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Recombinant Human Beta-NGF

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Product Source Size Cat. No. Price
Recombinant Human Beta-NGF CHO cells20 µg Z101545 $600.00
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Data Sheet
Print Version
Alternative Names NGF, NGFB
Recombinant Human NGF
Description NGF is mainly responsible for the survival and the differentiation and the functional activities of sensory and sympathetic neurons in the peripheral nervous system. It also plays an important role in the development and functional activities of cholinergic neurons in the central nervous system. Since NGF is synthesized also in non-neuronal tissues it may have a much wider spectrum of biological activities than thought previously. NGF stimulates chemotactic migration of human polymorphonuclear leukocytes in vitro. NGF stimulates the growth and differentiation of B cells and the growth of T cells and of some tumor cell types. NGF inhibits immunoglobulin production by various human plasma cell. The cytokines IL-1, IL-6, and bFGF are potent inducers of NGF. NGF induces the synthesis of IL-1 in pheochromocytoma cells which in turn acts as a growth factor for glial cells and induces the synthesis of NGF following nerve injuries. In thymic stromal cells NGF induces the synthesis of IL-6. NGF induces the synthesis of the fos oncogene and the myc oncogene and also influences the expression of EGF. One receptor that is responsible for mediating most of the activities of NGF is expressed preferentially in neuronal tissues. This glycoprotein of 140 kDa is the product of the trk gene. It possesses an intrinsic tyrosine-specific protein kinase in its intracellular domain.
Gene Symbol NGF
Gene ID 4803
Accession No. P01138
Source CHO cells
Appearance Lyophilized Powder
Molecular Weight 27.0 kDa
Endotoxin Level <1.0 EU/μg of recombinant protein as determined by the LAL method.
Purity >95% as determined by SDS-PAGE
Bioactivity The ED(50) was determined by the determined by its ability to proliferate TF-1 cells and was found to be in the range of 0.5 ng/mL.
Formulation NGF-beta was lyophilized from a 0.2 μm filtered solution in 20 mM sodium acetate, 150 mM NaCl, pH 5.5.
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.