Recombinant Human Betacellulin / BTC Protein

Name: Recombinant Human Betacellulin / BTC Protein
Brand: Beta LifeScience
SKU: BLPSN-0397
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	N/A
Host Species	Human
Accession	P35070
Background	Betacellulin(BTC) is a member of the epidermal growth factor (EGF) family. These soluble proteins are ligands for one or more of the four receptor tyrosine kinases encoded by the ErbB gene family (ErbB-1/epidermal growth factor receptor (EGFR), neu/ErbB-2/HER2, ErbB-3/HER3 and ErbB-4/HER4). Betacellulin is a 32-kilodalton glycoprotein that appears to be processed from a larger transmembrane precursor by proteolytic cleavage. This protein is a ligand for the EGF receptor. BTC is a polymer of about 62-111 amino acid residues. Secondary Structure: 6% helical (1 helices; 3 residues)36% beta sheet (5 strands; 18 residues). BTC was originally identified as a growth-promoting factor in mouse pancreatic beta-cell carcinoma cell line and has since been identified in humans. It plays a role in the growth and development of the neonate and/or mammary gland function. Betacellulin is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells.
Description	A DNA sequence encoding the human BTC (P35070) (Met1-Tyr111) was expressed with six amino acids (LEVLFQ) at the C-terminus.
Source	HEK293
Predicted N Terminal	Asp 32
AA Sequence	Met1-Tyr111
Molecular Weight	The recombinant human BTC comprises 87 a.a. and has a predicted molecular mass of 9.8 kDa. The apparent molecular mass of the protein is approximately 24 kDa in SDS-PAGE under reducing conditions.
Purity	>90% as determined by SDS-PAGE
Endotoxin	< 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity	Measured in a cell proliferation assay using Balb/3T3 mouse embryonic fibroblast cells.The ED50 for this effect is typically 0.2-1 ng/mL.
Formulation	Lyophilized from sterile PBS, pH 7.4..
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Growth factor that binds to EGFR, ERBB4 and other EGF receptor family members. Potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells.
Subcellular Location	[Betacellulin]: Secreted, extracellular space.; [Probetacellulin]: Cell membrane; Single-pass type I membrane protein.
Database References	HGNC: 1121 OMIM: 600345 KEGG: hsa:685 STRING: 9606.ENSP00000379092 UniGene: Hs.591704
Tissue Specificity	Synthesized in several tissues and tumor cells. Predominantly expressed in pancreas and small intestine.

Gene Functions References

Our results suggest that betacellulin induces ovarian cancer migration and Slug-dependent E-cadherin down-regulation PMID: 27129169
CXCL8 production from lung cancer cells could be initiated by an autocrine mechanism or external sources of BTC. PMID: 24629040
Data suggest that BTC (betacellulin), AREG (amphiregulin), and EREG (epiregulin) induced prostaglandin E2 production by induction of COX-2 (prostaglandin-endoperoxide synthase 2) through MAP kinase signaling in granulosa cells. PMID: 24092824
BTC has properties of increasing retinal vascular leakage that could contribute to the development of diabetic retinopathy. PMID: 22183345
Data suggest a novel receptor-independent role for betacellulin intracellular-domain fragment signaling due to its ability to inhibit cell growth in vitro. PMID: 20530572
These are the first data that demonstrate an influence of betacellulin upon mesenchymal stem cells and the first to implicate HIF-alpha in betacellulin-mediated proliferation. PMID: 20165885
The solution structure of the EGF-like domain of betacellulin has been determined using two-dimensional nuclear magnetic resonance spectroscopy PMID: 12074582
The main structural properties of the model and the templates are compared and the hBTC conformation is closely similar to that of hTGFalpha. PMID: 12111392
Betacellulin and heregulin/NDF-alpha are involved in epidermal morphogenesis and/or in maintenance of the differentiated phenotype. PMID: 12768307
although BTC and EGF share overlapping signaling properties, the ability of BTC to enhance Erk activation occurs independent of Ras. PMID: 15192046
BTC may play a pivotal role as a local growth factor in promoting the differentiated villous trophoblastic function via ErbB-1 in early placentas and in contributing to placental growth through EVT cell function via ErbB-4 in term placentas. PMID: 15248827
Betacellulin is expressed in malignant fibrous histiocytoma and is a regulator of tumor growth. PMID: 15274392
shedding of precursor is mediated by ADAM10 PMID: 15507448
To determine if mutations in the betacellulin gene play a role in the development of type 2 diabetes, we screened subjects with type 2 diabetes for the presence of mutations. PMID: 15793259
Genetic variations in the protein-coding region of the human BTC gene are unlikely to be a major contributor to development of type 2 diabetes. PMID: 15936459
-226A/G polymorphism of the BTC gene may contribute to the development of diabetes. PMID: 16306376
intron 4 T-4 allele in the betacellulin gene is associated with lower risk of type 1 diabetes mellitus and may interact with human leukocyte antigen PMID: 16683131
Failure to confirm a role for nonsynonymous coding variants of betacellulin in the propensity to type 2 diabetes or to impaired insulin secretion in African American subjects. PMID: 16869959
Variants in the betacellulin gene do not play a major role in the development of type 2 diabetes in an Amish Caucasian populations PMID: 17479438
the ADAM10 prodomain inhibits betacellulin shedding, demonstrating that it could be of potential use as a therapeutic agent to treat cancer. PMID: 17895248
1st report of BTC expression in breast cancer. Its expression was lower in lobular breast cancers than in ductal carcinomas. PMID: 17962208
These results indicate the possibility of designing BTC mutants, which have an activity of inducing differentiation only, without facilitating growth promotion. PMID: 18508082
In vivo, EGFR signaling is hyperactive in tumor cells of skin SCC but not of BCC, and in nearby asymptomatic epidermis of both tumor types. Hyperactivation is due to upregulation of EGFR ligands AREG, HBEGF and TGFA, and downregulation of BTC PMID: 17525275

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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.

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