Recombinant Human Pro-Epidermal Growth Factor (EGF), Active

Name: Recombinant Human Pro-Epidermal Growth Factor (EGF), Active
Brand: Beta LifeScience
SKU: BLC-05958P
Availability: InStock

Greater than 95% as determined by SDS-PAGE.

Collections: Buy cytokines, chemokines, and growth factors for research online, Growth factors and receptors for advanced research, High-quality cytokines for advanced research, High-quality recombinant proteins, Recombinant epidermal growth factor (egf) 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 Pro-Epidermal Growth Factor (EGF), Active is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 95% as determined by SDS-PAGE.
Endotoxin	Less than 1.0 EU/μg as determined by LAL method.
Activity	The ED50 as determined by the dose-dependent proliferation of murine BALB/c 3T3 cells is typically 0.1-0.5 ng/ml
Uniprotkb	P01133
Target Symbol	EGF
Synonyms	Beta urogastrone; beta-urogastrone; EGF; EGF_HUMAN; Epidermal growth factor; HOMG4; OTTHUMP00000219721; OTTHUMP00000219722; Pro epidermal growth factor; URG; Urogastrone
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	Tag-Free
Complete Sequence	NSDSECPLSHDGYCLHDGVCMYIEALDKYACNCVVGYIGERCQYRDLKWWELR
Expression Range	971-1023aa
Protein Length	Partial
Mol. Weight	6.2 kDa
Research Area	Signal Transduction
Form	Lyophilized powder
Buffer	Lyophilized from a 0.2 μm Filtered 20 mM Tris-HCl, 200 mM NaCl, pH 8.0
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	EGF stimulates the growth of various epidermal and epithelial tissues in vivo and in vitro and of some fibroblasts in cell culture. Magnesiotropic hormone that stimulates magnesium reabsorption in the renal distal convoluted tubule via engagement of EGFR and activation of the magnesium channel TRPM6. Can induce neurite outgrowth in motoneurons of the pond snail Lymnaea stagnalis in vitro.
Subcellular Location	Membrane; Single-pass type I membrane protein.
Database References	HGNC: 3229 OMIM: 131530 KEGG: hsa:1950 STRING: 9606.ENSP00000265171 UniGene: PMID: 30226622 These results highlight the potential role of EGF in promoting hepatocellular carcinoma (HCC) metastasis, demonstrate a novel pathway for regulation of FN expression and provide potential targets for HCC prevention and treatment. PMID: 29315755 The abnormally elevated expression of EGF and TGF-alpha are closely associated with the occurrence and development of chronic pancreatitis and pancreatic cancer PMID: 29125273 ERRa positively regulated the cell proliferation, migration and invasion of colon cancer cells, and the suppression of ERRa completely reduced the EGF treatment-induced proliferation of colon cancer cells. PMID: 30185207 EGF significantly upregulated RFPL3 and hTERT protein levels in the nonsmall cell lung cancer cells. RFPL3 and hTERT proteins upregulation by EGF were attenuated by pretreatment with AG1478 and erlotinib. EGF promoted proliferation and inhibited apoptosis; PD98059 decreased RFPL3 and hTERT protein expression; and RFPL3 overexpression increased the expression of hTERT and related MEKpathway proteins. PMID: 29749533 we have discovered the novel N-72, and it was crucial for EGF-induced migration by targeting MMP2 in Human amnion mesenchymal stem cells (hAMSCs) PMID: 29734654 The spleen can regulate the functions of hematopoietic stem cells in cirrhotic hypersplenism by regulating EGF signaling. PMID: 29721775 After HIP1 expression was blocked by siRNAs, EGFR endocytosis was accelerated and this effect was dependent on the EGF concentration. This endocytosis was colocalized with clathrin expression. These findings indicate that the inhibition of HIP1 can accelerate the endocytosis and degradation of EGFR PMID: 29039605 the present study demonstrated that EGF induced aggressiveness of gastric cancer cells by activating epithelial to mesenchymal transition, which involved the activation of the ERK1/2 pathway and, subsequently, uPAR expression PMID: 28849196 the EGF system is a mechanosensitizer in bone marrow stromal cells. PMID: 28843157 EGF counteracts Tat modulation of human endogenous retroviruses of the W family in astrocytes. PMID: 28474333 FTIR spectra of EGF, unconjugated, post treatment with alpha-lipoic acid, attached to gold nanoparticle, and bound to the bifunctional nanoprobe, showed decreasing disordered structures and turns, and increasing loops, as the synthesis process progressed. There was an overall increase in beta-sheets in final product compared to pure