Source:

Escherichia coli.

Molecular Weight:

22.1 kDa, observed by reducing SDS-PAGE.

Purity:

> 95% by SDS-PAGE and HPLC analyses.

Biological activity:

ED50 < 0.5 ng/ml, measured by a cell proliferation assay using Nb2-11 Cells, corresponding to a specific activity of > 2.0× 10ˆ6 units/mg.

AA Sequence:

FPT IPLSRLFDNA MLRAHRLHQL AFDTYQEFEE AYIPKEQKYS FLQNPQTSLC FSESIPTPSN REETQQKSNL ELLRISLLLI QSWLEPVQFL RSVFANSLVY GASDSNVYDL LKDLEEGIQT LMGRLEDGSP RTGQIFKQTY SKFDTNSHND DALLKNYGLL YCFRKDMDKV ETFLRIVQCR SVEGSCGF

Endotoxin:

< 0.2 EU/μg, determined by LAL method.

Formulation:

Lyophilized after extensive dialysis against PBS.

Background:

Growth Hormone (GH) is a member of the somatotropin/prolactin family which play an important role in growth control. The human GH cDNA encodes a 217 amino acid (aa), and the first 26 aa is a signal peptide. By alternative splicing, at least four isoforms of GH have been identified. The major role of GH in stimulating body growth is to stimulate the liver and other tissues to secrete IGF-1. GH stimulates both the differentiation and proliferation of myoblasts, and also stimulates amino acid uptake and protein synthesis in muscle and other tissues.Recombinant human Growth Hormone (rhGH) produced in E.coli is a single non-glycosylated polypeptide chain containing 191 amino acids. A fully biologically active molecule, rhGH has a molecular mass of 22.1 kDa analyzed by reducing SDS-PAGE and is obtained by proprietary chromatographic techniques at GenScript.

Usage:

This material is offered by USA Bioworld biotech for research, laboratory or further evaluation purposes. For research use only.

Physical Appearance:

Sterile Filtered White lyophilized (freeze-dried) powder.

Reconstitution:

Reconstituted in ddH2O at 100 μg/ml.

Storage:

Lyophilized recombinant human Growth Hormone (rhGH) remains stable up to 6 months at -80°C from date of receipt. Upon reconstitution, rhGH should be stable up to 2 weeks at 4°C or up to 3 months at -20°C.