GST-tag Polyclonal Antibody | anti-GST antibody

Anti-GST-tag Rabbit pAb

Cat. Num. AAA475560

• Applications: Western Blot
• Purity: Affinity Purified
• Synonyms: GST-tag; Polyclonal Antibody; Anti-GST-tag Rabbit pAb; Glutathione S Transferase; Glutathione S transferase Mu 1; Glutathione S-transferase class-mu 26 kDa isozyme; GST 26; GST; GST class mu 1; GST1; GSTM1 1; GSTM1a 1a; GSTM1b 1b; GTH4; GTM1; H B; HB subunit 4; MGC26563; MU 1; MU; SJ26 antigen; SjGST; anti-GST antibody

• Host: Rabbit; Source: Schistosoma japonicum
• Clonality: Polyclonal
• Isotype: IgG
• Purity/Purification: Affinity Purified
• Form/Format: Purified Rabbit polyclonal in PBS (pH 7.4) containing with 0.02% sodium azide and 50% glycerol.
• Concentration: 0.7mg/ml (varies by lot)

• Applicable Applications for anti-GST antibody: Western Blot (WB)
• Application Notes: WB: 1:10000
• Immunogen: Purified recombinant Escherichia coli BL21 (DE3) GST protein fragments expressed in E Coli.
• Sensitivity: Transfected Only.
• Subunit Structure: Protein sequence and structure are important classification methods for GSTs:while classes from the cytosolic superfamily of GSTs possess more than 40% sequence homology, those from other classes may have less than 25%. Cytosolic GSTs are divided into 13 classes based upon their structure:alpha, beta, delta, epsilon, zeta, theta, mu, nu, pi, sigma, tau, phi, and omega.Mitochondrial GSTs are in class kappa.The MAPEG superfamily of microsomal GSTs consists of subgroups designated I-IV, between which amino acid sequences share less than 20% identity.The glutathione binding site, or "G-site, " is located in the thioredoxin-like domain of both cytosolic and mitochondrial GSTs.The region containing the greatest amount of variability between the assorted classes is that of helix alpha2, where one of three different amino acid residues interacts with the glycine residue of glutathione.Two subgroups of cytosolic GSTs have been characterized based upon their interaction with glutathione:the Y-GST group, which uses a tyrosine residue to activate glutathione, and the S/C-GST, which instead use serine or cysteine residues.The porcine pi-class enzyme pGTSP1-1 was the first GST to have its structure determined, and it is representative of other members of the cytosolic GST superfamily, which contain a thioredoxin-like N-terminus domain as well as a C-terminus domain consisting of alpha helices.Mammalian cytosolic GSTs are dimeric, both subunits being from the same class of GSTs, although not necessarily identical.The monomers are in the range of 22-30 kDa.They are active over a wide variety of substrates with considerable overlap.
• Subcellular Location: Protein sequence and structure are important classification methods for GSTs:while classes from the cytosolic superfamily of GSTs possess more than 40% sequence homology, those from other classes may have less than 25%. Cytosolic GSTs are divided into 13 c

Western Blot (WB)

(Western blot detection of GST in CHO-K1 transfected with GST cell lysate and GST recombinant protein fragments, purified recombinant human GST-Lin28B & GST-Lin28A protein fragments expressed in E Coli, using GST rabbit pAb (1:10000 diluted).)

Related Product Information for anti-GST antibody

Entrez Summary: The glutathione S-transferase (GST, previously known as ligandins) family of enzymes are composed of many cytosolic, mitochondrial, and microsomal (now designated as MAPEG) proteins.GSTs are present in eukaryotes and in prokaryotes, where they catalyze a variety of reactions and accept endogenous and xenobiotic substrates.Members of the GST superfamily are extremely diverse in amino acid sequence, and a large fraction of the sequences deposited in public databases are of unknown function.The Enzyme Function Initiative (EFI) is using GSTs as a model superfamily to identify new GST functions.GSTs can constitute up to 10% of cytosolic protein in some mammalian organs.GSTs catalyse the conjugation of reduced glutathione — via a sulfhydryl group — to electrophilic centers on a wide variety of substrates in order to make the compounds more soluble.This activity detoxifies endogenous compounds such as peroxidised lipids, as well as breakdown of xenobiotics.GSTs may also bind toxins and function as transport proteins, which gave rise to the early term for GSTs of "ligandin".The mammalian GST super-family consists of cytosolic dimeric isoenzymes of 45-55 kDa size that have been assigned to at least six classes:Alpha, Mu, Pi, Theta, Zeta and Omega.Most mammalian isoenzymes have affinity for the substrate 1-chloro-2, 4-dinitrobenzene (CDNB), and spectrophotometric assays utilising this substrate are commonly used to report GST activity.However, some endogenous compounds, e.g., bilirubin, can inhibit the activity of GSTs.In mammals, GST isoforms have cell specific distributions (e.g., alpha GST in hepatocytes and pi GST in the biliary tract of the human liver).

NCBI and Uniprot Product Information

• NCBI GI #: 251785093
• NCBI GeneID: 8113787
• NCBI Accession #: YP_002999397
• NCBI GenBank Nucleotide #: NC_012892.2
• Molecular Weight: 26
• NCBI Official Full Name: glutathione S-transferase
• Protein Family: Glutathione S-transferase