EGF, but this increase was not linear and fluctuated. PMID: 29122663 EGF-mediated lysosome trafficking, protease secretion, and invasion is regulated by the activity of p38 mitogen activated protein kinase (MAPK) and sodium hydrogen exchangers (NHEs). Interestingly, EGF stimulates anterograde lysosome trafficking through a different mechanism than previously reported for HGF, suggesting that there are redundant signaling pathways that control lysosome positioning PMID: 28978320 Although the diabetic chronic wounds microenvironment is hostile for local GFs bioavailability, EGF local infiltration circumvented the limitations of its topical application, thus expanding its therapeutic prospect. Our clinical pharmacovigilance and basic studies attest the significance of the GF local infiltration for chronic wounds healing. PMID: 28904952 these results provide the first evidence for an association between the EGF rs2298999 C/T polymorphism and gout PMID: 27506295 The increased EGFR expression revealed in patients with seborrheic keratomas (SK)and concomitant (type 2 diabetes mellitus (DM2))is caused by insulin resistance and hyperinsulinemia, in which the dysregulation of insulin signal transmission into the cell leads to changes in EGF synthesis and signaling pathway that regulates cell proliferation and growth. PMID: 28791994 novel EGFR-NF-kappaB-FOXC1 signaling axis that is critical for BLBC cell function PMID: 28629477 EGFR pathway gene expression analysis indicated that DeltaNp63 alters EGFR-regulated genes involved in cell adhesion, migration, and angiogenesis. Addition of EGF or neutralizing EGFR antibodies demonstrated that EGFR activation is responsible for DeltaNp63-mediated loss of cellular adhesion PMID: 28349272 EGF up-regulated CCL2 expression in HNSCC cells, which recruited monocytes and turned them into M2-like macrophages, thus forming a positive feedback paracrine loop. PMID: 27888616 this study shows that EGF induces epithelial-mesenchymal transition through phospho-Smad2/3-Snail signaling pathway in breast cancer cells PMID: 27829223 EGF and TNFalpha cooperatively promoted the motility of HCC cells mainly through NF-kappaB/p65 mediated synergistic induction of FN in vitro. These findings highlight the crosstalk between EGF and TNFalpha in promoting HCC, and provide potential targets for HCC prevention and treatment. PMID: 28844984 Data suggest that EGF induces colorectal cancer cells to undergo epithelial-mesenchymal transition, enhances their ability to invade/migrate, and promotes phosphorylation of Ezrin at Tyr353. (EGF = epidermal growth factor) PMID: 28535417 Simulation results indicate that human epidermal growth factor receptor (hEGFR) soluble soluble extracellular domains (sECD):EGF show different dynamic properties between the two pHs, and the complex may have a higher tendency of activation at pH 8.5. PMID: 27179806 EGF and IP-10 were significantly elevated and GRO levels were lower in the tear profile of HIV patients with dry eye disease (DED) compared to immunocompetent patients with DED. PMID: 27585367 Data (including data from studies using transgenic/knockout mice) suggest that surfactant protein A1 (SPA1) interferes with EGF binding to EGFR in pulmonary alveoli cell lines; SPA1 directly binds extracellular domain of EGFR; binding of SPA1 to EGFR appears to be different from binding of SPD to EGFR; binding of SPA1 to EGFR does not suppress EGF-induced phosphorylation of EGFR or cell proliferation. PMID: 28972165 EGF-AREG interplay in airway basal cell stem/progenitor cells is one of the mechanisms that mediates the interconnected pathogenesis of all major smoking-induced lesions in the human airway epithelium. PMID: 27709733 caspase-3 inhibitors also suppressed the attenuation of cell adhesion and phosphorylation of p38 MAPK by EGF-F9. Our data indicated that EGF-F9 activated signals for apoptosis and induced de-adhesion in a caspase-3 dependent manner. PMID: 27129300 evidence that CDK1/2 participate in the regulation of constitutive pre-mRNA splicing by EGF stimulation in MDA-MB-468 cells. PMID: 27109354 The EGF rs4444903 GG genotype is associated with higher susceptibility to HCV-related liver cirrhosis and hepatocellular carcinoma in the Chinese Han population PMID: 28397482 TGF-beta opposes EGF-mediated sensitization to TRAIL-induced caspase-8 activation and apoptosis in non-transformed breast epithelial cells. EGF and TGF-beta finely regulate sensitivity of human breast