Anti-S. Japonicum Glutathione S-transferase/GST antibody [1E5] (STJA0041495)
SPECIFICATIONS
ClonalityMonoclonal
HostMouse
ConjugationUnconjugated
IsotypeIgG2bk
ImmunogenRecombinant Schistosoma japonicum Glutathione S transferase (GST) purified from E. coli
General Information
| Short Description | Mouse monoclonal anti-S. Japonicum Glutathione S-transferase/GST for use in ELISA, WB, ICC and IF in GST samples. Datasheet included with dilution recommendations, and related reagents. |
| Applications | ELISA/WB/ICC/IF |
| Host | Mouse |
| Reactivity | GST |
| Note | STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Product Properties
| Clonality | Monoclonal |
| Clone ID | 1E5 |
| Isotype | IgG2bk |
| Conjugation | Unconjugated |
| Concentration | 1 mg/mL |
| Purification | By protein-G affinity chromatography |
| Formulation | Liquid in phosphate-Buffered Saline (pH 7.4) with 0.02% Sodium Azide, 10% Glycerol |
| Storage Instruction | For short term storage, keep at +2C to +8C for up to 1 week. For long term storage, aliquot and store at-20C, and avoid repeat freeze-thaw cycles. |
Target Information
| Accession Number | AAB59203.1 |
| Immunogen | Recombinant Schistosoma japonicum Glutathione S transferase (GST) purified from E. coli |
Additional Info
| Background | Glutathione S transferases (GSTs) are a family of enzymes that play an important role in detoxification by catalyzing the conjugation of many hydrophobic and electrophilic compounds with reduced glutathione. GST proteins can be purified by immobilized glutathione affinity chromatography. Many recombinant proteins have been engineered with GST tags to facilitate the detection, isolation and purification of these proteins. Monoclonal antibody reacting specifically with GST may be useful in various immunotechnique, to identify the expression of a GST fusion protein in bacteria, bacterial lysates or cells and tissues transfected with a GST fusion protein expressing vectors. |
Information sourced from Uniprot.org