Human EGFR ELISA Kit | EGFR elisa kit

EGFR (Human) OmniKine ELISA Kit

Cat. Num. AAA9501944

• Gene Names: EGFR; ERBB; HER1; mENA; ERBB1; PIG61; NISBD2
• Reactivity: Human
• Synonyms: EGFR; EGFR (Human) OmniKine ELISA Kit; Epidermal growth factor receptor; Proto-oncogene c-ErbB-1; Receptor tyrosine-protein kinase erbB-1; ERBB1; EGFR elisa kit

• Reactivity: Human
• Specificity: The OmniKine Human EGF-R ELISA is capable of recognizing both recombinant and naturally produced Human EGF-R proteins. The antigens listed below were tested at 50 ng/ml and exhibited less than 3% cross reactivity.; Murine: EGF-R; The antigens listed below were tested at 50 ng/ml and did not exhibit significant cross reactivity or interference.; Human: EGF, ErbB2, ErbB3
• Form/Format: 12 x 8-Well Microstrips
• Sequence Length: 1210

• Assay Type: Quantitative Sandwich
• Preparation and Storage: Store at 4 degree C for 6 months.

Testing Data

(The OmniKine Human EGFR ELISA Kit allows for the detection and quantification of endogenous levels of natural and/or recombinant Human EGFR proteins within the range of 32-2000 pg/ml.)

Related Product Information for EGFR elisa kit

Principle of the Assay: The OmniKine Human BD-4 ELISA Kit contains the components necessary for quantitative determination of natural or recombinant Human BD-4 concentrations within any experimental sample including cell lysates, serum and plasma. This particular immunoassay utilizes the quantitative technique of a "Sandwich" Enzyme-Linked Immunosorbent Assay (ELISA) where the target protein (antigen) is bound in a "sandwich" format by the primary capture antibodies coated to each well-bottom and the secondary detection antibodies added subsequently by the investigator. The capture antibodies coated to the bottom of each well are specific for a particular epitope on Human BD-4 while the user-added detection antibodies bind to epitopes on the captured target protein. Amid each step of the procedure, a series of wash steps must be performed to ensure the elimination of non-specific binding between proteins to other proteins or to the solid phase. After incubation and "sandwiching" of the target antigen, a peroxidase enzyme is conjugated to the constant heavy chain of the secondary antibody (either covalently or via Avidin/Streptavidin-Biotin interactions), allowing for a colorimetric reaction to ensue upon substrate addition. When the substrate TMB (3, 3', 5, 5'-Tetramethylbenzidine) is added, the reaction catalyzed by peroxidase yields a blue color that is representative of the antigen concentration. Upon sufficient color development, the reaction can be terminated through addition of Stop Solution (2 N Sulfuric Acid) where the color of the solution will turn yellow. The absorbance of each well can then be read by a spectrophotometer, allowing for generation of a standard curve and subsequent determination of protein concentration!!Background/Introduction: cytokine protein, encoded by the DEFB104AB gene, which is commonly known for its antimicrobial activity via synergistic effects with lysozymes and Beta-Defensin 3. The antimicrobial activity displayed by BD-4 is commonly dependent upon the sodium chloride concentration in the vicinity of the cell such that the antibiotic capability is decreased as NaCl concentration increases and vice versa. The BD-4 peptide undergoes proteolytic processing further into its mature form via cleavage of its 22 residue signal sequence, resulting in the mature 50 residue BD-4 cytokine. The mature forms of all 4 types of Beta-Defensin cytokines are distinguished from their Alpha-Defensin counterparts such that they contain the characteristic 6 cysteine structural motifs via 3 disulfide linkages. Generally, defensins form a family of microbicidal and cytotoxic peptides made by neutrophils. Moreover, members of the defensin family are highly similar in protein sequence. In terms of tissue specificity, Human BD-4 is highly expressed in male testes while expressed much less in the female uterus. Furthermore, the cytokine is highly prevalent on the plasma membranes of gastric antrum while lower in neutrophils, thyroid glands, lungs and kidneys. Aside from its antimicrobial functions, human Beta-Defensin 4 is attracted via chemical stimuli towards immature dendritic cells and memory T-cells.

