Human ALPP(Alkaline Phosphatase, Placental) ELISA Kit

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Alkaline Phosphatase, Placental (ALPP) in serum, plasma, tissue homogenates and other biological fluids.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Alkaline Phosphatase, Placental (ALPP) in serum, plasma, tissue homogenates and other biological fluids.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Alkaline Phosphatase, Placental (ALPP) in serum, plasma, tissue homogenates and other biological fluids.

Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Alkaline Phosphatase, Placental (ALPP) in serum, plasma, tissue homogenates and other biological fluids.

Description: Enzyme-linked immunosorbent assay based on the Double-antibody Sandwich method for detection of Human Alkaline Phosphatase, Placental (ALPP) in samples from Serum, plasma, tissue homogenates and other biological fluids with no significant corss-reactivity with analogues from other species.

Description: Recombinant Rat Alkaline Phosphatase, Placental expressed in: E.coli

Description: Reacts with a 70kDa membrane-bound isozyme (Regan and Nagao type) of placental Alkaline Phosphatase (PLAP) occurring in the placenta during the 3rd trimester of gestation. It is highly specific for PLAP and shows no cross-reaction with other isozymes of alkaline phosphatase. Anti-PLAP reacts with germ cell tumors and can discriminate between these and other neoplasms. Somatic neoplasms e.g. breast, gastrointestinal, prostatic, and urinary cancers may also immunoreact with antibodies to PLAP. Anti-PLAP positivity in conjunction with anti-keratin negativity favors seminoma over carcinoma. Germ cell tumors are usually anti-keratin positive, but they regularly fail to stain with anti-EMA, whereas most carcinomas stain with anti-EMA. Anti-PLAP has been useful in the diagnosis of gestational trophoblastic disease.

Description: Reacts with a 70kDa membrane-bound isozyme (Regan and Nagao type) of placental Alkaline Phosphatase (PLAP) occurring in the placenta during the 3rd trimester of gestation. It is highly specific for PLAP and shows no cross-reaction with other isozymes of alkaline phosphatase. Anti-PLAP reacts with germ cell tumors and can discriminate between these and other neoplasms. Somatic neoplasms e.g. breast, gastrointestinal, prostatic, and urinary cancers may also immunoreact with antibodies to PLAP. Anti-PLAP positivity in conjunction with anti-keratin negativity favors seminoma over carcinoma. Germ cell tumors are usually anti-keratin positive, but they regularly fail to stain with anti-EMA, whereas most carcinomas stain with anti-EMA. Anti-PLAP has been useful in the diagnosis of gestational trophoblastic disease.

Description: Reacts with a 70kDa membrane-bound isozyme (Regan and Nagao type) of placental Alkaline Phosphatase (PLAP) occurring in the placenta during the 3rd trimester of gestation. It is highly specific for PLAP and shows no cross-reaction with other isozymes of alkaline phosphatase. Anti-PLAP reacts with germ cell tumors and can discriminate between these and other neoplasms. Somatic neoplasms e.g. breast, gastrointestinal, prostatic, and urinary cancers may also immunoreact with antibodies to PLAP. Anti-PLAP positivity in conjunction with anti-keratin negativity favors seminoma over carcinoma. Germ cell tumors are usually anti-keratin positive, but they regularly fail to stain with anti-EMA, whereas most carcinomas stain with anti-EMA. Anti-PLAP has been useful in the diagnosis of gestational trophoblastic disease.

Description: Reacts with a 70kDa membrane-bound isozyme (Regan and Nagao type) of placental Alkaline Phosphatase (PLAP) occurring in the placenta during the 3rd trimester of gestation. It is highly specific for PLAP and shows no cross-reaction with other isozymes of alkaline phosphatase. Anti-PLAP reacts with germ cell tumors and can discriminate between these and other neoplasms. Somatic neoplasms e.g. breast, gastrointestinal, prostatic, and urinary cancers may also immunoreact with antibodies to PLAP. Anti-PLAP positivity in conjunction with anti-keratin negativity favors seminoma over carcinoma. Germ cell tumors are usually anti-keratin positive, but they regularly fail to stain with anti-EMA, whereas most carcinomas stain with anti-EMA. Anti-PLAP has been useful in the diagnosis of gestational trophoblastic disease.