epithelial cells to TRAIL which may be relevant during morphogenesis. PMID: 27208428 Amplification of the EGFR gene can be maintained and modulated by variation of EGF concentrations in in vitro models of glioblastoma multiforme PMID: 28934307 Our study showed that the EGF61 rs4444903GA genotype had a decreased risk of non-syndromic cleft lip with or without cleft palate. Our data provides further evidence regarding the role of EGF61 variations in the development of non-syndromic cleft lip with or without cleft palate in families of the studied populations PMID: 28906376 Interestingly, EGF rapidly downregulates LINC01089 (here renamed LncRNA Inhibiting Metastasis; LIMT) expression by enhancing histone deacetylation at the respective promoter. PMID: 27485121 EGF-induced, calpain-mediated proteolysis contributes to the rapid destruction of cyclin G2 and that the PEST domain is critical for EGF/calpain actions PMID: 28640887 The salivary levels of EGF are significantly increased during the acute phase of natural rotavirus infection. PMID: 28558652 findings have identified a role for members of these signaling pathways in the regulation of EGF-induced vimentin expression in the MDA-MB-468 breast cancer cell line PMID: 27163529 miR-223 downregulated the local expression of epidermal growth factor (EGF), leading to decreased activation of EGF receptor (EGFR) on target cells and, eventually, dampening a positive EGF-EGFR autocrine/paracrine stimulation loop induced by the post-surgical wound-healing response. PMID: 26876200 EGFR and EGF expression showed no significant difference between placentas from normal pregnancies and those complicated with preeclampsia. PMID: 27657362 Atomistic molecular dynamics simulations show that N-glycosylation of the EGFR extracellular domain plays critical roles in the binding of growth factors, monoclonal antibodies, and the dimeric partners to the monomeric EGFR extracellular domain. PMID: 28486782 CMTM3 decreases EGFR expression, facilitates EGFR degradation, and inhibits the EGF-mediated tumorigenicity of gastric cancer cells by enhancing Rab5 activity. PMID: 27867015 Findings suggest EGF not only promotes the proliferation of adipose stem cells and delays their senescence, but also maintains the differentiation potency of adipose stem cells, which are related to the EGF-induced activation of STAT signal pathway. PMID: 28746211 The results show that the interaction between STS-1 and ShcA is regulated in response to EGF receptor activation. PMID: 28690151 Insulin treatment caused sustained Akt activity, whereas EGF or PDGF-AA promoted transient signaling; PDGF-BB produced sustained responses at higher concentrations.Transient responses to EGF were caused by negative feedback at the receptor level, as a second treatment yielded minimal responses, whereas parallel exposure to IGF-I caused full Akt activation PMID: 27044757 our results indicate that different concentrations of bFGF and EGF supplemented during propagation of neural rosettes are involved in altering the identity of the resultant neural cells. PMID: 27321088 F25P preproinsulin effectively reduced the concentrations of EGF, VEGF, and MMP-9 in the blood of tumor-bearing mice with EGFR-mutant glioblastoma. PMID: 27317648 Conformational stability of the EGFR as influenced by glycosylation, dimerization and EGF hormone binding has been described. PMID: 28019699 Differential expression patterns of EGF, EGFR, and ERBB4 are essential in epithelial restitution and remodeling in nasal epithelium. PMID: 27285994 Phosphorylation and immunohistochemical assays on the EGF receptor in HeLa cells indicate the EGF protein produced in soybean seed is bioactive and comparable to commercially available human EGF. This work demonstrates the feasibility of using soybean seeds as a biofactory to produce therapeutic agents in a soymilk delivery platform. PMID: 27314851 Data suggest that activated platelets release ADAMDEC1, which hydrolyzes pro-EGF (epidermal growth factor) to soluble, active HMW-EGF; proteolytic cleavage of pro-EGF first occurs at the C-terminal arginyl residue of the EGF domain; proteolysis is the regulated, rate-limiting step in generating soluble EGF from activated platelets. PMID: 28455445 Subgroup analysis in a Slovak population by gender showed the genotype EGF G61G and allele G was associated with non significantly increased risk of MDD. PMID: 27755861

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.