Interleukin 7, Recombinant, Human (IL-7)

Recombinant Human IL-7 is a single, non-glycosylated polypeptide chain containing 172 amino acids and having a molecular mass of 17412 Dalton. \n\nSequence:\nThe sequence of the first five N-terminal amino acids was determined and was found to be Met-Asp-Cys-Asp-Ile. \n\nDimers and Aggregates:\n(same/less than) 1% as determined by silver-stained SDS-PAGE gel analysis. \n\nBiological Activity:\nrHuIL-7 is fully biologically active when compared to standard. The ED50 as determined by the dose-dependent stimulation of murine IXN/2B cells is less then 0.5ng/ml, corresponding to a Specific Activity of 2 x 10e6 IU/mg. \n\nEndotoxin:\n(same/less than) 0.1ng/ug (IEU/ug) of rHuIL-7. \n\nProtein Content:\nProtein quantitation was carried out by two independent methods: \n1. UV spectroscopy at 280 nm using the absorbency value of 0.418 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the PC GENE computer analysis program of protein sequences (IntelliGenetics). \n2. Analysis by RP-HPLC, using a standard solution of IL-7 as a Reference Standard.\n\nReconstitution:\nReconstitute the lyophilized rHuIL-7 in sterile ddH2O not less than 100ug/ml, which can then be further diluted to other aqueous solutions. \n\nStorage and Stability:\nLyophilized powder may be stored at 4 degrees C for short-term only. Reconstitute to nominal volume by adding sterile dH2O and store at -20 degrees C. Reconstituted product is stable for 12 months at -20 degrees C. For maximum recovery of product, centrifuge the original vial prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

I8429-10A

Size

2ug

Form

Supplied as a lyophilized powder. No additives.

Purity

(same/more than) 98% by RP-HPLC, FPLC, or reducing/non-reducing SDS-PAGE Silver Stain. Chromatographically purified.

References

1. Disulfide bond assignment in human interleukin-7 by matrix-assisted laser desorption/ionization mass spectroscopy and site-directed cysteine to serine mutational analysis. Cosenza L, Sweeney E, J Biol Chem 1997 Dec 26;272(52):32995-3000 2. Homology modeling study of the human interleukin-7 receptor complex. Kroemer RT, Richards WG, Protein Eng 1996 Dec;9(12):1135-42 3. Quantitative and cell-cycle differences in progenitor cells mobilized by recombinant human interleukin-7 and recombinant human granulocyte colony-stimulating factor. Grzegorzewski KJ, Komschlies KL, Ruscetti FW, Blood 1996 Dec 1;88(11):4139-48 4. Prediction of the three-dimensional structure of human interleukin-7 by homology modeling. Kroemer RT, Doughty SW, Richards WG, Protein Eng 1996 Jun;9(6):493-8 5. Mobilization of long-term reconstituting hematopoietic stem cells in mice by recombinant human interleukin 7. Grzegorzewski KJ, Komschlies KL, Ruscetti FW, J Exp Med 1995 Jan 1;181(1):369-74 6. Consequences of stable transduction and antigen-inducible expression of the human interleukin-7 gene on tetanus-toxoid-specific T cells. Kim JH, Ratto S, Mosca JD, St Louis D, Hum Gene Ther 1994 Dec;5(12):1457-66.