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Beta-galactosidase is a hydrolase enzyme that catalyzes the hydrolysis of Beta-galactosides into monosaccharides. Substrates of different Beta-galactosidases include ganglioside GM1, lactosylceramides, lactose, and various glycoproteins. Beta-galactosidase is produced In E. coli by activation of the lac operon as the lacZ gene.

Beta-galactosidase or GLB1 is a B-galactosidase found in the lysosome. This enzyme hydrolyzes the finale B-galactose from the precursors ganglioside & keratin sulfate. GLB1 has a crucial part in the creation of elastogenesis (extracellular elastic fibers) and connective tissue development. This enzyme is similar to elastin-binding protein which is a key part in non-integrin cell surface receptor. In cells that extort elastin GLB1 is linked to tropoelastin intracellularly and act as recycling molecular chaperone.

GLC8 is a regulatory subunit of protein phosphatase 1 (Glc7p). GLC8 plays a role in glycogen metabolism and chromosome segregation, and regulates Glc7p activity through conformational alteration; ortholog of the mammalian protein phosphatase inhibitor 2. Under regular conditions, GLC8 triggers GLC7, but when GLC8 is over epxressed, it inhibits Glc7p function. GLC8 is activated upon phosphoylation by Pho85p complexed with four cyclins (Pcl6p, Pcl7p, Pcl8p, or Pcl10p).

Glycerol dehydrogenase (GldA) catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone). The GldA protein allows microorganisms to use glycerol as a source of carbon under anaerobic conditions. Furthermore, in E.coli GldA has an imperative role by regulating the intracellular level of dihydroxyacetone by catalyzing the reverse reaction, i.e. the conversion of dihydroxyacetone into glycerol. GldA possesses an extensive substrate specificity, due to its ability to oxidize 1,2-propanediol and to reduce glycolaldehyde, methylglyoxal and hydroxyacetone into ethylene glycol, lactaldehyde and 1,2-propanediol, respectively.

Glycerol dehydrogenase (GldA) catalyzes the NAD-dependent oxidation of glycerol to dihydroxyacetone (glycerone). The GldA protein allows microorganisms to use glycerol as a source of carbon under anaerobic conditions. Furthermore, in E.coli GldA has an imperative role by regulating the intracellular level of dihydroxyacetone by catalyzing the reverse reaction, i.e. the conversion of dihydroxyacetone into glycerol. GldA possesses an extensive substrate specificity, due to its ability to oxidize 1,2-propanediol and to reduce glycolaldehyde, methylglyoxal and hydroxyacetone into ethylene glycol, lactaldehyde and 1,2-propanediol, respectively.

Wheat Gliadin and related gluten components from barley, rye and possibly oats can cause an abnormal immune response called Celiac disease which is a chronic gastrointestinal disorder. Celiac disease characteristics are flattening of the jejunal mucosa and intestinal lesions of variable severity in hereditarily inclined individuals. Even though Celiac disease is not a classic autoimmune disease it is related to anti-tissue transglutaminase antibodies and gliadin antibodies tests are most recommended in screening populations at risk for CD and other gluten-sensitive enteropathies. In the past, serologic tests for gliadin antibodies usually were not very precise and were not enough for accurate diagnosis due to missing deamidated epitopes within the authentic gliadin fraction traditionally used in diagnostic test kits. ProSpec's deamidated Gliadin isoform matches to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation.

Wheat Gliadin and related gluten components from barley, rye and possibly oats can cause an abnormal immune response called Celiac disease which is a chronic gastrointestinal disorder. Celiac disease characteristics are flattening of the jejunal mucosa and intestinal lesions of variable severity in hereditarily inclined individuals. Even though Celiac disease is not a classic autoimmune disease it is related to anti-tissue transglutaminase antibodies and gliadin antibodies tests are most recommended in screening populations at risk for CD and other gluten-sensitive enteropathies. In the past, serologic tests for gliadin antibodies usually were not very precise and were not enough for accurate diagnosis due to missing deamidated epitopes within the authentic gliadin fraction traditionally used in diagnostic test kits. ProSpec's deamidated Gliadin isoform matches to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation.