Description: Reacts with a 70kDa membrane-bound isozyme (Regan and Nagao type) of placental Alkaline Phosphatase (PLAP) occurring in the placenta during the 3rd trimester of gestation. It is highly specific for PLAP and shows no cross-reaction with other isozymes of alkaline phosphatase. Anti-PLAP reacts with germ cell tumors and can discriminate between these and other neoplasms. Somatic neoplasms e.g. breast, gastrointestinal, prostatic, and urinary cancers may also immunoreact with antibodies to PLAP. Anti-PLAP positivity in conjunction with anti-keratin negativity favors seminoma over carcinoma. Germ cell tumors are usually anti-keratin positive, but they regularly fail to stain with anti-EMA, whereas most carcinomas stain with anti-EMA. Anti-PLAP has been useful in the diagnosis of gestational trophoblastic disease.

Description: Reacts with a 70kDa membrane-bound isozyme (Regan and Nagao type) of placental Alkaline Phosphatase (PLAP) occurring in the placenta during the 3rd trimester of gestation. It is highly specific for PLAP and shows no cross-reaction with other isozymes of alkaline phosphatase. Anti-PLAP reacts with germ cell tumors and can discriminate between these and other neoplasms. Somatic neoplasms e.g. breast, gastrointestinal, prostatic, and urinary cancers may also immunoreact with antibodies to PLAP. Anti-PLAP positivity in conjunction with anti-keratin negativity favors seminoma over carcinoma. Germ cell tumors are usually anti-keratin positive, but they regularly fail to stain with anti-EMA, whereas most carcinomas stain with anti-EMA. Anti-PLAP has been useful in the diagnosis of gestational trophoblastic disease.

Description: Reacts with a 70kDa membrane-bound isozyme (Regan and Nagao type) of placental Alkaline Phosphatase (PLAP) occurring in the placenta during the 3rd trimester of gestation. It is highly specific for PLAP and shows no cross-reaction with other isozymes of alkaline phosphatase. Anti-PLAP reacts with germ cell tumors and can discriminate between these and other neoplasms. Somatic neoplasms e.g. breast, gastrointestinal, prostatic, and urinary cancers may also immunoreact with antibodies to PLAP. Anti-PLAP positivity in conjunction with anti-keratin negativity favors seminoma over carcinoma. Germ cell tumors are usually anti-keratin positive, but they regularly fail to stain with anti-EMA, whereas most carcinomas stain with anti-EMA. Anti-PLAP has been useful in the diagnosis of gestational trophoblastic disease.

Description: Reacts with a 70kDa membrane-bound isozyme (Regan and Nagao type) of placental Alkaline Phosphatase (PLAP) occurring in the placenta during the 3rd trimester of gestation. It is highly specific for PLAP and shows no cross-reaction with other isozymes of alkaline phosphatase. Anti-PLAP reacts with germ cell tumors and can discriminate between these and other neoplasms. Somatic neoplasms e.g. breast, gastrointestinal, prostatic, and urinary cancers may also immunoreact with antibodies to PLAP. Anti-PLAP positivity in conjunction with anti-keratin negativity favors seminoma over carcinoma. Germ cell tumors are usually anti-keratin positive, but they regularly fail to stain with anti-EMA, whereas most carcinomas stain with anti-EMA. Anti-PLAP has been useful in the diagnosis of gestational trophoblastic disease.

Description: PLAP is a tissue specific, trophoblast-derived, 70kDa, glycosyl-phosphatidylinositol (GPI)-anchored, dimeric, Zn2+ metallo glycoprotein that catalyzes the hydrolysis of phosphomonoesters into an inorganic phosphate and an alcohol. It is present in the placenta and serum of pregnant women and in high frequency in gynecological and testicular cancers and in lower frequency in other tumors. The three tissue-specific AP's in humans, PLAP, germ cell AP (GCAP) and intestinal AP, are 90-98% homologous. Non-tissue specific AP is found in kidney, liver and bone. This mAb binds equally well to all common allelic variants (S, F, FS and I) of PLAP as to AP from normal human testis. This mAb can be used both as coating as well as tracer antibody in the same ELISA to detect PLAP in serum of S, F, FS and I phenotypes.

