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Neuroglobin Human E. coli

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:E. coli
  • Other names:NGB
  • Species:Human
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Cat. No. Size Price


RD172043100-B 0.1 mg
PubMed Product Details
Technical Data

Type

Recombinant protein

Description

Total 161 AA. MW: 18 kDa (calculated). UniProtKB acc.no. Q9NPG2 (Met1-Glu151). N-terminal his-tag (10 extra AA). Protein identity confirmed by LC-MS/MS.

Amino Acid Sequence

MKHHHHHHASMERPEPELIRQSWRAVSRSPLEHGTVLFARLFALEPDLLPLFQYNCRQFSSPEDCLSSPEFLDHIRKVMLVIDAAVTNVEDLSSLEEYLASLGRKHRAVGVKLSSFSTVGESLLYMLEKCLGPAFTPATRAAWSQLYGAVVQAMSRGWDGE

Source

E. coli

Purity

Purity as determined by densitometric image analysis: > 90%

SDS-PAGE Gel

14 % SDS-PAGE separation of Human Neuroglobin:
1. M.W. marker – 14, 21, 31, 45, 66, 97 kDa
2. Reduced and boiled sample, 2.5 μg/lane
3. Non-reduced and non-boiled sample, 2.5 μg/lane

Endotoxin

< 1.0 EU/μg

Formulation

Filtered (0.4 μm) and lyophilized from 0.5 mg/ml solution in phosphate buffered saline.

Reconstitution

Add 200 µl of deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Filter sterilize your culture media/working solutions containing this non-sterile product before using in cell culture.

Applications

Western blotting, ELISA

Shipping

At ambient temperature. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Store the lyophilized protein at –80 °C. Lyophilized protein remains stable until the expiry date when stored at –80 °C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80 °C for long term storage. Reconstituted protein can be stored at 4 °C for a week.

Quality Control Test

BCA to determine quantity of the protein.

SDS PAGE to determine purity of the protein.

LAL to determine quantity of endotoxin.

Note

This product is intended for research use only.

Summary

Research topic

Neural tissue markers

Summary

Neuroglobin, 151 amino acid reside protein, mainly expressed in vertebrate brain and retina, is a recently identified member of the globin superfamily. Augmenting O(2) supply, neuroglobin promotes survival of neurons upon hypoxic injury, potentially limiting brain damage. Moreover, neuroglobin may be a novel oxidative stress-responsive sensor for signal transduction in the brain. Neuroglobin expression is increased by neuronal hypoxia in vitro and focal cerebral ischemia in vivo, and neuronal survival after hypoxia is reduced by inhibiting neuroglobin expression with an antisense oligodeoxynucle­otide and enhanced by neuroglobin overexpression

Summary References (5)

References to Neuroglobin

  • Garry DJ, Mammen PP. Neuroprotection and the role of neuroglobin. Lancet. 2003 Aug 2;362 (9381):342-3
  • Mammen PP, Shelton JM, Goetsch SC, Williams SC, Richardson JA, Garry MG, Garry DJ. Neuroglobin, a novel member of the globin family, is expressed in focal regions of the brain. J Histochem Cytochem. 2002 Dec;50 (12):1591-8
  • Pesce A, Dewilde S, Nardini M, Moens L, Ascenzi P, Hankeln T, Burmester T, Bolognesi M. Human brain neuroglobin structure reveals a distinct mode of controlling oxygen affinity. Structure. 2003 Sep;11 (9):1087-95
  • Sun Y, Jin K, Mao XO, Zhu Y, Greenberg DA. Neuroglobin is up-regulated by and protects neurons from hypoxic-ischemic injury. Proc Natl Acad Sci U S A. 2001 Dec 18;98 (26):15306-11
  • Sun Y, Jin K, Peel A, Mao XO, Xie L, Greenberg DA. Neuroglobin protects the brain from experimental stroke in vivo. Proc Natl Acad Sci U S A. 2003 Mar 18;100 (6):3497-500
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