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Overview
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HMGB1 15N labelled for Mass Spectrometry and NMR, LPS-Free
Full length HMGB1 for Mass Spectrometry is the 25 kDa HMGB1 protein uniformly labelled with isotope 15N.
This protein is suitable for mass spectrometry and NMR studies.
This product corresponds to the human sequence and is produced in E.coli using a media in which the only source of nitrogen come from 15NH4Cl.
The Fully reduced HMGB1 we provide is the natural protein, with no tags or additional amino acids.
It has the sequence:
["MGKGDPKKPR GKMSSYAFFV QTCREEHKKK HPDASVNFSE FSKKCSERWK TMSAKEKGKF EDMAKADKAR YEREMKTYIP PKGETKKKFK DPNAPKRPPS AFFLFCSEYR PKIKGEHPGL SIGDVAKKLG EMWNNTAADD KQPYEKKAAK LKEKYEKDIA AYRAKGKPDA AKKGVVKAEK SKKKKEEEDD EEDEEDEEEE EEEEDEDEEE DDDDE" ]
Molecular Mass: HMGB1 consists of 215 amino acid residues and has a calculated molecular mass of approximately 24.8 kDa. It migrates at a position of approximately 30 kD in SDS-PAGE gels, possibly because of the unusual number of positively charged amino acids it contains.
Structure: HMGB1 consists of two fairly rigid, L-shaped DNA-binding domains, each referred to as a 'HMG box', and an unstructured tail that ends with 30 consecutive negatively charged amino acids.
Purity: The purified protein is >95% homogeneous (electrophoresis ). It contains no nucleic acids.
Endotoxin Level: The purified protein is free from LPS (Pierce™ Chromogenic Endotoxin Quant Kit, <0.1 EU/mL). The product contains <0.006% v/v of Triton X-114 due to LPS removal procedure. The remaining traces of Triton X-114 can be removed upon request.
Buffer & Reconstitution: the lyophilized protein once reconstituted with distilled water will be dissolved in a solution containing 50 mM HEPES pH 7.9, 500 mM NaCl, 0.5 mM DTT.
Storage: the protein is shipped lyophilized. Once resuspended can be stored frozen at -20°C. To avoid cysteine oxidation, DTT 0.5mM is added during protein purification.
This product is intended for research only, and cannot be used on humans.Please contact us at for specific academic pricing.
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- Properties
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Overview