Analytical Data
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Gene name
Ngf
- Application
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Alternative Names
Ngf；NGFB；Beta-nerve growth factor
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P01138
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Expression Region
122-241aa
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AA Sequence
SSSHPIFHRG EFSVCDSVSV WVGDKTTATD IKGKEVMVLG EVNINNSVFK QYFFETKCRD PNPVDSGCRG IDSKHWNSYC TTTHTFVKAL TMDGKQAAWR FIRIDTACVC VLSRKAVRRA SSSHPIFHRG EFSVCDSVSV WVGDKTTATD IKGKEVMVLG EVNINNSVFK QYFFETKCRD PNPVDSGCRG IDSKHWNSYC TTTHTFVKAL TMDGKQAAWR FIRIDTACVC VLSRKAVRRA
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Molecular Weight
27 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Nerve Growth Factor (NGF) is a neurotrophic factor crucial for the growth, maintenance, and survival of certain target neurons, primarily in the peripheral nervous system. The discovery of NGF in the 1950s marked a significant advancement in neurobiology, as it was the first protein identified to promote neuron survival and differentiation, earning the Nobel Prize in Physiology or Medicine in 1986. Subsequent research has demonstrated NGF's critical role not only in neurodevelopment but also in neurodegeneration and various neurological disorders, including Alzheimer's disease and chronic pain conditions. The recombinant production of NGF has enabled scientists to study its structure-function relationships and therapeutic potential in a controlled manner. By utilizing recombinant DNA technology, researchers can produce NGF in vitro, allowing for detailed investigations into its signaling pathways and interaction with its receptor, TrkA. Furthermore, understanding the mechanisms of NGF action at the molecular level has led to potential therapeutic avenues for conditions characterized by nerve damage or dysfunction. The ongoing study of NGF, particularly in recombinant form, continues to provide insights that may lead to novel treatments for a range of neurological challenges, emphasizing its importance in both fundamental research and clinical applications in neuroscience.
