Thermo Fisher Scientific Human IGF-II, Animal-Free Recombinant Protein, PeproTech

Applications

Tested Dilution

Publications

Functional Assay (Functional)

Assay-dependent

-

Product Specifications

Species

Human

Expression System

E. coli

Amino acid sequence

AYRPSETLCG GELVDTLQFV CGDRGFYFSR PASRVSRRSR GIVEECCFRS CDLALLETYC ATPAKSE

Molecular weight

7.5 kDa

Class

Recombinant

Type

Protein

Purity

≥ 98% by SDS-PAGE gel and HPLC analyses.

Endotoxin concentration

<0.1 EU/µg

Activity

Determined by its ability to stimulate the proliferation of mouse FDC-P1 cells. The expected ED50 is ≤ 2.0 ng/ml, corresponding to a specific activity of ≥ 5 x 10^5 units/mg.

Conjugate

Unconjugated Unconjugated Unconjugated

Form

Lyophilized

Purification

purified

Contains

no preservative

Storage conditions

-20°C

Shipping conditions

Ambient

Product Specific Information

Recombinant Human IGF-I and IGF-II are globular proteins containing 70 and 67 amino acids, respectively, and 3 intra-molecular disulfide bonds. The calculated molecular weight of Recombinant Human IGF-II is 7.5 kDa.

This product is shipped at ambient temperature. For storage, handling and reconstitution information, please see the lot-specific Certificate of Analysis

Target Information

The IGFs are mitogenic, polypeptide growth factors that stimulate the proliferation and survival of various cell types, including muscle, bone, and cartilage tissue in vitro. IGFs are predominantly produced by the liver, although a variety of tissues produce the IGFs at distinctive times. The IGFs belong to the Insulin gene family, which also contains insulin and relaxin. The IGFs are similar to insulin by structure and function, but have a much higher growth-promoting activity than insulin. IGF-II expression is influenced by placenta lactogen, while IGF-I expression is regulated by growth hormone. Both IGF-I and IGF-II signal through the tyrosine kinase type I receptor (IGF-IR), but IGF-II can also signal through the IGF-II/Mannose-6-phosphate receptor. Mature IGFs are generated by proteolytic processing of inactive precursor proteins, which contain N-terminal and C-terminal propeptide regions.

For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.