You Searched For: N-Carbobenzoxy-L-glutamine

Catalog Number: (10491-246)

Supplier: Bioss

Description: Mammalian protein farnesyl transferases are heterodimeric proteins containing two nonidentical Alpha and beta subunits that attach farnesyl residues to a cysteine at the fourth position from the COOH terminus of several proteins, including nuclear lamins and p21Ras proteins. The natural substrates contain the Cys-A-A-Xaa recognition sequence, where the A residues are aliphatic and Xaa represents methionine, serine, glutamine or cysteine. The purified farnesyl transferase is an a-b heterodimer. The beta subunit, which is known as FT beta, CAAX farnesyltransferase subunit beta, or Ras proteins prenyltransferase subunit beta, is a 437 amino acid protein that contains five PFTB repeats and binds the peptide substrate. The Alpha subunit is suspected to participate in formation of a stable complex with the substrate farnesyl pyrophosphate.

Catalog Number: (76107-876)

Supplier: Bioss

Description: Mammalian protein farnesyl transferases are heterodimeric proteins containing two nonidentical Alpha and beta subunits that attach farnesyl residues to a cysteine at the fourth position from the COOH terminus of several proteins, including nuclear lamins and p21Ras proteins. The natural substrates contain the Cys-A-A-Xaa recognition sequence, where the A residues are aliphatic and Xaa represents methionine, serine, glutamine or cysteine. The purified farnesyl transferase is an a-b heterodimer. The beta subunit, which is known as FT beta, CAAX farnesyltransferase subunit beta, or Ras proteins prenyltransferase subunit beta, is a 437 amino acid protein that contains five PFTB repeats and binds the peptide substrate. The Alpha subunit is suspected to participate in formation of a stable complex with the substrate farnesyl pyrophosphate.

Catalog Number: (103007-212)

Supplier: Anaspec Inc

Description: This peptide is the mutant form of beta-Amyloid 1 to 40. These mutations within the beta-Amyloid precursor protein (APP) regions result in the substitution of glutamine for glutamic acid and asparagine for aspartic acid. The peptide rapidly assembles in solution to form fibrils compared to the wild-type beta-Amyloid 1 to 40. Double-mutant E22Q/D23N Dutch/Iowa beta-Amyloid 40 is more potent than either of the single mutant form in causing pathologic responses in culture cells. The double mutations further enhances the fibrillogenic and pathogenic properties of beta-Amyloid.
Sequence: DAEFRHDSGYEVHHQKLVFFAQNVGSNKGAIIGLMVGGVV
Molecular Weight: 4327.9 Da
% Peak Area by HPLC: ≥95
Peptide Content: ≥ 60%
Storage condition: -20°C

Catalog Number: (10491-244)

Supplier: Bioss

Description: Mammalian protein farnesyl transferases are heterodimeric proteins containing two nonidentical Alpha and beta subunits that attach farnesyl residues to a cysteine at the fourth position from the COOH terminus of several proteins, including nuclear lamins and p21Ras proteins. The natural substrates contain the Cys-A-A-Xaa recognition sequence, where the A residues are aliphatic and Xaa represents methionine, serine, glutamine or cysteine. The purified farnesyl transferase is an a-b heterodimer. The beta subunit, which is known as FT beta, CAAX farnesyltransferase subunit beta, or Ras proteins prenyltransferase subunit beta, is a 437 amino acid protein that contains five PFTB repeats and binds the peptide substrate. The Alpha subunit is suspected to participate in formation of a stable complex with the substrate farnesyl pyrophosphate.

Catalog Number: (10491-238)

Supplier: Bioss

Description: Mammalian protein farnesyl transferases are heterodimeric proteins containing two nonidentical Alpha and beta subunits that attach farnesyl residues to a cysteine at the fourth position from the COOH terminus of several proteins, including nuclear lamins and p21Ras proteins. The natural substrates contain the Cys-A-A-Xaa recognition sequence, where the A residues are aliphatic and Xaa represents methionine, serine, glutamine or cysteine. The purified farnesyl transferase is an a-b heterodimer. The beta subunit, which is known as FT beta, CAAX farnesyltransferase subunit beta, or Ras proteins prenyltransferase subunit beta, is a 437 amino acid protein that contains five PFTB repeats and binds the peptide substrate. The Alpha subunit is suspected to participate in formation of a stable complex with the substrate farnesyl pyrophosphate.

