Recombinant Human EGFR Protein

Name: Recombinant Human EGFR Protein
Brand: Beta LifeScience
SKU: BL-1132PS
Availability: InStock

Collections: Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, Car-nk targets proteins, Car-t cell therapy targets, Cytokines and growth factors, Growth factors and receptors, Recombinant proteins

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Product Overview

Tag	His
Host Species	Human
Synonym	Epidermal Growth FactorReceptor, Receptor Tyrosine-Protein Kinase ErbB-1, Erb-B2 Receptor TyrosineKinase, Proto-Oncogene C-ErbB-1, EC 2.7.10.1, ERBB1, ERBB, HER1, EpidermalGrowth Factor Receptor (Avian Erythroblastic Leukemia Viral (V-Erb-B)Oncogene Homolog), Erythroblastic Leukemia Viral (V-Erb-B) Oncogene Homolog(Avian), Avian Erythroblastic Leukemia Viral (V-Erb-B) Oncogene Homolog, CellProliferation-Inducing Protein 61, Cell Growth Inhibiting Protein 40, EC 2.7.10,NISBD2, PIG61, MENA.
Background	The epidermal growth factor receptor(EGF R) subfamily of receptor tyrosine kinases comprises four members: EGF R(also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), andErbB4 (HER-4). All family members are type I transmembrane glycoprotein thathas an extracellular domain which contains two cysteine-rich domains separatedby a spacer region that is involved in ligand-binding, and a cytoplasmic domainwhich has a membrane-proximal tyrosine kinase domain and a C-terminal tail withmultiple tyrosine autophosphorylation sites. The human EGF R gene encodes a1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aacytoplasmic domain. EGF R has been shown to bind a subset of the EGF familyligands, including EGF, amphiregulin, TGFa , betacellulin, epiregulin,heparin-binding EGF and neuregulin-2 in the absence of a co-receptor. Ligandbinding induces EGF R homodimerization as well as heterdimerization with ErbB2,resulting in kinase activation, tyrosine phosphorylation and cell signaling.EGF R can also be recruited to form heterodimers with the ligand-activatedErbB3 or ErbB4. EGF R signaling has been shown to regulate multiple biologicalfunctions including cell proliferation, differentiation, motility andapoptosis. In addition, EGF R signaling has also been shown to play a role incarcinogenesis.
Description	EGFR expressed in CHO cells is a single, glycosylated polypeptide chain containing 860a.a. (25-645 a.a.) and having a molecular weight of 95.5 kDa (Migrates at 100-150 on SDS-PAGE under reducing conditions). EGFR is expressed with a 239a.a. hIgG-His tag at C-Terminus and purified by unique purification methods.
Source	CHO
AA Sequence	LEEKKVCQGT SNKLTQLGTF EDHFLSLQRM FNNCEVVLGN LEITYVQRNY DLSFLKTIQE VAGYVLIALN TVERIPLENL QIIRGNMYYE NSYALAVLSN YDANKTGLKE LPMRNLQEIL HGAVRFSNNP ALCNVESIQW RDIVSSDFLS NMSMDFQNHL GSCQKCDPSC PNGSCWGAGE ENCQKLTKII CAQQCSGRCR GKSPSDCCHN QCAAGCTGPR ESDCLVCRKF RDEATCKDTC PPLMLYNPTT YQMDVNPEGK YSFGATCVKK CPRNYVVTDH GSCVRACGAD SYEMEEDGVR KCKKCEGPCR KVCNGIGIGE FKDSLSINAT NIKHFKNCTS ISGDLHILPV AFRGDSFTHT PPLDPQELDI LKTVKEITGF LLIQAWPENR TDLHAFENLE IIRGRTKQHG QFSLAVVSLN ITSLGLRSLK EISDGDVIIS GNKNLCYANT INWKKLFGTS GQKTKIISNR GENSCKATGQ VCHALCSPEG CWGPEPRDCV SCRNVSRGRE CVDKCNLLEG EPREFVENSE CIQCHPECLP QAMNITCTGR GPDNCIQCAH YIDGPHCVKT CPAGVMGENN TLVWKYADAG HVCHLCHPNC TYGCTGPGLE GCPTNGPKIP SRSPKSCDKT HTCPPCPAPE LLGGPSVFLF PPKPKDTLMI SRTPEVTCVV VDVSHEDPEV KFNWYVDGVE VHNAKTKPRE EQYNSTYRVV SVLTVLHQDW LNGKEYKCKV SNKALPAPIE KTISKAKGQP REPQVYTLPP SRDELTKNQV SLTCLVKGFY PSDIAVEWES NGQPENNYKT TPPVLDSDGS FFLYSKLTVD KSRWQQGNVF SCSVMHEALH NHYTQKSLSL SPGKHHHHHH.
Purity	Greaterthan 90.0% as determined by SDS-PAGE.
Endotoxin	<1.0 EU per μg by the LAL method.
Formulation	EGFR protein solution (0.25mg/ml) contains Phosphate Buffered Saline (pH 7.4) and 10% glycerol.
Stability	Recombinant protein is stable for 12 months at -70°C
Usage	For Research Use Only
Storage	Store at 4°C if entire vial will be used within 2-4 weeks. Store, frozen at -20°C for longer periods of time.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

FAQs

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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.