表皮生长因子受体2(EGFR2)重组蛋白

YB867Ra012
Recombinant Epidermal Growth Factor Receptor 2 (EGFR2)
Organism Species: Homo sapiens (Human)
Instruction manual
FOR IN VITRO USE AND RESEARCH USE ONLY
NOT FOR USE IN CLINICAL DIAGNOSTIC PROCEDURES
表皮生长因子受体2(EGFR2)重组蛋白10th Edition (Revised in Jan, 2014)
[ PROPERTIES ]
Residues: Phe376~Gly578
Tags: Two N-terminal Tags, His-tag and GST-tag
Accession: P04626
Host: E. coli
Subcellular Location: Cell membrane; Nucleus. Single-pass type I membrane protein. Cytoplasm,
perinuclear region.
Purity: >95%
表皮生长因子受体2(EGFR2)重组蛋白Endotoxin Level: <1.0EU per 1μg
(determined by the LAL method).
Formulation: Supplied as lyophilized form in 20mM Tris,
150mM NaCl, pH8.0, containing 1mM EDTA, 1mM DTT,
0.01% sarcosyl, 5% trehalose, and preservative.
Predicted isoelectric point: 5.9
Predicted Molecular Mass: 54.3kDa
Applications: SDS-PAGE; WB; ELISA; IP.
(May be suitable for use in other assays to be determined by the end user.)
[ USAGE ]
Reconstitute in sterile ddH2O.
[ STORAGE AND STABILITY ]
Storage: Avoid repeated freeze/thaw cycles.
Store at 2-8oC for one month.
Aliquot and store at -80oC for 12 months.
表皮生长因子受体2(EGFR2)重组蛋白Stability Test: The thermal stability is described by the loss rate of the target
protein. The loss rate was determined by accelerated thermal degradation test,
that is, incubate the protein at 37oC for 48h, and no obvious degradation and
precipitation were observed. (Referring from China Biological Products Standard,
which was calculated by the Arrhenius equation.) The loss of this protein is less
than 5% within the expiration date under appropriate storage condition.
[ SEQUENCES ]
The sequence of the target protein is listed below.
FLPES FDGDPASNTA PLQPEQLQVF ETLEEITGYL YISAWPDSLP DLSVFQNLQV
IRGRILHNGA YSLTLQGLGI SWLGLRSLRE LGSGLALIHH NTHLCFVHTV PWDQLFRNPH
QA LL HTA NRP EDE CVGEG LA CHQ L CA RGHC WGPGPTQCV N CSQ FL RGQE C
VEECRVLQGL PREYVNARHC LPCHPECQPQ NGSVTCFG
[ REFERENCES ]
1. Yamamoto T., et al. (1986) Nature 319:230-234. 2. Coussens L., et al. (1985) Science 230:1132-1139. 3. Semba K., et al. (1985) Proc. Natl. Acad. Sci. U.S.A. 82:6497-6501. 4. King C.R., et al. (1985) Science 229:974-976. 5. Sarkar F.H., et al. (1993) DNA Cell Biol. 12:611-615.