Catalog Number: (89417-782)

Supplier: Prosci

Description: GLS2 Antibody: Phosphate-activated glutaminase, also known as Glutaminase 2 (GLS2), was initially isolated from rat liver, although it has been shown to be expressed in other tissues. Like the functionally similar, larger kidney glutaminase, GLS2 catalyzes the hydrolysis of glutamine to stoichiometric amounts of glutamate and ammonia. Expression of GLS2 is increased by p53 under both stressed and nonstressed conditions, resulting in increased levels of glutamate and alpha-ketoglutarate, which in turn results in enhanced mitochondrial respiration and ATP generation. GLS2 also regulates antioxidant defense function in cells by increasing reduced glutathione levels and decreasing ROS-levels, suggesting that GLS2 acts as a mediator of p53's role in antioxidant defense in addition to its role in energy metabolism.

Catalog Number: (10491-226)

Supplier: Bioss

Description: Mammalian protein farnesyl transferases are heterodimeric proteins containing two nonidentical Alpha and beta subunits that attach farnesyl residues to a cysteine at the fourth position from the COOH terminus of several proteins, including nuclear lamins and p21Ras proteins. The natural substrates contain the Cys-A-A-Xaa recognition sequence, where the A residues are aliphatic and Xaa represents methionine, serine, glutamine or cysteine. The purified farnesyl transferase is an a-b heterodimer. The beta subunit, which is known as FT beta, CAAX farnesyltransferase subunit beta, or Ras proteins prenyltransferase subunit beta, is a 437 amino acid protein that contains five PFTB repeats and binds the peptide substrate. The Alpha subunit is suspected to participate in formation of a stable complex with the substrate farnesyl pyrophosphate.

Catalog Number: (10491-240)

Supplier: Bioss

Description: Mammalian protein farnesyl transferases are heterodimeric proteins containing two nonidentical Alpha and beta subunits that attach farnesyl residues to a cysteine at the fourth position from the COOH terminus of several proteins, including nuclear lamins and p21Ras proteins. The natural substrates contain the Cys-A-A-Xaa recognition sequence, where the A residues are aliphatic and Xaa represents methionine, serine, glutamine or cysteine. The purified farnesyl transferase is an a-b heterodimer. The beta subunit, which is known as FT beta, CAAX farnesyltransferase subunit beta, or Ras proteins prenyltransferase subunit beta, is a 437 amino acid protein that contains five PFTB repeats and binds the peptide substrate. The Alpha subunit is suspected to participate in formation of a stable complex with the substrate farnesyl pyrophosphate.

Catalog Number: (10089-168)

Supplier: Proteintech

Description: GLS, also named as GLS1 and KIAA0838, belongs to the glutaminase family. It catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. Glutaminase-, glutamate-, and taurine-immunoreactive neurons develop neurofibrillary tangles in Alzheimer's disease.The glutaminase band in AA/C1 cells is more intense than in HT29 cells, in accordance with measurements of glutaminase activity, and had the same molecular mass of approx. 63 kDa. The bands for both cell lines are clearly different in size from both rat liver glutaminase (58 kDa) and rat kidney glutaminase (65 kDa). It also reveals a molecular weight of 83-84 kDa as a phosphate-dependent glutaminase. It has 3 isoforms named as KGA, GAM, GAC. This antibody can recognize KGA and GAC.

Catalog Number: (76107-878)

Supplier: Bioss

Description: Mammalian protein farnesyl transferases are heterodimeric proteins containing two nonidentical Alpha and beta subunits that attach farnesyl residues to a cysteine at the fourth position from the COOH terminus of several proteins, including nuclear lamins and p21Ras proteins. The natural substrates contain the Cys-A-A-Xaa recognition sequence, where the A residues are aliphatic and Xaa represents methionine, serine, glutamine or cysteine. The purified farnesyl transferase is an a-b heterodimer. The beta subunit, which is known as FT beta, CAAX farnesyltransferase subunit beta, or Ras proteins prenyltransferase subunit beta, is a 437 amino acid protein that contains five PFTB repeats and binds the peptide substrate. The Alpha subunit is suspected to participate in formation of a stable complex with the substrate farnesyl pyrophosphate.

Catalog Number: (10491-396)

Supplier: Bioss

Description: GTP-binding protein 9 is a 396 amino acid protein that belongs to the Obg-related GTPase family under the translation factors (TRAFAC) class. Originally thought to only have GTPase activity, Obg-related GTPase family members have been shown to also have ATPase activity. In Homo sapians, GTPBP9 exhibits a preference for binding ATP over GTP, with GTP binding occuring only at high nucleotide concentration. One cause for ATP affinity and GTP discrimination is thought to be a substitution of glutamine for a hydrophobic amino acid in Obg-related family members; this is the same substitution that inactivates Ras-like GTPases. GTPBP9 contains a C-terminal TGS domain that binds to ligands and an N-terminal G domain which binds nucleotides. GTPBP9 is expressed as three isoforms produced by alternative splicing.

