NBP1-46102-5-5 NT3 Protein

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5 µg / €340.00

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NT3 Protein


Product Description for NT3 Protein

NT3 Protein.
Presentation: Purified

Properties for NT3 Protein

Product Category Proteins & Growth Factors
Quantity 5 µg
Presentation Purified
Reactivity Hu
Molecular weight 29.3 kDa
Species (Protein) Human
Shipping to Not USA/Canada
PDF datasheet View Datasheet
Manufacturer Novus Biologicals Inc.

Datasheet Extract

Swiss Prot Num:
Background Neurotrophin-3 (NT-3), also known as nerve growth factor-2 (NGF2) or hippocampus-derived neurotrophic factor (HDNF), is a 257 amino acid precursor protein with a secretory signal sequence of 16 amino acids, a pro-peptide of 122 amino acids and a mature protein of 119 amino acids. NT-3 is found in neurons of the central nervous system and is secreted by many human gliomas. NT-3 is also expressed in muscles and its expression is downregulated in denervated muscles. NT-3 selectively supports the survival of certain neuronal cell populations, for example, cultured embryonic rat spinal motor neurons, enhances axon sprouting following adult spinal cord lesions and is involved in the regulation of developing neuromuscular synapses. NT-3 is a useful growth factor, differentiation factor and survival factor for cultured stem cells e.g. neural stem cells, cardiomyocytes and embryonic stem cells as well as various types of differentiated neural cells such as oligodendrocytes. NT-3 acts as a mitogen for cells of the neural crest in serum-free media. The biological activities of NT-3 are mediated by receptors belonging to the Trk family of receptors with intrinsic tyrosine-specific protein kinase activity. NT-3 binds to TrkA, TrkB and TrkC, the first two of which are the high-affinity receptors for NGF and BDNF, respectively. NT-3 also binds to the low affinity nerve growth factor receptor (LAN R). This is a HCX protein. HCX Expression System Details HCX proteins mimic the proteins in the human body because they are expressed from human, rather than animal, insect or bacterial cells. This process gives them human post-translational modifications. Recombinant DNA techniques allow a human protein with the correct amino acid sequence to be expressed in a non-human cell line. However, non-human cells lack the appropriate cellular machinery, such as specific glycosyltransferases, necessary to produce the correct human post-translational modifications of a protein. An extreme example is seen in E. coli cells, which produce recombinant proteins with no glycosylation, as the above figure illustrates. Rodent and yeast cells are able to glycosylate proteins, but they are still different from glycosylation in human cells. Expression System Resultant Proteins Human (e.g. K562, HEK293) Correct amino acid sequence Human post-translational modifications Rodent (e.g. CHO, NSO) Correct amino acid sequence Some natural glycosylation - not human-like Yeast (e.g. Pichia) Correct amino acid sequence Some natural glycosylation - not human-like E.Coli Correct amino acid sequence No PTMs Although there have been significant attempts to make non-human cell derived cytokines more human-like, there is a growing awareness that in many instances, particularly in therapeutics, cytokines should mimic those found in the body as closely as possible.
Concentration Lyoph mg/ml
General Readings Chao MV, Rajagopal R, and Lee FS (2006) Clin. Sci (Lond) 110(2): 167-173.
Storage Store at -80C. Avoid freeze-thaw cycles.
Buffer System:
Lyophilized. Reconstitute in 0.5 ml sterile PBS the solution will contain 1% human serum albumin and 10% trehalose.
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