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Recombinant Human IGFBP3

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Product Source Size Cat. No. Price
Recombinant Human IGFBP3 E. coli25 µg Z100375 $70.00
100 µg Z100377 $210.00
1.0 mg Z100379 $1,890.00
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Data Sheet
Print Version
Alternative Names IGF-binding protein 3, IGF-BP3, IBP-3
Recombinant Human Insulin-like Growth Factor Binding Protein 3 (IGFBP3)
Description IGFBPs are synthesized in the liver and are produced also by various tumor cell lines and cell types. IGFBPs are high affinity binding proteins for IGF. The major fraction of both types of IGF circulating in the blood are bound non- covalently to these carrier proteins. IGF binding proteins modulate IGF activities by increasing their plasma half lives and by inhibiting or promoting the interactions of IGF with receptors on certain target cells. In addition these binding proteins provide a reservoir for IGF in pericellular spaces. Some IGFBPs also have stimulating effects in vitro and some may inhibit the growth of cells. IGFBP1 is found predominantly in the placenta and the amniotic fluid. The predominant sites of IGFBP1 transcription in the human fetal kidney are those with most active differentiation. Elevated serum levels have been observed in patients with Laron-type dwarfism and Growth hormone deficiency. High serum levels of IGFBP1 are found in newborns and it has been suggested that this could be important in protecting them from hypoglycemia.
Gene Symbol IGFBP3
Gene ID 3486
Accession No. P17936
Source E. coli
Appearance Lyophilized Powder
Molecular Weight 28.0 kDa
Endotoxin Level <1.0 EU/μg of recombinant protein as determined by the LAL method.
Purity >95% as determined by SDS-PAGE
Gel Image Click To Enlarge
Bioactivity The ED(50) was determined by the ability to inhibit IGF-I induced proliferation of MCF-7 and was found to be ≤ 0.5 μg/mL.
Formulation Recombinant IGFBP3 was lyophilized from a 0.2 μm filtered PBS solution.
Reconstitution A 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.
Storage The 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 loss of activity. Avoid repeated freeze/thaw cycles.
Usage For research use only. Not for diagnostic or therapeutic use.
Product Documents
Product References
FAQs
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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.