Recombinant Human NGFR/TNFRSF16/p75NTR Protein

Product Discontinued

Recombinant Human NGFR/TNFRSF16/p75NTR Protein Summary

• Description: A recombinant protein corresponding to amino acids 209 of NGFR.
• Specificity: NGF R (209 aa) - Fc HCX Chimera migrates as a broad band between 65 and 90 kDa in SDS-PAGE due to post-translation modifications, in particular glycosylation. This compares with the unmodified NGFR-Fc Chimera that has a predicted mass of 49.2kDa. NGF R (209 aa) - Fc HCX Chimera has N-linked and O-linked oligosaccharides.
• Preparation Method: A DNA sequence encoding the signal peptide and extracellular domain of human NGF receptor (aa 1-237) was fused to the Fc region of human IgG1 (aa 93-330). The chimeric protein was expressed in modified human 293 cells.
• Protein/Peptide Type: Recombinant Protein
• Gene: NGFR

Applications/Dilutions

• Dilutions:
  • Block/Neutralize
  • Functional
  • SDS-Page
  • Western Blot
• Application Notes: This protein is functionally active and can be used for Blocking and Neutralizing. It can also be used for Western Blot. NGF R (209 aa) - Fc HCX Chimera separates into a number of isoforms with a pI between 4.2 and 5.3 in 2D PAGE due to post-translational modifications, in particular glycosylation. This compares with the unmodified NGF R-Fc Chimera that has a predicted pI of 4.89.

Reactivity Notes

This is a Human protein

Packaging, Storage & Formulations

• Storage: Store at -80C. Avoid freeze-thaw cycles.
• Concentration: LYOPH
• Reconstitution Instructions: Reconstitute with 0.5 ml sterilized PBS containing 1% human serum albumin and 10% trehalose.

Notes

Purity is greater than 95%, as determined by SDS-PAGE and visualized by silver stain.

Alternate Names for Recombinant Human NGFR/TNFRSF16/p75NTR Protein

• CD271 antigen
• CD271
• Gp80-LNGFR
• member 16
• nerve growth factor receptor
• NGF R
• NGF receptor
• NGFR
• p75 ICD
• p75 NTR
• TNFRSF16
• TNFRSF16nerve growth factor receptor (TNFR superfamily, member 16)
• tumor necrosis factor receptor superfamily member 16

Background

Nerve growth factor receptor (NGF R; NGFR) is a low affinity NGF receptor. NGF R binds with equal affinity all neurotrophins including NGF beta, brain derived neurotrophic factor (BDNF) and neurotrophin-3 (NT3) and neurotrophin-5 (NT4/5). The association of NGF R with the other NGF receptors such as TrkA, B and C results in higher affinity ligand binding. Ligand binding to the NGF R can promote either survival or apoptosis of neurons. The effects of neurotrophins exerted through NGF R include conditions such as pain, depression, obesity, nerve regeneration disorders, learning and memory. Additionally, NGF R may play a role in neuronal death that occurs in disorders of the CNS such as Alzheimer's disease.NGF R is a type I membrane protein that is synthesized as a 427 amino acid glycoprotein comprised of a 28 amino acid signal peptide, a 222 amino acid extracellular domain that includes four TNFR-Cys repeats (aa31-aa188), a Ser/Thr rich stalk (aa197-aa248), a 22 amino acid transmembrane region, and a 155 amino acid cytoplasmic domain. NGF R is N-glycosylated and phosphorylated on serine residues, and mass spectroscopic analysis of the NGF R stalk identified 7 sites of O-linked glycosylation that may affect the affinity of neurotrophin binding (see Chapman et al., 1996 J. Neurochem. 66, 1707-1716). NGF R (209 aa) does not contain the aforementioned stalk. In contrast to TrkA, B and C, which contain intracellular tyrosine kinase domains, NGF R lacks intracellular enzymatic activity. However NGF R does contain a type II death domain for binding TNF receptor associated factors (TRAFs) that function in mediating the effects of NGF R signaling. 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. Purified NGF R (209 aa) - Fc HCX Chimera consists of 25-45% carbohydrate by weight.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 3 months from date of receipt.

Bioinformatics

• Gene Symbol: NGFR