Catalog Number: (76107-900)

Supplier: Bioss

Description: GTP-binding protein 9 is a 396 amino acid protein that belongs to the Obg-related GTPase family under the translation factors (TRAFAC) class. Originally thought to only have GTPase activity, Obg-related GTPase family members have been shown to also have ATPase activity. In Homo sapians, GTPBP9 exhibits a preference for binding ATP over GTP, with GTP binding occurring only at high nucleotide concentration. One cause for ATP affinity and GTP discrimination is thought to be a substitution of glutamine for a hydrophobic amino acid in Obg-related family members; this is the same substitution that inactivates Ras-like GTPases. GTPBP9 contains a C-terminal TGS domain that binds to ligands and an N-terminal G domain which binds nucleotides. GTPBP9 is expressed as three isoforms produced by alternative splicing.

Catalog Number: (10751-254)

Supplier: Prosci

Description: GLS2 Antibody: Phosphate-activated glutaminase, also known as Glutaminase 2 (GLS2), was initially isolated from rat liver, although it has been shown to be expressed in other tissues. Like the functionally similar, larger kidney glutaminase, GLS2 catalyzes the hydrolysis of glutamine to stoichiometric amounts of glutamate and ammonia. Expression of GLS2 is increased by p53 under both stressed and nonstressed conditions, resulting in increased levels of glutamate and alpha-ketoglutarate, which in turn results in enhanced mitochondrial respiration and ATP generation. GLS2 also regulates antioxidant defense function in cells by increasing reduced glutathione levels and decreasing ROS-levels, suggesting that GLS2 acts as a mediator of p53's role in antioxidant defense in addition to its role in energy metabolism.

Catalog Number: (10666-270)

Supplier: Bioss

Description: DR1, also known as NC2∫ (negative cofactor 2 subunit ∫), is a TFIID (TATA box-binding protein)-associated protein. DR1 localizes to the nucleus and contains an N-terminal histone fold motif, a TFIID-binding domain and an alanine and glutamine rich region. Via its histone fold motif, DR1 forms a heterodimer with NC2å (DRAP1) to comprise the conserved eukaryotic complex, NC2 (negative cofactor 2). The NC2 complex can both positively and negatively regulate transcription by RNA Pol II. More specifically, NC2 acts as a repressor of TATA-dependent transcription and acts as an activator for DPE-dependent transcription. NC2 represses RNA Pol II transcription by binding to TFIID and inhibiting association of the transcription factors TFIIA and TFIIB. NC2 activity is regulated by phosphorylation. Both subunits, NC2å and DR1, are phosphorylated in vivo.

Catalog Number: (76109-818)

Supplier: Bioss

Description: DR1, also known as NC2 (negative cofactor 2 subunit ), is a TFIID (TATA box-binding protein)-associated protein. DR1 localizes to the nucleus and contains an N-terminal histone fold motif, a TFIID-binding domain and an alanine and glutamine rich region. Via its histone fold motif, DR1 forms a heterodimer with NC2å (DRAP1) to comprise the conserved eukaryotic complex, NC2 (negative cofactor 2). The NC2 complex can both positively and negatively regulate transcription by RNA Pol II. More specifically, NC2 acts as a repressor of TATA-dependent transcription and acts as an activator for DPE-dependent transcription. NC2 represses RNA Pol II transcription by binding to TFIID and inhibiting association of the transcription factors TFIIA and TFIIB. NC2 activity is regulated by phosphorylation. Both subunits, NC2å and DR1, are phosphorylated <i>in vivo</i>.

Catalog Number: (10491-248)

Supplier: Bioss

Description: Mammalian protein farnesyl transferases are heterodimeric proteins containing two nonidentical Alpha and beta subunits that attach farnesyl residues to a cysteine at the fourth position from the COOH terminus of several proteins, including nuclear lamins and p21Ras proteins. The natural substrates contain the Cys-A-A-Xaa recognition sequence, where the A residues are aliphatic and Xaa represents methionine, serine, glutamine or cysteine. The purified farnesyl transferase is an a-b heterodimer. The beta subunit, which is known as FT beta, CAAX farnesyltransferase subunit beta, or Ras proteins prenyltransferase subunit beta, is a 437 amino acid protein that contains five PFTB repeats and binds the peptide substrate. The Alpha subunit is suspected to participate in formation of a stable complex with the substrate farnesyl pyrophosphate.