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Merck

57600

IL-2 human

≥98% (GE), recombinant, expressed in E. coli, liquid

Synonym(s):

Interleukin-2 human, TCGF, hIL-2, IL-2

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About This Item

CAS Number:
UNSPSC Code:
12352202
NACRES:
NA.32
MDL number:
Biological source:
human
Recombinant:
expressed in E. coli
Form:
liquid
Mol wt:
Mr ~15500
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Product Name

Interleukin-2 human, recombinant, expressed in E. coli, ~10000 U/mL

biological source

human

Quality Level

recombinant

expressed in E. coli

form

liquid

mol wt

Mr ~15500

packaging

vial of 1 mL

concentration

~10000 U/mL

color

colorless

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... IL2(3558)

Biochem/physiol Actions

Promotes the growth of IL-2 dependent lymphocytes. Amino acid sequence of IL-2.

Packaging

One vial contains 10′000 Units

Physical form

Clear; colorless solution in Dulbecco-PBS; containing 1 mg BSA/mL.

Other Notes

1 U corresponds to the unit activity in the colorimetric MTT-assay with CTLL-2 cells.
Sales restrictions may apply.

Disclaimer

Stable at −20 °C; prepare appropriate aliquots and avoid repeated freezing and thawing, since aggregation may occur resulting in apparent loss of activity.


Storage Class

10 - Combustible liquids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable



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S Gillis et al.
Journal of immunology (Baltimore, Md. : 1950), 120(6), 2027-2032 (1978-06-01)
Several soluble factors have recently been associated with the proliferation and differentiation of thymus-derived lymphocytes. One of these factors present in medium conditioned by T cell mitogen-stimulated lymphocytes has the ability to promote the long-term culture of normal and antigen-specific
Interleukin 2.
K A Smith
Annual review of immunology, 2, 319-333 (1984-01-01)
R J Robb et al.
Proceedings of the National Academy of Sciences of the United States of America, 81(20), 6486-6490 (1984-10-01)
Human interleukin 2 was separated into multiple molecular forms by selective immunoaffinity chromatography and chromatofocusing. For the most part, this heterogeneity was attributed to variations in glycosylation of the threonine residue in position 3 of the polypeptide chain. The various