生长激素受体(GHR)重组蛋白
[ PROPERTIES ]
Residues: Lys315~Thr574 (Accession # P10912),
with two N-terminal Tags, His-tag and T7-tag. Host: E. coli
Subcellular Location: Cell membrane; Single-pass type I
membrane protein. Secreted.
Purity: >95%
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: 4.8
Predicted Molecular Mass: 32.5kDa
Accurate Molecular Mass: 44kDa 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 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 target protein is fused with two N-terminal Tags, His-tag and T7-tag, its
sequence is listed below.
MGSSHHHHHH SSGLVPRGSH MASMTGGQQM GRGSEF - KEGKLE EVNTILAIHD
SYKPEFHSDD SWVEFIELDI DEPDEKTEES DTDRLLSSDH EKSHSNLGVK DGDSGRTSCC
EPDILETDFN ANDIHEGTSE VAQPQRLKGE ADLLCLDQKN QNNSPYHDAC PATQQPSVIQ
AEKNKPQPLP TEGAESTHQA AHIQLSNPSS LSNIDFYAQV SDITPAGSVV LSPGQKNKAG
MSQCDMHPEM VSLCQENFLM DNAYFCEADA KKCIPVAPHI KVESHIQPSL NQEDIYITTE
SLTT
[ REFERENCES ]
1.Leung D.W., et al. (1987) Nature 330:537-543.
2. Godowski P.J., et al. (1989) Proc. Natl. Acad. Sci. U.S.A. 86:8083-8087.
3. Urbanek M., et al. (1992) Mol. Endocrinol. 6:279-287.
4. Dastot F., et al. (1996) Proc. Natl. Acad. Sci. U.S.A. 93:10723-10728.
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