THNS2 Rabbit Polyclonal Antibody

Description: A polyclonal antibody for detection of THNS2 from Human, Mouse, Rat. This THNS2 antibody is for WB, ELISA. It is affinity-purified from rabbit serum by affinity-chromatography using the specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthesized peptide derived from part region of human THNS2 protein at amino acid sequence of 91-140

Description: This gene encodes a threonine synthase-like protein. A similar enzyme in mouse can catalyze the degradation of O-phospho-homoserine to a-ketobutyrate, phosphate, and ammonia. This protein also has phospho-lyase activity on both gamma and beta phosphorylated substrates. In mouse an alternatively spliced form of this protein has been shown to act as a cytokine and can induce the production of the inflammatory cytokine IL6 in osteoblasts. Alternate splicing results in multiple transcript variants.

Description: This gene encodes a threonine synthase-like protein. A similar enzyme in mouse can catalyze the degradation of O-phospho-homoserine to a-ketobutyrate, phosphate, and ammonia. This protein also has phospho-lyase activity on both gamma and beta phosphorylated substrates. In mouse an alternatively spliced form of this protein has been shown to act as a cytokine and can induce the production of the inflammatory cytokine IL6 in osteoblasts. Alternate splicing results in multiple transcript variants.

Description: This gene encodes a threonine synthase-like protein. A similar enzyme in mouse can catalyze the degradation of O-phospho-homoserine to a-ketobutyrate, phosphate, and ammonia. This protein also has phospho-lyase activity on both gamma and beta phosphorylated substrates. In mouse an alternatively spliced form of this protein has been shown to act as a cytokine and can induce the production of the inflammatory cytokine IL6 in osteoblasts. Alternate splicing results in multiple transcript variants.

Description: Available in various conjugation types.

Description: Biotin-Conjugated, FITC-Conjugated , AF350 Conjugated , AF405M-Conjugated ,AF488-Conjugated, AF514-Conjugated ,AF532-Conjugated, AF555-Conjugated ,AF568-Conjugated , HRP-Conjugated, AF405S-Conjugated, AF405L-Conjugated , AF546-Conjugated, AF594-Conjugated , AF610-Conjugated, AF635-Conjugated , AF647-Conjugated , AF680-Conjugated , AF700-Conjugated , AF750-Conjugated , AF790-Conjugated , APC-Conjugated , PE-Conjugated , Cy3-Conjugated , Cy5-Conjugated , Cy5.5-Conjugated , Cy7-Conjugated Antibody

Description: Biotin-Conjugated, FITC-Conjugated , AF350 Conjugated , AF405M-Conjugated ,AF488-Conjugated, AF514-Conjugated ,AF532-Conjugated, AF555-Conjugated ,AF568-Conjugated , HRP-Conjugated, AF405S-Conjugated, AF405L-Conjugated , AF546-Conjugated, AF594-Conjugated , AF610-Conjugated, AF635-Conjugated , AF647-Conjugated , AF680-Conjugated , AF700-Conjugated , AF750-Conjugated , AF790-Conjugated , APC-Conjugated , PE-Conjugated , Cy3-Conjugated , Cy5-Conjugated , Cy5.5-Conjugated , Cy7-Conjugated Antibody

Description: Biotin-Conjugated, FITC-Conjugated , AF350 Conjugated , AF405M-Conjugated ,AF488-Conjugated, AF514-Conjugated ,AF532-Conjugated, AF555-Conjugated ,AF568-Conjugated , HRP-Conjugated, AF405S-Conjugated, AF405L-Conjugated , AF546-Conjugated, AF594-Conjugated , AF610-Conjugated, AF635-Conjugated , AF647-Conjugated , AF680-Conjugated , AF700-Conjugated , AF750-Conjugated , AF790-Conjugated , APC-Conjugated , PE-Conjugated , Cy3-Conjugated , Cy5-Conjugated , Cy5.5-Conjugated , Cy7-Conjugated Antibody

Description: THNS2 Rabbit Polyclonal Antibody

Description: THNS2 Rabbit Polyclonal Antibody

Description: Unconjugated

Description: Unconjugated

Description: Unconjugated

Description: Unconjugated

Description: Unconjugated

Description: Unconjugated

Description: Unconjugated

Description: Unconjugated

Description: Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2

Description: 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2

Description: Available in various conjugation types.

Description: THNSL1 (threonine synthase-like 1), also known as TSH1, is a 743 amino acid member of the serine/threonine dehydratase family. Expressed primarily in brain and endocrine glands, THNSL1 is thought to function as a pyridoxal-5'-phosphate (PLP)-dependent enzyme that uses pyridoxal phosphate as a cofactor. THNSL1 shares similarity with bacterial threonine synthases (which synthesize threonine from aspartic acid), suggesting that THNSL1 may have once participated in de novo threonine synthesis within the body, but has since lost its original metabolic role.

Description: THNSL1 (threonine synthase-like 1), also known as TSH1, is a 743 amino acid member of the serine/threonine dehydratase family. Expressed primarily in brain and endocrine glands, THNSL1 is thought to function as a pyridoxal-5'-phosphate (PLP)-dependent enzyme that uses pyridoxal phosphate as a cofactor. THNSL1 shares similarity with bacterial threonine synthases (which synthesize threonine from aspartic acid), suggesting that THNSL1 may have once participated in de novo threonine synthesis within the body, but has since lost its original metabolic role.

Description: THNSL1 (threonine synthase-like 1), also known as TSH1, is a 743 amino acid member of the serine/threonine dehydratase family. Expressed primarily in brain and endocrine glands, THNSL1 is thought to function as a pyridoxal-5'-phosphate (PLP)-dependent enzyme that uses pyridoxal phosphate as a cofactor. THNSL1 shares similarity with bacterial threonine synthases (which synthesize threonine from aspartic acid), suggesting that THNSL1 may have once participated in de novo threonine synthesis within the body, but has since lost its original metabolic role.

Description: THNSL1 (threonine synthase-like 1), also known as TSH1, is a 743 amino acid member of the serine/threonine dehydratase family. Expressed primarily in brain and endocrine glands, THNSL1 is thought to function as a pyridoxal-5'-phosphate (PLP)-dependent enzyme that uses pyridoxal phosphate as a cofactor. THNSL1 shares similarity with bacterial threonine synthases (which synthesize threonine from aspartic acid), suggesting that THNSL1 may have once participated in de novo threonine synthesis within the body, but has since lost its original metabolic role.