Fosfo-EGFR (Tyr1068) Polyklonale Antilichaam, APC-Cy7 Vervoeging

Protein kinases are enzymes that transfer a phosphate group from a phosphate donor onto an acceptor amino acid in a substrate protein. By this basic mechanism, protein kinases mediate most of the signal transduction in eukaryotic cells, regulating cellular metabolism, transcription, cell cycle progression, cytoskeletal rearrangement and cell movement, apoptosis, and differentiation. The protein kinase family is one of the largest families of proteins in eukaryotes, classified in 8 major groups based on sequence comparison of their tyrosine (PTK) or serine/threonine (STK) kinase catalytic domains. Epidermal Growth factor receptor (EGFR) is the prototype member of the type 1 receptor tyrosine kinases. EGFR overexpression in tumors indicates poor prognosis and is observed in tumors of the head and neck, brain, bladder, stomach, breast, lung, endometrium, cervix, vulva, ovary, esophagus, stomach and in squamous cell carcinoma.

EGFR; Avian erythroblastic leukemia viral v erb b oncogene homolog; Avian erythroblastic leukemia viral verbb oncogene homolog; Cell growth inhibiting protein 40; Cell proliferation inducing protein 61; EGF R; EGFR; Epidermal growth factor receptor avian erythroblastic leukemia viral v erb b oncogene homolog; Epidermal growth factor receptor erythroblastic leukemia viral v erb b oncogene homolog avian; Epidermal growth factor receptor; erbb 1; Erbb; Erbb1; HER1; mENA; Oncogene ERBB; PIG61; Receptor tyrosine protein kinase ErbB 1; Receptor tyrosine protein kinase ErbB1; Urogastrone; wa2; Wa5.

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Tyr1068

Human, Mouse, Rat

Phospho-EGFR (Tyr1068)

APC-Cy7

KLH conjugated synthetic phosphopeptide derived from rat EGFR around the phosphorylation site of Tyr1068

Flow-Cyt

Purified by Protein A.

650nm/780nm

1µg/µl

Flow-Cyt (1ug/Test)

Aqueous buffered solution containing 0.01M TBS (pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.

Phosphorylation

Store at -20°C. Aliquot into multiple vials to avoid repeated freeze-thaw cycles.

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