NCBI and Uniprot Product Information

• NCBI GI #: 29725609
• NCBI GeneID: 1956
• NCBI Accession #: NP_005219.2
• NCBI GenBank Nucleotide #: NM_005228.4
• UniProt Accession #: P00533; O00688; O00732; P06268; Q14225; Q68GS5; Q92795; Q9BZS2; Q9GZX1; Q9H2C9; Q9H3C9; Q9UMD7
• Molecular Weight: 69,228 Da
• NCBI Official Full Name: epidermal growth factor receptor isoform a
• NCBI Official Synonym Full Names: epidermal growth factor receptor
• NCBI Official Symbol: EGFR
• NCBI Official Synonym Symbols: ERBB; HER1; mENA; ERBB1; PIG61; NISBD2
• NCBI Protein Information: epidermal growth factor receptor
• UniProt Protein Name: Epidermal growth factor receptor
• Protein Family: Epidermal growth factor receptor
• UniProt Gene Name: EGFR
• UniProt Synonym Gene Names: ERBB; ERBB1; HER1

NCBI Description

The protein encoded by this gene is a transmembrane glycoprotein that is a member of the protein kinase superfamily. This protein is a receptor for members of the epidermal growth factor family. EGFR is a cell surface protein that binds to epidermal growth factor. Binding of the protein to a ligand induces receptor dimerization and tyrosine autophosphorylation and leads to cell proliferation. Mutations in this gene are associated with lung cancer. [provided by RefSeq, Jun 2016]

Uniprot Description

EGFR: a receptor tyrosine kinase. This is a receptor for epidermal growth factor (EGF) and related growth factors including TGF-alpha, amphiregulin, betacellulin, heparin-binding EGF-like growth factor, GP30, and vaccinia virus growth factor. EGFR is involved in the control of cell growth and differentiation. It is a single-pass transmembrane tyrosine kinase. Ligand binding to this receptor results in receptor dimerization, autophosphorylation (in trans), activation of various downstream signaling molecules and lysosomal degradation. It can be phosphorylated and activated by Src. Activated EGFR binds the SH2 domain of phospholipase C-gamma (PLC-gamma), activating PLC-gamma-mediated downstream signaling. Phosphorylated EGFR binds Cbl, leading to its ubiquitination and degradation. Grb2 and SHC bind to phospho-EGFR and are involved in the activation of MAP kinase signaling pathways. Phosphorylation on Ser and Thr residues is thought to represent a mechanism for attenuation of EGFR kinase activity. EGFR is overexpressed in breast, head and neck cancers, correlating with poor survival. Activating somatic mutations are seen in lung cancer, corresponding to the minority of patients with strong responses to the EGFR inhibitor Iressa (gefitinib). Mutations and amplifications are also seen in glioblastoma, and upregulation is seen in colon cancer and neoplasms. In xenografts, inhibitors synergize with cytotoxic drugs in the inhibition of many tumor types. Inhibitors include: Iressa/ZD1839, Erbitux, Tarceva, and lapatinib. Four alternatively spliced isoforms have been described.

