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Human Glycine Metabolic Process

Also showing Human Glycine Biosynthetic Process

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Serine hydroxymethyltransferases 1 and 2 (SHMT1, SHMT2) are cytoplasmic and mitochondrial serine hydroxylmethyltransferases, respectively (1,2). They catalyze the conversion of serine to glycine with the transfer of β-carbon from serine to tetrahydrofolate (THF) to form 5, 10-methylene-THF (1, 2). Research studies indicate that SHMT1 hemizygosity is associated with higher risk of intestinal cancer in mice of a certain genetic background (3). Suppression of SHMT2 was shown to block cell proliferation (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Mammalian cells synthesize serine de novo by diverting a portion of the glycolytic intermediate 3-phosphoglycerate into the phosphorylated pathway of serine synthesis. This shift supports anabolism by providing precursors for the biosynthesis of proteins, nucleotides, creatine, porphyrins, phospholipids, and glutathione. Phosphoglycerate dehydrogenase (PHGDH) catalyzes the first step in the serine biosynthesis pathway by converting 3-phosphoglycerate into phosphohydroxy pyruvate (1).Research studies demonstrate that an increase in serine biosynthesis supports growth and proliferation of cancer cells (2-4), which is supported by amplification and overexpression of PHGDH in a subset of melanoma and breast cancers (5,6). Suppression of PHGDH expression in cell lines with elevated PHGDH levels causes a strong decrease in cell proliferation and inhibits tumor growth in vivo (5). Additional evidence suggests that PHGDH interacts with and stabilizes FoxM1, which promotes the proliferation, invasion, and tumorigenicity of glioma cells (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Mammalian cells synthesize serine de novo by diverting a portion of the glycolytic intermediate 3-phosphoglycerate into the phosphorylated pathway of serine synthesis. This shift supports anabolism by providing precursors for the biosynthesis of proteins, nucleotides, creatine, porphyrins, phospholipids, and glutathione. Phosphoglycerate dehydrogenase (PHGDH) catalyzes the first step in the serine biosynthesis pathway by converting 3-phosphoglycerate into phosphohydroxy pyruvate (1).Research studies demonstrate that an increase in serine biosynthesis supports growth and proliferation of cancer cells (2-4), which is supported by amplification and overexpression of PHGDH in a subset of melanoma and breast cancers (5,6). Suppression of PHGDH expression in cell lines with elevated PHGDH levels causes a strong decrease in cell proliferation and inhibits tumor growth in vivo (5). Additional evidence suggests that PHGDH interacts with and stabilizes FoxM1, which promotes the proliferation, invasion, and tumorigenicity of glioma cells (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry)

Background: Mammalian cells synthesize serine de novo by diverting a portion of the glycolytic intermediate 3-phosphoglycerate into the phosphorylated pathway of serine synthesis. This shift supports anabolism by providing precursors for the biosynthesis of proteins, nucleotides, creatine, porphyrins, phospholipids, and glutathione. Phosphoglycerate dehydrogenase (PHGDH) catalyzes the first step in the serine biosynthesis pathway by converting 3-phosphoglycerate into phosphohydroxy pyruvate (1).Research studies demonstrate that an increase in serine biosynthesis supports growth and proliferation of cancer cells (2-4), which is supported by amplification and overexpression of PHGDH in a subset of melanoma and breast cancers (5,6). Suppression of PHGDH expression in cell lines with elevated PHGDH levels causes a strong decrease in cell proliferation and inhibits tumor growth in vivo (5). Additional evidence suggests that PHGDH interacts with and stabilizes FoxM1, which promotes the proliferation, invasion, and tumorigenicity of glioma cells (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Serine hydroxymethyltransferases 1 and 2 (SHMT1, SHMT2) are cytoplasmic and mitochondrial serine hydroxylmethyltransferases, respectively (1,2). They catalyze the conversion of serine to glycine with the transfer of β-carbon from serine to tetrahydrofolate (THF) to form 5, 10-methylene-THF (1, 2). Research studies indicate that SHMT1 hemizygosity is associated with higher risk of intestinal cancer in mice of a certain genetic background (3). Suppression of SHMT2 was shown to block cell proliferation (4).

$108
250 PCR reactions
500 µl
SimpleChIP® Human DHFR Intron 1 Primers contain a mix of forward and reverse PCR primers that are specific to the intron 1 region of the human dihydrofolate reductase (DHFR) gene. These primers can be used to amplify DNA that has been isolated using chromatin immunoprecipitation (ChIP). Primers have been optimized for use in SYBR® Green quantitative real-time PCR and have been tested in conjunction with SimpleChIP® Enzymatic Chromatin IP Kits #9002 and #9003 and ChIP-validated antibodies from Cell Signaling Technology®. The DHFR gene is actively transcribed in all cell types and is required for cell growth. There are several GC elements around the DHFR promoter that when bound by SP1, promote gene transcription.
REACTIVITY
Human

Background: The chromatin immunoprecipitation (ChIP) assay is a powerful and versatile technique used for probing protein-DNA interactions within the natural chromatin context of the cell (1,2). This assay can be used to either identify multiple proteins associated with a specific region of the genome or to identify the many regions of the genome bound by a particular protein (3-6). ChIP can be used to determine the specific order of recruitment of various proteins to a gene promoter or to "measure" the relative amount of a particular histone modification across an entire gene locus (3,4). In addition to histone proteins, the ChIP assay can be used to analyze binding of transcription factors and co-factors, DNA replication factors, and DNA repair proteins. When performing the ChIP assay, cells are first fixed with formaldehyde, a reversible protein-DNA cross-linking agent that "preserves" the protein-DNA interactions occurring in the cell (1,2). Cells are lysed and chromatin is harvested and fragmented using either sonication or enzymatic digestion. Fragmented chromatin is then immunoprecipitated with antibodies specific to a particular protein or histone modification. Any DNA sequences that are associated with the protein or histone modification of interest will co-precipitate as part of the cross-linked chromatin complex and the relative amount of that DNA sequence will be enriched by the immunoselection process. After immunoprecipitation, the protein-DNA cross-links are reversed and the DNA is purified. Standard PCR or quantitative real-time PCR are often used to measure the amount of enrichment of a particular DNA sequence by a protein-specific immunoprecipitation (1,2). Alternatively, the ChIP assay can be combined with genomic tiling micro-array (ChIP on chip) techniques, high throughput sequencing (ChIP-Seq), or cloning strategies, all of which allow for genome-wide analysis of protein-DNA interactions and histone modifications (5-8). SimpleChIP® primers have been optimized for amplification of ChIP-isolated DNA using real-time quantitative PCR and provide important positive and negative controls that can be used to confirm a successful ChIP experiment.