Description: PLAP is a tissue specific, trophoblast-derived, 70kDa, glycosyl-phosphatidylinositol (GPI)-anchored, dimeric, Zn2+ metallo glycoprotein that catalyzes the hydrolysis of phosphomonoesters into an inorganic phosphate and an alcohol. It is present in the placenta and serum of pregnant women and in high frequency in gynecological and testicular cancers and in lower frequency in other tumors. The three tissue-specific AP's in humans, PLAP, germ cell AP (GCAP) and intestinal AP, are 90-98% homologous. Non-tissue specific AP is found in kidney, liver and bone. This mAb binds equally well to all common allelic variants (S, F, FS and I) of PLAP as to AP from normal human testis. This mAb can be used both as coating as well as tracer antibody in the same ELISA to detect PLAP in serum of S, F, FS and I phenotypes.

Description: PLAP is a tissue specific, trophoblast-derived, 70kDa, glycosyl-phosphatidylinositol (GPI)-anchored, dimeric, Zn2+ metallo glycoprotein that catalyzes the hydrolysis of phosphomonoesters into an inorganic phosphate and an alcohol. It is present in the placenta and serum of pregnant women and in high frequency in gynecological and testicular cancers and in lower frequency in other tumors. The three tissue-specific AP's in humans, PLAP, germ cell AP (GCAP) and intestinal AP, are 90-98% homologous. Non-tissue specific AP is found in kidney, liver and bone. This mAb binds equally well to all common allelic variants (S, F, FS and I) of PLAP as to AP from normal human testis. This mAb can be used both as coating as well as tracer antibody in the same ELISA to detect PLAP in serum of S, F, FS and I phenotypes.

Description: PLAP is a tissue specific, trophoblast-derived, 70kDa, glycosyl-phosphatidylinositol (GPI)-anchored, dimeric, Zn2+ metallo-glycoprotein that catalyzes the hydrolysis of phosphomonoesters into an inorganic phosphate and an alcohol. It is present in the placenta and serum of pregnant women and in high frequency in gynecological and testicular cancers and in lower frequency in other tumors. The three tissue-specific AP's in humans, PLAP, germ cell AP (GCAP) and intestinal AP, are 90-98% homologous. Non-tissue specific AP is found in kidney, liver and bone. This mAb binds equally well to all common allelic variants (S, F, FS and I) of PLAP and to some variants of AP from normal human testis. This mAb can be used as tracer antibody in ELISA to detect PLAP in serum of S, F, FS and I phenotypes.

Description: PLAP is a tissue specific, trophoblast-derived, 70kDa, glycosyl-phosphatidylinositol (GPI)-anchored, dimeric, Zn2+ metallo-glycoprotein that catalyzes the hydrolysis of phosphomonoesters into an inorganic phosphate and an alcohol. It is present in the placenta and serum of pregnant women and in high frequency in gynecological and testicular cancers and in lower frequency in other tumors. The three tissue-specific AP's in humans, PLAP, germ cell AP (GCAP) and intestinal AP, are 90-98% homologous. Non-tissue specific AP is found in kidney, liver and bone. This mAb binds equally well to all common allelic variants (S, F, FS and I) of PLAP and to some variants of AP from normal human testis. This mAb can be used as tracer antibody in ELISA to detect PLAP in serum of S, F, FS and I phenotypes.

Description: PLAP is a tissue specific, trophoblast-derived, 70kDa, glycosyl-phosphatidylinositol (GPI)-anchored, dimeric, Zn2+ metallo-glycoprotein that catalyzes the hydrolysis of phosphomonoesters into an inorganic phosphate and an alcohol. It is present in the placenta and serum of pregnant women and in high frequency in gynecological and testicular cancers and in lower frequency in other tumors. The three tissue-specific AP's in humans, PLAP, germ cell AP (GCAP) and intestinal AP, are 90-98% homologous. Non-tissue specific AP is found in kidney, liver and bone. This mAb binds equally well to all common allelic variants (S, F, FS and I) of PLAP and to some variants of AP from normal human testis. This mAb can be used as tracer antibody in ELISA to detect PLAP in serum of S, F, FS and I phenotypes.

