407251
Insulin-Like Growth Factor-I, Human, Recombinant, E. coli, Animal-Free
别名:
hIGF-I
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关于此项目
UNSPSC Code:
12352202
Assay:
≥98% (SDS-PAGE and HPLC)
Form:
lyophilized
Impurities:
≤0.1 ng/μg Endotoxins
assay
≥98% (SDS-PAGE and HPLC)
form
lyophilized
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
impurities
≤0.1 ng/μg Endotoxins
shipped in
wet ice
storage temp.
−20°C
Quality Level
General description
Full-length, recombinant, human insulin-like growth factor I (IGFI) expressed in E. coli. The IGFI growth factor regulates proliferation and survival signals through the AKT pathway. This animal free growth hormone is useful in the study of cell proliferation and survival signals.
Biochem/physiol Actions
ED ₅₀: ≤1 ng/ml as determined by a cell proliferation assay using FDC-P1 cells; this corresponds to a specific ≥1 x 10⁶ units/mg.
Preparation Note
Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C. Avoid freeze/thaw cycles of solutions.
Reconstitute with H₂O to a final concentration of 0.1-1 mg/ml. Further dilute with physiological buffer prior to use.
Other Notes
Stabnov, L., et al. 2002. Bone30, 909.
Devireddy, L.R., et al. 2001. Science 293, 829.
Chen, C.W., and Ray, D. 1995. Carcinogenesis 16, 1339.
Devireddy, L.R., et al. 2001. Science 293, 829.
Chen, C.W., and Ray, D. 1995. Carcinogenesis 16, 1339.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Toxicity: Standard Handling (A)
存储类别
11 - Combustible Solids
wgk
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Longxing Cao et al.
Nature, 605(7910), 551-560 (2022-03-26)
The design of proteins that bind to a specific site on the surface of a target protein using no information other than the three-dimensional structure of the target remains a challenge1-5. Here we describe a general solution to this problem
Blaz Lupse et al.
Cell reports, 36(5), 109490-109490 (2021-08-05)
Pancreatic β-cell failure is the key pathogenic element of the complex metabolic deterioration in type 2 diabetes (T2D); its underlying pathomechanism is still elusive. Here, we identify pleckstrin homology domain leucine-rich repeat protein phosphatases 1 and 2 (PHLPP1/2) as phosphatases
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