Description: GUP1 is a 504 amino acid multipass membrane protein of the endoplasmic reticulum that functions as a membrane bound O-acyltransferase. With specific expression in heart, GUP1 negatively regulates amino-terminal palmitoylation of Shh by HHAT, a protein that is required for Shh signaling. Deletion of the gene encoding GUP1 results in higher sensibility to specific sphinogolipid biosynthesis inhibitors and resistance to ergosterol biosynthesis inhibitors, indicating that GUP1 is an essential component in lipid metabolism. Also, GUP1 also seems to be important for cell wall assembly and stability due to evidence in Saccharomyces cerevisiae GUP1 mutants, which exhibit altered plasma membrane lipid composition and membrane potential.

Catalog Number: BOSSBS-12315R-CY3

UOM: 1 * 100 µl

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Description: GUP1 is a 504 amino acid multipass membrane protein of the endoplasmic reticulum that functions as a membrane bound O-acyltransferase. With specific expression in heart, GUP1 negatively regulates amino-terminal palmitoylation of Shh by HHAT, a protein that is required for Shh signaling. Deletion of the gene encoding GUP1 results in higher sensibility to specific sphinogolipid biosynthesis inhibitors and resistance to ergosterol biosynthesis inhibitors, indicating that GUP1 is an essential component in lipid metabolism. Also, GUP1 also seems to be important for cell wall assembly and stability due to evidence in Saccharomyces cerevisiae GUP1 mutants, which exhibit altered plasma membrane lipid composition and membrane potential.

Catalog Number: BOSSBS-12315R-A555

UOM: 1 * 100 µl

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Description: Acetyl-CoA carboxylase (ACC) is a complex multifunctional enzyme system. ACC is a biotin-containing enzyme which catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the rate-limiting step in fatty acid synthesis. There are two ACC forms, alpha and beta, encoded by two different genes. ACC-alpha is highly enriched in lipogenic tissues. The enzyme is under long term control at the transcriptional and translational levels and under short term regulation by the phosphorylation/dephosphorylation of targeted serine residues and by allosteric transformation by citrate or palmitoyl-CoA. Multiple alternatively spliced transcript variants divergent in the 5' sequence and encoding distinct isoforms have been found for this gene. [provided by RefSeq, Jul 2008].

Catalog Number: BOSSBS-2745R-CY5

UOM: 1 * 100 µl

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Description: Paralemmin, also called Paralemmin-1 or PALM, is a widely expressed peripheral membrane protein that is involved in cell structure and shape. A hydrophobic protein, Paralemmin is anchored to the cytoplasmic side of the cell membrane via di-palmitoylation and prenylation of its C-terminal cysteine cluster. Functioning at the synapse to regulate neuronal plasticity and plasma membrane dynamics, Paralemmin can bind to the dopamine receptor D3, thereby reducing D3 expression and subsequent adenylate cyclase activity. Overexpression of Paralemmin induces fibroblasts to extend long filopodia and to assume extreme cell shapes, suggesting involvement in the formation and stabilization of the plasma membrane. Two isoforms of Paralemmin exists due to alternative splicing events.

Catalog Number: BOSSBS-12035R-HRP

UOM: 1 * 100 µl

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Description: Acetyl-CoA carboxylase (ACC) is a complex multifunctional enzyme system. ACC is a biotin-containing enzyme which catalyses the carboxylation of acetyl-CoA to malonyl-CoA, the rate-limiting step in fatty acid synthesis. There are two ACC forms, alpha and beta, encoded by two different genes. ACC-alpha is highly enriched in lipogenic tissues. The enzyme is under long term control at the transcriptional and translational levels and under short term regulation by the phosphorylation/dephosphorylation of targeted serine residues and by allosteric transformation by citrate or palmitoyl-CoA. Multiple alternatively spliced transcript variants divergent in the 5' sequence and encoding distinct isoforms have been found for this gene.

Catalog Number: BOSSBS-12952R-A680

UOM: 1 * 100 µl

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Description: P55 is an extensively palmitoylated erythrocyte membrane protein, and a member of the MAGUK family. P55 also resists salt extraction, resulting in a high affinity for the plasma membrane. P55 contains a PDZ/DHR domain, a conserved SH-3 domain that appears to suppress tyrosine kinase activity of various oncoproteins, a 39-amino acid motif that binds to cytoskeletal protein 4.1R, and a guanylate kinase-like domain. Interaction with glycophorin C (GPC) and 4.1R suggests that p55 may play a role in the dynamic regulation in the erythrocyte membrane. In addition, p55 gene expression in vivo may be associated with a CpG island. P55 is constitutively expressed in K562 erythroleukemia cells during erythropoiesis and undergoes a 2-fold amplification after induction.