Protein type: EC 2.7.10.1; EGFR family; Kinase, protein; Membrane protein, integral; Protein kinase, TK; Protein kinase, tyrosine (receptor); TK group; Tumor suppressor

Chromosomal Location of Human Ortholog: 7p11.2

Cellular Component: AP-2 adaptor complex; apical plasma membrane; basolateral plasma membrane; cell surface; clathrin-coated vesicle membrane; cytoplasm; early endosome membrane; endoplasmic reticulum membrane; endosome; endosome membrane; extracellular space; focal adhesion; Golgi membrane; integral component of membrane; membrane; membrane raft; nuclear membrane; nucleus; perinuclear region of cytoplasm; plasma membrane; protein complex; receptor complex; Shc-EGFR complex; synapse

Molecular Function: actin filament binding; ATP binding; cadherin binding; calmodulin binding; chromatin binding; double-stranded DNA binding; enzyme binding; epidermal growth factor binding; epidermal growth factor receptor activity; identical protein binding; integrin binding; MAP kinase kinase kinase activity; nitric-oxide synthase regulator activity; phosphatidylinositol-4,5-bisphosphate 3-kinase activity; protein binding; protein heterodimerization activity; protein kinase binding; protein phosphatase binding; protein tyrosine kinase activity; Ras guanyl-nucleotide exchange factor activity; signal transducer, downstream of receptor, with protein tyrosine kinase activity; transmembrane receptor activity; transmembrane receptor protein tyrosine kinase activity; ubiquitin protein ligase binding; viral receptor activity

Biological Process: activation of MAPKK activity; activation of phospholipase C activity; astrocyte activation; calcium-dependent phospholipase A2 activation; cell proliferation; cell surface receptor signaling pathway; cellular response to cadmium ion; cellular response to dexamethasone stimulus; cellular response to epidermal growth factor stimulus; cellular response to estradiol stimulus; cellular response to reactive oxygen species; cerebral cortex cell migration; circadian rhythm; digestive tract morphogenesis; diterpenoid metabolic process; embryonic placenta development; entry of virus into host cell; epidermal growth factor receptor signaling pathway; ERBB2 signaling pathway; hair follicle development; hydrogen peroxide metabolic process; learning and/or memory; lung development; magnesium ion homeostasis; MAPK cascade; midgut development; negative regulation of apoptosis; negative regulation of cardiocyte differentiation; negative regulation of epidermal growth factor receptor signaling pathway; negative regulation of ERBB signaling pathway; negative regulation of mitotic cell cycle; negative regulation of protein catabolic process; neuron projection morphogenesis; ossification; ovulation cycle; peptidyl-tyrosine autophosphorylation; peptidyl-tyrosine phosphorylation; phosphatidylinositol phosphorylation; positive regulation of blood vessel diameter; positive regulation of bone resorption; positive regulation of cell growth; positive regulation of cell migration; positive regulation of cell proliferation; positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle; positive regulation of DNA repair; positive regulation of DNA replication; positive regulation of epithelial cell proliferation; positive regulation of ERK1 and ERK2 cascade; positive regulation of fibroblast proliferation; positive regulation of inflammatory response; positive regulation of MAP kinase activity; positive regulation of NIK/NF-kappaB signaling; positive regulation of nitric oxide biosynthetic process; positive regulation of peptidyl-serine phosphorylation; positive regulation of phosphorylation; positive regulation of prolactin secretion; positive regulation of protein kinase B signaling; positive regulation of protein kinase C activity; positive regulation of protein phosphorylation; positive regulation of smooth muscle cell proliferation; positive regulation of superoxide anion generation; positive regulation of synaptic transmission, glutamatergic; positive regulation of transcription from RNA polymerase II promoter; positive regulation of transcription, DNA-templated; positive regulation of vasoconstriction; protein autophosphorylation; protein insertion into membrane; regulation of cell motility; regulation of ERK1 and ERK2 cascade; regulation of JNK cascade; regulation of nitric-oxide synthase activity; regulation of peptidyl-tyrosine phosphorylation; regulation of phosphatidylinositol 3-kinase signaling; regulation of transcription from RNA polymerase II promoter; response to calcium ion; response to cobalamin; response to hydroxyisoflavone; response to osmotic stress; response to stress; salivary gland morphogenesis; signal transduction; tongue development; translation; wound healing

Disease: Inflammatory Skin And Bowel Disease, Neonatal, 2; Lung Cancer