Wheat Gliadin and related gluten components from barley, rye and possibly oats can cause an abnormal immune response called Celiac disease which is a chronic gastrointestinal disorder. Celiac disease characteristics are flattening of the jejunal mucosa and intestinal lesions of variable severity in hereditarily inclined individuals. Even though Celiac disease is not a classic autoimmune disease it is related to anti-tissue transglutaminase antibodies and gliadin antibodies tests are most recommended in screening populations at risk for CD and other gluten-sensitive enteropathies. In the past, serologic tests for gliadin antibodies usually were not very precise and were not enough for accurate diagnosis due to missing deamidated epitopes within the authentic gliadin fraction traditionally used in diagnostic test kits. ProSpec's deamidated Gliadin isoform matches to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation.

Gliadin is a common substrate of transglutaminase, which generates neo-epitopes by deamidation of glutamine side chains. In the past, serologic tests for gliadin antibodies usually were not very precise and were not enough for accurate diagnosis due to missing deamidated epitopes within the authentic gliadin fraction traditionally used in diagnostic test kits. ProSpec's deamidated Gliadin isoform matches to the deamidated neo-epitopes, which in the natural antigen are formed by transglutaminase-mediated glutamine side chain deamidation.

GLIPR2 is linked to plant pathogenesis-related (PR-1) proteins, which are upregulated in reaction to pathogen attack. GLIPR2 is localized within lipid-enriched microdomains on the cytosolic side of the endomembrane system. GLIPR2 is closely attached to membranes and lacks the cytosol, though it lacks a membrane-spanning domain.

Glucokinase also known as GLK is a member of the bacterial glucokinase family. GLK is not highly significant in E.coli since glucoseis already transported into the cell through the PTS system as glucose 6-phosphate.

Glucokinase or GLK, is a protein, part of the bacterial glucokinase superfamily. In the bacteria E. coli, glucose can be transported to the inner cell through a system called PTS as glucose 6-phosphate, therefore, GLK is less crucial to the bacteria.

GLO1 is involved in the catalysis and formation of S-lactoyl-glutathione from methylglyoxal condensation and reduced glutatione. GLO1 is linked to HLA and is localized to 6p21.3-p21.1, between HLA and the centromere. GLO1 enzyme is ubundantly expressed and present in numerous tumor cell lines, in which its concentration is often upregulated ubiquitisly. GLO1 is a major susceptible gene for autism in an ethnic Chinese population from Taiwan. GLO1 might be involved in the pathophysiology of mood disorders. GLO1 plays a role in the pathophysiology of mood disorders. Overexpression of GLO1 is associated with kidney tumor.

GLO1 is involved in the catalysis and formation of S-lactoyl-glutathione from methylglyoxal condensation and reduced glutatione. GLO1 is linked to HLA and is localized to 6p21.3-p21.1, between HLA and the centromere. GLO1 enzyme is ubundantly expressed and present in numerous tumor cell lines, in which its concentration is often upregulated ubiquitisly. GLO1 is a major susceptible gene for autism in an ethnic Chinese population from Taiwan. GLO1 might be involved in the pathophysiology of mood disorders. GLO1 plays a role in the pathophysiology of mood disorders. Overexpression of GLO1 is associated with kidney tumor.

GLO1 is involved in the catalysis and formation of S-lactoyl-glutathione from methylglyoxal condensation and reduced glutatione. GLO1 is linked to HLA and is localized to 6p21.3-p21.1, between HLA and the centromere. GLO1 enzyme is ubundantly expressed and present in numerous tumor cell lines, in which its concentration is often upregulated ubiquitisly. GLO1 is a major susceptible gene for autism in an ethnic Chinese population from Taiwan. GLO1 might be involved in the pathophysiology of mood disorders. GLO1 plays a role in the pathophysiology of mood disorders. Overexpression of GLO1 is associated with kidney tumor.

GLOD4 is a part of the glyoxalase system which is a group of enzymes that is in charge of the detoxification of methylglyoxal and other reactive aldehydes that are usually produced in metabolism. The mitochondrial protein GLOD4 is known to interact with NUDT9.

