Technical Data
A0007-07A
Abl Kinase Substrate (Abltide)
1mg
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Technical Data |
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A0007-07A |
Abl Kinase Substrate (Abltide) |
1mg |
| Molecular Biology | Storage: -20°CShipping: Blue Ice |
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Synthetic linear peptide (EAIYAAPFAKKK)(K); substrate for Abl kinase. Abl Protein Tyrosine Kinase (AbI) is a truncated form of the v-AbI Protein Tyrosine Kinase, a partner in the Gag-Abl fusion protein of the Abelson murine leukemia virus. Abl contains 407 amino acids (residues 237-643 of the p120-gag-abl polyprotein) which include the kinase catalytic domain, SH2 domain on the N-terminus and the I237M mutation. Abl is identical to the normal c-Abl. Abl is autophosphorylated on tyrosine(s). Applications: Suitable for use in Kinase assay. Other applications not tested. Recommended Dilution: Kinase Assay: This lot at 50uM, was successfully phosphorylated using Abl, active. Assay background was subtracted from the actual counts. Representative results from a previous lot are shown at right. This peptide may also be used as a substrate for Abl (T315I), active and Abl, active, mouse. Optimal dilutions to be determined by the researcher. Storage and Stability: Lyophilized powder may be stored at 4°C for short-term only. Stable for 12 months at -20°C. Reconstitute to nominal volume (see reconstitution instructions for peptides) and store at -20°C. For maximum recovery of product, centrifuge the original vial prior to removing the cap. Further dilutions can be made in assay buffer. |
Source: Synthetic peptide Purity: ~90% determined by HPLC and mass spectroscopy. Concentration: ~1mg/ml Form: Supplied as a lyophilized powder. Important Note: This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological. |
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1. Songyang, Z., et al., Nature 373: 536-539, 1995. General References: 1. Reddy, P.E. et al. (1983) Proc. Natl. Acad. Sci. USA, 80, 3623-3627. 2. Foulkes, J.G. et al. (1985) J. Biol. Chem., 260, 8070-8077. 3. Oppi, C. et al. (1987) Proc. Natl. Acad. Sci. USA, 84, 8200-8204.
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