A2 and HB-EGF are overexpressed and are being secreted into serum in Her-2 negative breast cancer patients. PMID: 27496793 Study demonstrates that HBEGF is post-transcriptionally regulated by low O2 (placental environment) through a mechanism involving interactions of miRNAs with its 3'UTR. PMID: 27701455 MMP14 plays an important mechanistic role in NSCLC progression, by supporting cancer invasiveness, promoting collagen degradation, and releasing HB-EGF, which accelerates lung tumor progression. PMID: 28013056 These results indicate that this new anti-HB-EGF mAb 2-108 would be useful in the diagnosis of HB-EGF-related cancers and would be a strong tool in both basic and clinical research on HB-EGF. PMID: 26974561 This antibody reacts with human HB-EGF but not mouse HB-EGF. No cross-reactivity to other EGFR ligands was observed by antigen ELISA. PMID: 27097072 HB-EGF is a molecular target for the resistance of ovarian cancer to paclitaxel and CRM197 as a HB-EGF-targeted agent might be a chemosensitizing agent for paclitaxel-resistant ovarian carcinoma PMID: 26572150 Data suggest that placental expression of HBEGF, EGF (epidermal GF), and TGFA (transforming GF alpha) is down-regulated in pre-eclampsia as compared to normal term birth; each growth factor blocks cell death/apoptosis of cytotrophoblast cell line. PMID: 25589361 Serum sHB-EGF is closely correlated with advanced stage gastric cancer and can be a promising serological biomarker for GC. PMID: 25717241 Studies indicate that heparin-binding EGF-like growth factor (HB-EGF) is a therapeutic target in some types of cancers. PMID: 25517307 the relative expression of hyalurosome (CD44, HAS3, HB-EGF) genes was found to be reduced in patients prior to topical treatment and to be notably increased following treatment. PMID: 25138066 Urinary levels of NGF and HB-EGF may be potential biomarkers for evaluating outcome of overactive bladder syndrome treatment. PMID: 25510766 HB-EGF is a biomarker for LPA1 receptor activation in human breast and prostate cancers. PMID: 24828490 MiR-212 exerts suppressive effect on SKOV3 ovarian cancer cells through targeting HBEGF. PMID: 25201063 Suggest high levels of HB-EGF contribute to carotid plaque stabilization and reduce the incidence of acute coronary events. PMID: 25359857 Autocrine HBEGF expression promotes breast cancer intravasation, metastasis and macrophage-independent invasion in vivo. PMID: 24013225 studies suggest disintegrin and metalloproteinase domain-containing protein 12(ADAM 12S) and heparin-binding epidermal growth factor-like growth factor(HB-EGF) are involved in cellular plasticity resulting in production of brown adipose tissue-like cells PMID: 24116709 Knockdown of HSP27 by shRNA decreased HB-EGF plus CXCL5-mediated tumor spheroid formation in a three-dimensional culture system, suggesting that AKT/HSP27 was required for HB-EGF/CXCL5-mediated cancer progression PMID: 24346967 Heparin-binding epidermal growth factor and CD9 are likely implicated in processes that are highly relevant for MS lesion formation PMID: 24038577 HB-EGF acts as a potent paracrine and/or autocrine chemotactic factor as well as a mitogen that mediates HER1 and/or HER4 in the invasion and metastasis of thyroid carcinoma cells. PMID: 23917679 Results suggest that HB-EGF plays a pivotal role in the acquisition of tumor aggressiveness in TNBC by orchestrating a molecular hierarchy regulating tumor angiogenesis. PMID: 23443317 HB-EGF overexpression and Kras(G12D) together, but neither alone, increase cancer cell proliferation. PMID: 23376846 Correlation has been found between HB-EGF expression/immunostaining and the different types of analyzed soft tissue sarcomas. PMID: 23597914 The study suggest that one of the causes of unexplained miscarriages may result from the impaired expression of heparanase and heparin-binding EGF-like growth factor. PMID: 23907942 A reciprocal cross-talk between intrahepatic cholangiocarcinoma cells and myofibroblasts through the HB-EGF/EGFR axis contributes to CCA progression. PMID: 23787814 a mechanism of a probiotic-derived soluble protein in modulating intestinal epithelial cell homeostasis through ADAM17-mediated HB-EGF release, leading to transactivation of EGFR. PMID: 24043629 visualized spatiotemporal regulation of proHB-EGF shedding in individual cells using a simple method that measures changes in fluorescence ratios PMID: 23598347 results indicate that Abl kinases negatively regulate HNSCC invasive processes through suppression of an HB-EGF autocrine loop responsible for activating a EGFR-Src-cortactin cascade PMID: 23146907 Our results show that HB-EGF acts as a cell proliferation and cell survival factor in cancer cells. PMID: 23349913 Hypoxia increased the levels and activity of the ADAM12 metalloprotease in a Notch signaling-dependent manner, leading to increased ectodomain shedding of the epidermal growth factor (EGF) receptor (EGFR) ligand heparin-binding EGF-like growth factor. PMID: 23589494 HB-EGF-C nuclear translocation might be crucial in gastric cancer invasion. HB-EGF-C nuclear translocation may offer a prognostic marker and a new molecular target for gastric cancer therapy. PMID: 22646534 expression of HB-EGF in human KCs triggers a migratory and invasive phenotype with many features of epithelial-mesenchymal transition (EMT), which may be beneficial in the context of cutaneous wound healing. PMID: 22592159 Results suggest that heparin-binding epidermal growth factor (EGF)-like growth factor (HB-EGF) is a target for oral cancer and that CRM197 is effective in oral cancer therapy. PMID: 22718294 variant 1936T prevents hsa-miR-1207-5p from down-regulating HBEGF in podocytes PMID: 22319602 study is the first report demonstrating a role for the ADAM-HBEGF-EGF receptor axis in Ox-PAPC induction of IL-8 in HAECs. PMID: 22402363 These results confirm that polymorphisms in the HGEGF gene are associated with pre-eclampsia. PMID: 22136955 Heparin-binding epidermal growth factor-like growth factor is a potent autocrine regulator of invasion activity in oral squamous cell carcinoma. PMID: 22209887 Lung cancer-derived galectin-1 enhances tumorigenic potentiation of tumor-associated dendritic cells by expressing heparin-binding EGF-like growth factor. PMID: 22291012

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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