Glucagon-like peptide-1 (GLP-1) is derived from the transcription product of the proglucagon gene. The major source of GLP-1 in the body is the intestinal L cell that secretes GLP-1 as a guthormone. The biologically active forms of GLP-1 are: GLP-1-(7-37) and GLP-1-(7-36)NH2.
GLP-1 secretion by L cells is dependent on the presence of nutrients in the lumen of the small intestine. The secretagogues (agents that causes or stimulates secretion) of this hormone include major nutrients like carbohydrate, proteinand lipid. Once in the circulation, GLP-1 has a half life of less than 2 minutes, due to rapid degradation by the enzyme dipeptidyl peptidase-4.
GLP-1 possesses several physiological properties that make it a subject of intensive investigation as a potential treatment of diabetes mellitus. The known physiological functions of GLP-1 include: Increases insulin secretion from the pancreas in a glucose-dependent manner, decreases glucagon secretion from the pancreas, increases beta cells mass and insulin gene expression, inhibits acid secretion and gastric emptying in the stomach, decreases food intake by increasing satiety.

GLP-2 functions as an intestinal growth factor, which stimulates intestinal epithelial growth. GLP2 is involved in diabetes-associated bowel growth. GLP2 enhances cell differentiation, playing a role as a cytokine and in tissue regeneration, and mediating cytoprotection. GLP2 is invloded numerous therapeutic applications. GLP2 regulates signaling pathways coupled to cell proliferation and cell death by apoptosis.
GLP-2 is produced by specific post-translational proteolytic cleavage of proGLP. GLP-2 is manufactured by the intestinal endocrine L cell and by several neurons in the central nervous system.

Glucagon-like peptide-1 (GLP-1) is derived from the transcription product of the proglucagon gene. The major source of GLP-1 in the body is the intestinal L cell that secretes GLP-1 as a guthormone. The biologically active forms of GLP-1 are: GLP-1-(7-37) and GLP-1-(7-36)NH2.
GLP-1 secretion by L cells is dependent on the presence of nutrients in the lumen of the small intestine. The secretagogues (agents that causes or stimulates secretion) of this hormone include major nutrients like carbohydrate, proteinand lipid. Once in the circulation, GLP-1 has a half life of less than 2 minutes, due to rapid degradation by the enzyme dipeptidyl peptidase-4.
GLP-1 possesses several physiological properties that make it a subject of intensive investigation as a potential treatment of diabetes mellitus. The known physiological functions of GLP-1 include: Increases insulin secretion from the pancreas in a glucose-dependent manner, decreases glucagon secretion from the pancreas, increases beta cells mass and insulin gene expression, inhibits acid secretion and gastric emptying in the stomach, decreases food intake by increasing satiety.

The glucagon-like peptide-1 receptor, also known as GLP1R, is a receptor protein found on brain neurons and beta cells of the pancreas. GLP1R activates a signalling cascade that leads to the initiation of adenylyl cyclase and increased intracellular cAMP levels. In humans, GLP1R is synthesized by GLP1R gene, which is present on chromosome 6.
GLP1R takes part in the control of blood sugar level by enhancing insulin secretion. GLP1R is a part of the glucagon receptor family of G protein-coupled receptors. GLP1R consists of two domains, one transmembrane (TMD) domain, that binds the N-terminal region of GLP-1. And one extracellular (ECD) which binds the C-terminal helix of GLP-1. The TMD domain contains a fulcrum of polar residues that controls the biased signaling of the receptor, while the transmembrane helical boundaries and extracellular surface are a trigger for biased agonism.

Thiosulfate sulfurtransferase (glpE) is a mitochondrial matrix enzyme which is encoded by the nucleus. Escherichia coli glpE is a prototype for the single-domain rhodanese superfamily. glpE catalyzes the sulfur-transfer reaction in which a sulfur atom is transferred from thiosulfate to cyanide by a double-displacement mechanism.

GlpK also known as glycerol kinase, is a member of the FGGY kinase family. GlpK catalyzes the transfer of a phosphate group from ATP to glycerol, thereby forming glycerol phosphate. Furthermore, this intermediate can then be converted to dihydroxyacetone phosphate (DHAP), which is utilized in either glycolysis or gluconeogenesis. The activity of GlpK is affected by numerous metabolites. The non-competitive allosteric inhibition by fructose 1,6-bisphosphate (FBP) triggers modifications in the quaternary structure of Glpk.

GLRX1 has a glutathione-disulfide oxidoreductase activity in the presence of nadph and glutathione reductase. reduces low molecular weight disulfides and proteins. Glutaredoxin is a glutathione (GSH)-dependent hydrogen donor for ribonucleotide reductase and also catalyzes glutathione-disulfide oxidoreduction reactions in the presence of NADPH and glutathione reductase. GLRX1 is multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage.

