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GST Protein (AA 1-218)

This Recombinant GST protein is produced in Escherichia coli (E. coli).
Catalog No. ABIN6388215

Quick Overview for GST Protein (AA 1-218) (ABIN6388215)

Target

See all GST Proteins
GST (Glutathione S Transferase (GST))

Protein Type

Recombinant

Biological Activity

Active

Origin

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Schistosoma japonicum

Source

  • 9
  • 8
Escherichia coli (E. coli)

Application

SDS-PAGE (SDS), Enzyme Activity Assay (EAA)

Purity

> 90% by SDS-PAGE
  • Protein Characteristics

    AA 1-218

    Sequence

    MSPILGYWKI KGLVQPTRLL LEYLEEKYEE HLYERDEGDK WRNKKFELGL EFPNLPYYID GDVKLTQSMA IIRYIADKHN MLGGCPKERA EISMLEGAVL DIRYGVSRIA YSKDFETLKV DFLSKLPEML KMFEDRLCHK TYLNGDHVTH PDFMLYDALD VVLYMDPMCL DAFPKLVCFK KRIEAIPQID KYLKSSKYIA WPLQGWQATF GGGDHPPK

    Endotoxin Level

    < 1 EU per 1ug of protein (determined by LAL method)

    Biological Activity Comment

    Specific activity is > 30unit/mg, and is defined as the amount of enzyme that conjugate 1.0 umole of 1-chloro-2,4-dinitrobenzene (CDNB) with reduced glutathione per minute at pH 6.5 at 25C.
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  • Application Notes

    Optimal working dilution should be determined by the investigator.

    Comment

    Bioactivity Validated

    Restrictions

    For Research Use only
  • Format

    Liquid

    Concentration

    1 mg/mL

    Buffer

    Liquid. In Phosphate Buffer Saline containing 10 % glycerol

    Storage

    4 °C,-20 °C,-80 °C

    Storage Comment

    Can be stored at +2°C to +8°C for 1 week. For long term storage, aliquot and store at -20°C to -80°C. Avoid repeated freezing and thawing cycles.
  • Target

    GST (Glutathione S Transferase (GST))

    Alternative Name

    Glutathione S-transferase/GST

    Background

    GST, also known as, Glutathione S-transferase, represents a major group of detoxification enzymes. GST acts by catalyzing the reaction of glutathione with an acceptor molecule to form an S-substituted glutathione (S=sulfur). The reactions utilizing glutathione contribute the transformation of a wide range of compounds, including carcinogens, therapeutic drugs, and products of oxidative stress. As well as its enzymatic activities, GST may also bind toxins and function as transport protein. Because of this, an early term for GSTs was ligandin. GST was originally separated from Schistosomajaponicum but currently isolated from recombinant E. coli source. Recombinant Schistosoma japonicum GST was expressed in E. coli and purified by conventional chromatography techniques.

    Molecular Weight

    25.4 kDa (218aa)

    UniProt

    P08515
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