Recombinant Human proHB-EGF Protein (C-6His)

Name: Recombinant Human proHB-EGF Protein (C-6His)
Brand: Beta LifeScience
SKU: BL-1115NP
Availability: InStock

BL-1115NP: Greater than 95% as determined by reducing SDS-PAGE. (QC verified)

Collections: Cytokines, Cytokines and growth factors, Growth factors and receptors, Recombinant proteins

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Heparin Binding EGF like Growth Factor is produced by our Mammalian expression system and the target gene encoding Leu20-Leu148 is expressed with a 6His tag at the C-terminus.
Accession	Q99075
Synonym	Diphtheria toxin receptor; DTR;HEGFL; heparin-binding EGF-like growth factor; DTS; DTSF; heparin-binding epidermal growth factor; proheparin-binding EGF-like growth factor; HB-EGF; pro HB-EGF
Gene Background	Heparin-binding EGF-like growth factor (HB-EGF) is a 1216 kDa member of the epidermal growth factor (EGF) family. It possesses an EGFlike domain, and a heparin-binding motif. Mature HBEGF is a soluble peptide that arises from proteolytic processing of the transmembrane form. Human HBEGF shows 76% and 73% aa sequence identity with rat and mouse HBEGF, respectively. It is required for normal cardiac valve formation and normal heart function, promotes smooth muscle cell proliferation. It may be involved in macrophage-mediated cellular proliferation; it is mitogenic for fibroblasts, but not endothelial cells. HBEGF classified as a group 2 ErbB ligand based on its ability to activate both the EGF/ErbB1 and ErbB4 receptors. Activity associated with ErbB4 binding appears to be limited to nonmitogenic actions, while EGFR binding induces both mitogenic and nonmitogenic activity.
Molecular Mass	15.1 KDa
Apmol Mass	16-27 KDa, reducing conditions
Formulation	Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.
Endotoxin	Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Biological Activity	Not tested
Reconstitution	Always centrifuge tubes before opening.Do not mix by vortex or pipetting.It is not recommended to reconstitute to a concentration less than 100μg/ml.Dissolve the lyophilized protein in distilled water.Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt.Reconstituted protein solution can be stored at 2-8°C for 2-7 days.Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping	The product is shipped at ambient temperature.Upon receipt, store it immediately at the temperature listed below.
Usage	For Research Use Only

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: Hs.592942

Gene Functions References

levels of the angiogenesis mediators endoglin, HB-EGF, BMP-9 and FGF-2 in patients with severe sepsis and septic shock; endoglin and HB-EGF could be involved in the host response of sepsis; additional studies are warrant to investigate their role as biomarker or therapeutic targets in sepsis 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

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.