GLRX1 has a glutathione-disulfide oxidoreductase activity in the presence of nadph and glutathione reductase. reduces low molecular weight disulfides and proteins. Glutaredoxin is a glutathione (GSH)-dependent hydrogen donor for ribonucleotide reductase and also catalyzes glutathione-disulfide oxidoreduction reactions in the presence of NADPH and glutathione reductase. GLRX1 is multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage.

GLRX2 is a multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. Glutaredoxins are a family of glutathione-dependent hydrogen donors that participate in a variety of cellular redox reactions.

GLRX2 is a multifunctional enzyme with glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-protein-disulfides in a coupled system with glutathione reductase. Required for resistance to reactive oxygen species (ROS) by directly reducing hydroperoxides and for the detoxification of ROS-mediated damage. Glutaredoxins are a family of glutathione-dependent hydrogen donors that participate in a variety of cellular redox reactions.

Glutaredoxin belongs to the thiol-disulfide oxidoreductase family. Glutraredoxins catalyze the reversible reduction of protein-glutathionyl mixed disulfides to free sulfhydryl groups though a monothiol mechanism. Glutaredoxin-3 (GRX3) is an important protein involved in the regulation of signal transduction, for example during immune cell activation and development of cardiac hypertrophy, apparently in response to redox signals. GRX3 interacts with PRKCQ. GRX3 may have a role in the regulation the function of the thioredoxin system. GRX3 is expressed in the heart, spleen, testis and, to a lower extent, in the thymus and peripheral blood leukocytes. GRX3 is weakly expressed in lung, placenta, colon and small intestine.

GLRX5 is small redox enzyme of approximately 100 amino acids which uses glutathione as a cofactor. GLRX5 is a mitochondrial protein, which is evolutionarily conserved. GLRX5 is oxidized by substrates, and reduced non-enzymatically by glutathione. GLRX5 is involved in the biogenesis of iron-sulfur clusters that are required for normal iron homeostasis. GLRX5 is necessary for normal regulation of hemoglobin synthesis by the iron-sulfur protein ACO1. Defects in the GLRX5 gene are a cause of anemia sideroblastic pyridoxine-refractory autosomal recessive (PRARSA).

GlsA1 is a member of the great superfamily of serine-dependent beta-lactamases and penicillin-binding proteins which exist almost in every bacteria and eukaryotes and catalyze the hydrolytic deamidation of l-glutamine to l-glutamate and free NH4+.

Glycolipid transfer protein (GLTP) accelerates the intermembrane transfer of different glycolipids. GLTP catalyzes the transfer of various glycosphingolipids between membranes however does not catalyze the transfer of phospholipids. GLTP is involved in the intracellular translocation of glucosylceramides. The GLTP protein is similar to bovine and porcine proteins which accelerate transfer of certain glycosphingolipids and glyceroglycolipids between membranes. GLTP is assumed to be a cytoplasmic protein. GLTP is detected in fibroblasts and in various cancer cell lines.

Glycolipid Transfer Protein Domain Containing 1 (GLTPD1) belongs to the GLTP family. GLTPD1 mediates the intracellular transfer of ceramide-1-phosphate between organelle membranes and the cell membrane. GLTPD1 is essential for normal structure of the Golgi stacks. In addition, GLTPD1 is able to bind phosphoceramides with a diversity of aliphatic chains, however GLTPD1 has a preference for lipids with saturated C16:0 or monounsaturated C18:1 aliphatic chains. Moreover, GLTPD1 is inefficient with phosphoceramides which contains lignoceryl (C24:0). GLTPD1 participates in the regulation of the cellular levels of ceramide-1-phosphate, and in that way contributes to the regulation of phospholipase PLA2G4A activity and the release of arachidonic acid.

Glutamyl endopeptidase (GLU-C) is an enzyme which cleaves peptide bonds on the carboxyl-terminal side of glutamic acid and, less frequently, aspartic acid (for example: Glu-|-Xaa, Asp-|-Xaa). GLU-C is a pathogenic factor involved in the adherence and colonization of human tissue. GLU-C preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. GLU-C is required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. GLU-C is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. Furthermore, GLU-C protects bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. GLU-C may also be involved in the stability of secreted lipases.