Catalog Number: BOSSBS-9393R-CY7

UOM: 1 * 100 µl

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Description: HHAT is a 493 amino acid multi-pass membrane protein that localises to the endoplasmic reticulum and belongs to the membrane-bound acyltransferase family. Expressed ubiquitously, HHAT functions to catalyse the N-terminal palmitoylation of SSH (slingshot homolog), an event that is required for SHH signaling pathways. HHAT is expressed in cancer cell lines, suggesting a role for HHAT in tumorigenesis. The gene encoding HHAT maps to human chromosome 1 and is expressed as four alternatively spliced isoforms. Chromosome 1 is the largest human chromosome, spanning about 260 million base pairs and making up 8% of the human genome. Several disorders, including Stickler syndrome, Parkinsons Disease, Gaucher disease, malignant melanoma and Usher syndrome, are caused by defects in genes that localise to chromosome 1.

Catalog Number: BOSSBS-15474R-A647

UOM: 1 * 100 µl

Supplier: Bioss

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Description: Acetyl-CoA carboxylase (ACC) is a complex multifunctional enzyme system. ACC is a biotin-containing enzyme which catalyzes the carboxylation of acetyl-CoA to malonyl-CoA, the rate-limiting step in fatty acid synthesis. There are two ACC forms, alpha and beta, encoded by two different genes. ACC-alpha is highly enriched in lipogenic tissues. The enzyme is under long term control at the transcriptional and translational levels and under short term regulation by the phosphorylation/dephosphorylation of targeted serine residues and by allosteric transformation by citrate or palmitoyl-CoA. Multiple alternatively spliced transcript variants divergent in the 5' sequence and encoding distinct isoforms have been found for this gene. [provided by RefSeq, Jul 2008].

Catalog Number: BOSSBS-2745R-A647

UOM: 1 * 100 µl

Supplier: Bioss

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Description: HHAT is a 493 amino acid multi-pass membrane protein that localises to the endoplasmic reticulum and belongs to the membrane-bound acyltransferase family. Expressed ubiquitously, HHAT functions to catalyse the N-terminal palmitoylation of SSH (slingshot homolog), an event that is required for SHH signaling pathways. HHAT is expressed in cancer cell lines, suggesting a role for HHAT in tumorigenesis. The gene encoding HHAT maps to human chromosome 1 and is expressed as four alternatively spliced isoforms. Chromosome 1 is the largest human chromosome, spanning about 260 million base pairs and making up 8% of the human genome. Several disorders, including Stickler syndrome, Parkinsons Disease, Gaucher disease, malignant melanoma and Usher syndrome, are caused by defects in genes that localise to chromosome 1.

Catalog Number: BOSSBS-15474R-A750

UOM: 1 * 100 µl

Supplier: Bioss

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Description: P55 is an extensively palmitoylated erythrocyte membrane protein, and a member of the MAGUK family. P55 also resists salt extraction, resulting in a high affinity for the plasma membrane. P55 contains a PDZ/DHR domain, a conserved SH-3 domain that appears to suppress tyrosine kinase activity of various oncoproteins, a 39-amino acid motif that binds to cytoskeletal protein 4.1R, and a guanylate kinase-like domain. Interaction with glycophorin C (GPC) and 4.1R suggests that p55 may play a role in the dynamic regulation in the erythrocyte membrane. In addition, p55 gene expression in vivo may be associated with a CpG island. P55 is constitutively expressed in K562 erythroleukemia cells during erythropoiesis and undergoes a 2-fold amplification after induction.

Catalog Number: BOSSBS-9393R-A555

UOM: 1 * 100 µl

Supplier: Bioss

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Description: P55 is an extensively palmitoylated erythrocyte membrane protein, and a member of the MAGUK family. P55 also resists salt extraction, resulting in a high affinity for the plasma membrane. P55 contains a PDZ/DHR domain, a conserved SH-3 domain that appears to suppress tyrosine kinase activity of various oncoproteins, a 39-amino acid motif that binds to cytoskeletal protein 4.1R, and a guanylate kinase-like domain. Interaction with glycophorin C (GPC) and 4.1R suggests that p55 may play a role in the dynamic regulation in the erythrocyte membrane. In addition, p55 gene expression in vivo may be associated with a CpG island. P55 is constitutively expressed in K562 erythroleukemia cells during erythropoiesis and undergoes a 2-fold amplification after induction.

Catalog Number: BOSSBS-9393R-A488

UOM: 1 * 100 µl

Supplier: Bioss

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Description: Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs.

Catalog Number: BOSSBS-5040R-CY5.5

UOM: 1 * 100 µl

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Description: Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs.

Catalog Number: BOSSBS-5040R-CY5

UOM: 1 * 100 µl

Supplier: Bioss

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Description: Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs.

Catalog Number: BOSSBS-5040R-A647

UOM: 1 * 100 µl

Supplier: Bioss

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Description: Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs.

Catalog Number: BOSSBS-5040R-HRP

UOM: 1 * 100 µl

Supplier: Bioss

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Description: Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs.

Catalog Number: BOSSBS-5040R-CY3

UOM: 1 * 100 µl

Supplier: Bioss

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