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Dima Biotech

PME30027

Human LR3-IGF-1 Protein

Human LR3-IGF-1 Protein

$100.00 USD
$100.00 USD
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Size
Target
Uniprot ID
PRODUCT DATA
TARGET

SYNONYMS

Insulin-Like Growth Factor I;IGF-I;Mechano Growth Factor;MGF;Somatomedin-C;IGF1;IBP1
DESCRIPTION

Recombinant Human LR3 Insulin-Like Growth Factor-I is produced by our E.coli expression system and the target gene encoding Gly49-Ala118 is expressed.
DELIVERY

In Stock
UNIPROT ID

P05019
EXPRESSION HOST

E.coli
TAG
MOLECULAR CHARACTERIZATION

Not available
MOLECULAR WEIGHT

9.1 KDa
PURITY

Greater than 95% as determined by reducing SDS-PAGE.
FORMULATION & RECONSTITUTION

Lyophilized from a 0.2 μm filtered solution of 20mM NaAc-HAc, 4% Mannitol, pH 4.5.
STORAGE & SHIPPING

Store at -20°C to -80°C for 12 months in lyophilized form. After reconstitution, if not intended for use within a month, aliquot and store at -80°C (Avoid repeated freezing and thawing). Lyophilized proteins are shipped at ambient temperature.
BACKGROUND

Insulin-like growth factor I (IGF1) belongs to the family of insulin-like growth factors that are structurally homologous to proinsulin. Mature IGFs are generated by proteolytic processing of inactive precursor proteins, which contains the N- and C-terminal propeptide regions. Mature human IGF-I consisting of 70 amino acids has 94% identity with mouse IGF-I and exhibits cross-species activity. IGF-1 binds IGF-IR, IGF-IIR, and the insulin receptor and plays a key role in cell cycle progression, cell proliferation and tumor progression. IGF-1 expression is regulated by growth hormone. R3 IGF-1 is an 83 amino acid analog of IGF-1 comprising the complete human IGF-1 sequence with the substitution of an Arg (R) for the Glu(E) at position three, hence R3, and a 13 amino acid extension peptide at the N terminus. R3 IGF-1 has been produced with the purpose of increasing biological activity. R3 IGF-1 is significantly more potent than human IGF-I in vitro.
USAGE

Research use only
IMAGES

sp-PME30027 C023 P05019 SDS PAGE 0

Figure 1. Greater than 95% as determined by reducing SDS-PAGE.

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