Glucagon is an important hormone involved in carbohydrate metabolism. The hormone is synthesized and secreted from alpha cells (?-cells) of the islets of Langerhans, which are located in the endocrine portion of the pancreas. Glucagon is released when the glucose level in the blood is low (hypoglycemia), causing the liver to convert stored glycogen into glucose and release it into the bloodstream. The action of glucagon is thus opposite to that of insulin, which instructs the body's cells to take in glucose from the blood in times of satiation.
Glucagon is beneficial for the culture of some cell types. It has been used in some biochemical regulation studies of glycogenolysis in hepatocytes. It has been also been found to induce DNA replication in primary cultures of adult rat hepatocytes when used in combinations with EGF and Insulin. Glucagon increases the blood glucose concentration by promoting rapid breakdown of liver glycogen, and also acts to relax smooth muscle such as the gastrointestinal tract.

Glucagon is an important hormone involved in carbohydrate metabolism. The hormone is synthesized and secreted from alpha cells (a-cells) of the islets of Langerhans, which are located in the endocrine portion of the pancreas. Glucagon is released when the glucose level in the blood is low (hypoglycemia), causing the liver to convert stored glycogen into glucose and release it into the bloodstream. The action of glucagon is thus opposite to that of insulin, which instructs the body's cells to take in glucose from the blood in times of satiation.
Glucagon is beneficial for the culture of some cell types. It has been used in some biochemical regulation studies of glycogenolysis in hepatocytes. It has been also been found to induce DNA replication in primary cultures of adult rat hepatocytes when used in combinations with EGF and Insulin. Glucagon increases the blood glucose concentration by promoting rapid breakdown of liver glycogen, and also acts to relax smooth muscle such as the gastrointestinal tract.

Glucagon is an important hormone involved in carbohydrate metabolism. The hormone is synthesized and secreted from alpha cells (a-cells) of the islets of Langerhans, which are located in the endocrine portion of the pancreas. Glucagon is released when the glucose level in the blood is low (hypoglycemia), causing the liver to convert stored glycogen into glucose and release it into the bloodstream. The action of glucagon is thus opposite to that of insulin, which instructs the body's cells to take in glucose from the blood in times of satiation.
Glucagon is beneficial for the culture of some cell types. It has been used in some biochemical regulation studies of glycogenolysis in hepatocytes. It has been also been found to induce DNA replication in primary cultures of adult rat hepatocytes when used in combinations with EGF and Insulin. Glucagon increases the blood glucose concentration by promoting rapid breakdown of liver glycogen, and also acts to relax smooth muscle such as the gastrointestinal tract.

Glutamate dehydrogenase 1, mitochondrial precursor (GLUD1) is a member of the Glu/Leu/Phe/Val dehydrogenases family. GLUD1 is a mitochondrial glutamate dehydrogenase, which converts L-glutamate into alpha-ketoglutarate. GLUD1 has a pivotal role in nitrogen metabolism in plants and animals. GLUD1 is observed in all organisms and catalyzes the oxidative deamination of 1-glutamate to 2-oxoglutarate. The GLUD1 enzyme has a vital role in regulating amino acid induced insulin secretion. GLUD1 gene mutations cause hyperinsulinism-hyperammonemia syndrome (HHS), which is an inherited condition characterized by high insulin and ammonia levels in the blood. GLUD1 enzyme is allosterically activated by ADP and inhibited by GTP and ATP.

GLUL catalyzes the synthesis of glutamine from glutamate and ammonia. Glutamine is a major source of energy and that takes part in cell proliferation, inhibition of apoptosis, and cell signaling. GLUL is expressed during early fetal stages, and has a role in maintaining body pH by removing ammonia from circulation. Mutations in GLUL gene are related with congenital glutamine deficiency.

GLUL catalyzes the synthesis of glutamine from glutamate and ammonia. Glutamine is a major source of energy and that takes part in cell proliferation, inhibition of apoptosis, and cell signaling. GLUL is expressed during early fetal stages, and has a role in maintaining body pH by removing ammonia from circulation. Mutations in GLUL gene are related with congenital glutamine deficiency.

GLUL catalyzes the synthesis of glutamine from glutamate and ammonia. Glutamine is a major source of energy and that takes part in cell proliferation, inhibition of apoptosis, and cell signaling. GLUL is expressed during early fetal stages, and has a role in maintaining body pH by removing ammonia from circulation. Mutations in GLUL gene are related with congenital glutamine deficiency.

