Recombinant Human GH1 (E. coli)



DescriptionThe physiological activity for which growth hormone is best known is the promotion of growth of bone, cartilage, and soft tissues. Detectable levels of growth hormone are found throughout the remainder of adulthood, suggesting other functions in addition to promotion of growth. Growth hormone may be important for the maintenance of lean body mass; most growth-promoting effects of growth hormone are mediated by IGF-1 the synthesis of which is regulated by growth hormone. The biological activities of growth hormone are mediated by receptors belonging to one of the cytokine receptor families. Growth hormone has been shown to be produced by T cells, B cells, and macrophages. In human lymphocytes growth hormone appears to up-regulate its own expression. Growth hormone appears to act as an enhancer of immune responses and is produced in considerable amounts by T helper cells.
FamilySomatotropin/Sclerostin/Serpin Families
AliasesGH, GH-N, Growth hormone 1, Pituitary growth hormone, Somatotropin
Recombinant Human Growth Hormone (GH1)
Gene SymbolGH1
Gene ID2688
Accession NumberP01241
SourceE. coli
SpeciesHuman (H. sapiens)
AppearanceLyophilized Powder
Molecular Weight22 kDa
Endotoxin Level<1.0 EU/µg of recombinant protein as determined by the LAL method.
Purity>95% as determined by SDS-PAGE
FormulationLyophilized from a 0.2 μm filtered in Tris and NaCl (pH 7.5).
FunctionThe ED(50) was determined by the dose-dependent cell proliferation assay using the rat lymphoma, Nb2-11, and was found to be in the range of 0.1 ng/mL.
ReconstitutionA quick spin of the vial followed by reconstitution in distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers.
StorageThe lyophilized protein is stable for at least one year from date of receipt at -70°C. Upon reconstitution, this cytokine can be stored in working aliquots at 2° - 8°C for one month, or at -20°C for six months, with a carrier protein without detectable lo
UsageFor research use only. Not for diagnostic or therapeutic use.

How are endotoxin levels measured?
1. For estimating the endotoxin levels; we use the LAL (Limulus Amebocyte Lysate) method: The lysate from horseshoe crab amebocytes clots in the presence of very low endotoxin. This reaction is the basis of the Limulus amebocyte lysate (LAL) assay which was approved by the FDA in 1970. · Endotoxin is generally measured in Endotoxin Units per milliliter (EU/mL). · For recombinant proteins: EU is reported per microgram of protein. · One EU = 0.1-0.2 ng endotoxin/µg of protein. · At abm, we do the LAL chromogenic assays that can detect down to 0.01 EU/ml.
With regard to the BSA levels in some Growth Factors and Cytokines, can you please provide an explanation as to why they are so high?
The amount of BSA, as part of the formulation of a protein, can vary considerably depending on how much BSA was deemed optimum/necessary for protein stability in combination with /in-lieu of - other possible additives. The aforementioned formulations are somewhat analogous to the “carrier” versions of many formulations from “R and D systems” that have as high as 50 µg of BSA per µg of the recombinant protein product. If, needed or desired, abm scientists can substitute BSA for other stabilizing additives for most formulations.
Are your Escherichia coli sourced growth factors: 1) Human derived materials free? 2) Recombinant proteins free?
Yes, all of abm's growth factors made in Escherichia coli using recombinant technology contain no human derived-products or other recombinant proteins. In the rare cases of BSA presence, this will be mentioned in the product's formulation.

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