HMGB1 15N labelled for Mass Spectrometry and NMR

 320 1800

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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.

Publications:

16th June 2023
HMGB1●CXCL12 : the first fuzzy chemokines heterocomplex reported so far

HMGBiotech Srl participated in a recent study in which, through an integrative structural approach,
molecular details of HMGB1●CXCL12 heterocomplex formation were unveiled.
This dynamic complex is formed equimolarly, contrary to previous assumptions.
Structured and unstructured HMGB1 regions interact with the dimerization surface of CXCL12. This work elucidated how the acidic IDR is involved in HMGB1●CXCL12 complex formation.The findings suggest that interfering with the interactions in the HMGB1●CXCL12 complex could potentially inhibit its detrimental effects in inflammatory conditions. Read the full article about the study…

Mantonico et al. The acidic intrinsically disordered region of the inflammatory mediator HMGB1 mediates fuzzy interactions with chemokine CXCL12. bioRxiv 2023.

Download HMGB1 for Mass Spectrometry Datasheet

Complete Name: High Mobility Group 1https://www.hmgbiotech.eu/wp-content/uploads/2017/12/HMGB1-for-mass-spec11.pdf
Other Names: Amphoterin-1, High mobility group protein 1,HMG-1, SBP-1, high mobility group protein B1, high-mobility group box 1, Amphoterin, HMG1, HMGB1, SBP-1, recombinant HMGB1, 15N labelled, Mass Spectrometry

*The product contains <0.006% v/v of Triton X-114 (upon request it is possible to remove it).

Size

5 µg, 50 µg

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HMGB1 15N labelled for Mass Spectrometry and NMR
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