血管紧张素原(AGT)重组蛋白

血管紧张素原(AGT)重组蛋白

[ PROPERTIES ]

Residues: Ala155~Lys355

Tags: N-terminal His-Tag

Accession: P01019

Host: E. coli

Subcellular Location: Secreted.

Purity: >90%

Endotoxin Level: <1.0EU per 1μg

(determined by the LAL method).

Formulation: Supplied as lyophilized form in 10mM

PBS, pH7.4, containing 1mM DTT, 5% trehalose,

0.01% sarcosyl and preservative.

Predicted isoelectric point: 6.1

Predicted Molecular Mass: 24.5kDa

Accurate Molecular Mass: 21kDa as determined by SDS-PAGE reducing conditions.

Applications: SDS-PAGE; WB; ELISA; IP.

(May be suitable for use in other assays to be determined by the end user.)

Note: The possible reasons that the actual band size differs from the predicted are as follows:

1. Splice variants: Alternative splicing may create different sized proteins from the same gene.

2. Relative charge: The composition of amino acids may affects the charge of the protein.

3. Post-translational modification: Phosphorylation, glycosylation, methylation etc.

4. Post-translation cleavage: Many proteins are synthesized as pro-proteins, and then cleaved to

give the active form.

5. Polymerization of the target protein: Dimerization, multimerization etc.

[ 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.

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.

ADRLQA ILGVPWKDKN CTSRLDAHKV LSALQAVQGL LVAQGRADSQ AQLLLSTVVG

VFTAPGLHLK QPFVQGLALY TPVVLPRSLD FTELDVAAEK IDRFMQAVTG WKTGCSLMGA

SV DS T L A F N T YV H FQ GKM K G FS L L AE P QE F WV D NST S V SV PM L S GMG T FQ

HWSDIQDNFS VTQVPFTESA CLLLIQPHYA SDLDK

[ REFERENCES ]

1. Kageyama R., et al. (1984) Biochemistry 23:3603-3609.

2. Fukamizu A., et al. (1990) J. Biol. Chem. 265:7576-7582.

3. Kunapuli S.P., Kumar A. (1987) Circ. Res. 60:786-790.

4. Kunapuli S.P., et al. (1987) Arch. Biochem. Biophys. 254:642-646.

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