GLUL catalyzes the synthesis of glutamine from glutamate and ammonia. Glutamine is a major source of energy and that takes part in cell proliferation, inhibition of apoptosis, and cell signaling. GLUL is expressed during early fetal stages, and has a role in maintaining body pH by removing ammonia from circulation. Mutations in GLUL gene are related with congenital glutamine deficiency.

Stress-Induced Protein SAM22 (Gly m 4.0101) causes an allergic reaction in humans. Gly m 4 is the main soy allergen for patients allergic to birch pollen with soy allergy.

GLYAT is a mitochondrial acyltransferase that conjugates glycine with acyl-CoA substrates in the mitochondria. GLYAT is vital to the detoxification of endogenous and xenobiotic acyl-CoA's.

Glycine-N-Acyltransferase-Like 2 (GLYATL2) is a part of the glycine N-acyltransferase family expressed mainly in salivary gland and trachea. GLYATL2 is a mitochondrial acyltransferase that transfers the acyl group to the N-terminus of glycine. GLYATL2 conjugates numerous substrates, like arachidonoyl-CoA and saturated medium and longchain acyl-CoAs ranging from chain-length C8:0-CoA to C18:0-CoA, to form a variety of N-acylglycines. GLYATL2 also shows a preference for monounsaturated fatty acid oleoyl-CoA (C18:1-CoA) as an acyl donor.

Glycinin Ara h 3 is a seed storage protein, 11 S globulin and trypsin inhibitor from peanut. Each subunit of the hexamer is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond. Ara h 3 and Ara h 4 are isoforms. Glycinin is the source of sulfur-containing amino acids in seed meals and it exists in the seeds of many leguminous and non-leguminous plants.

GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

Granulocyte Macrophage Colony Stimulating Factor (GM-CSF) was first characterized as a growth factor that supports the in-vitro colony formation of granulocytes-macrophages progenitor cells. It is a pleiotropic cytokine and a member of a family of endogenous cytokines of the hematopoietic system. GM-CSF is produced as a response to immune or inflammatory stimuli by activated cells of the hematopoietic system such as T cells, B cells, macrophages, mast cells and also fibroblasts and alveolar epithelial cells. It plays an important role in regulating the proliferation, differentiation, survival and activation of hematopoietic cells such as granulocytes and monocytes ,neutrophiles, basophiles and eosonophoiles, erythroid cells, megakaryocytes and T cells.
Human and mouse GM-CSF have about 56% homology and are species specific. Human GM-CSF is not active on mouse cells and vice versa. It is active on canine and feline cells.
GMCSF is 144 amino acids, 22kDa glycoprotein. It is composed of four bundles alpha helices. Its receptor is heterodimers with a ligand-specific alpha subunit and a betac subunit that is shared with the interleukin IL-3 and IL-5 receptors. This unusual form of receptor assembly likely applies also to IL-3 and IL-5 receptors. Cross-linking the two receptor subunits is required for receptor activation and signaling .
GMCSF has been shown to be involved in maturation, mobilization and antigen presentation of myeloid dentritic cells (DCs) in-vivo or ex-vivo. This function promotes Th1 immune responses, cytotoxcity, anti-angiogenesis as well as allergic inflammation, and the development of autoimmunity. Therefore GMCSF can be used in immunotherapy for the treatment of immune suppressed and immune-compromised patients as well as in veterinary medicine for the same purpose. GM-CSF is also important in regulation of embryo development and pregnancy and specifically in embryo implantation and subsequent development .

GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes. Granulocyte Macrophage Colony Stimulating Factor is a potent species-specific growth factor produced by a variety of cell types including T cells, B cells, macrophages, mast cells and endothelial cells. GM-CSF is produced in response to cytokine or immune stimulation and has been shown to stimulate the proliferation, maturation and function of hematopoietic cells.

GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.

GMCSF is a cytokine that controls the production, differentiation, and function of granulocytes and macrophages. The active form of the protein is found extracellularly as a homodimer. This gene has been localized to a cluster of related genes at chromosome region 5q31, which is known to be associated with interstitial deletions in the 5q- syndrome and acute myelogenous leukemia. Other genes in the cluster include those encoding interleukins 4, 5, and 13.
GM-CSF stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.