Description: Reacts with a 70kDa membrane-bound isozyme (Regan and Nagao type) of placental Alkaline Phosphatase (PLAP) occurring in the placenta during the 3rd trimester of gestation. It is highly specific for PLAP and shows no cross-reaction with other isozymes of alkaline phosphatase. Anti-PLAP reacts with germ cell tumors and can discriminate between these and other neoplasms. Somatic neoplasms e.g. breast, gastrointestinal, prostatic, and urinary cancers may also immunoreact with antibodies to PLAP. Anti-PLAP positivity in conjunction with anti-keratin negativity favors seminoma over carcinoma. Germ cell tumors are usually anti-keratin positive, but they regularly fail to stain with anti-EMA, whereas most carcinomas stain with anti-EMA. Anti-PLAP has been useful in the diagnosis of gestational trophoblastic disease.

Description: Reacts with a 70kDa membrane-bound isozyme (Regan and Nagao type) of placental Alkaline Phosphatase (PLAP) occurring in the placenta during the 3rd trimester of gestation. It is highly specific for PLAP and shows no cross-reaction with other isozymes of alkaline phosphatase. Anti-PLAP reacts with germ cell tumors and can discriminate between these and other neoplasms. Somatic neoplasms e.g. breast, gastrointestinal, prostatic, and urinary cancers may also immunoreact with antibodies to PLAP. Anti-PLAP positivity in conjunction with anti-keratin negativity favors seminoma over carcinoma. Germ cell tumors are usually anti-keratin positive, but they regularly fail to stain with anti-EMA, whereas most carcinomas stain with anti-EMA. Anti-PLAP has been useful in the diagnosis of gestational trophoblastic disease.

Description: Reacts with a 70kDa membrane-bound isozyme (Regan and Nagao type) of placental Alkaline Phosphatase (PLAP) occurring in the placenta during the 3rd trimester of gestation. It is highly specific for PLAP and shows no cross-reaction with other isozymes of alkaline phosphatase. Anti-PLAP reacts with germ cell tumors and can discriminate between these and other neoplasms. Somatic neoplasms e.g. breast, gastrointestinal, prostatic, and urinary cancers may also immunoreact with antibodies to PLAP. Anti-PLAP positivity in conjunction with anti-keratin negativity favors seminoma over carcinoma. Germ cell tumors are usually anti-keratin positive, but they regularly fail to stain with anti-EMA, whereas most carcinomas stain with anti-EMA. Anti-PLAP has been useful in the diagnosis of gestational trophoblastic disease.

Description: Reacts with a 70kDa membrane-bound isozyme (Regan and Nagao type) of placental Alkaline Phosphatase (PLAP) occurring in the placenta during the 3rd trimester of gestation. It is highly specific for PLAP and shows no cross-reaction with other isozymes of alkaline phosphatase. Anti-PLAP reacts with germ cell tumors and can discriminate between these and other neoplasms. Somatic neoplasms e.g. breast, gastrointestinal, prostatic, and urinary cancers may also immunoreact with antibodies to PLAP. Anti-PLAP positivity in conjunction with anti-keratin negativity favors seminoma over carcinoma. Germ cell tumors are usually anti-keratin positive, but they regularly fail to stain with anti-EMA, whereas most carcinomas stain with anti-EMA. Anti-PLAP has been useful in the diagnosis of gestational trophoblastic disease.

Description: There are at least four distinct but related alkaline phosphatases: intestinal, placental, placental-like, and liver/bone/kidney (tissue non-specific). The first three are located together on chromosome 2, while the tissue non-specific form is located on chromosome 1. The product of this gene is a membrane bound glycosylated enzyme that is not expressed in any particular tissue and is, therefore, referred to as the tissue-nonspecific form of the enzyme. The exact physiological function of the alkaline phosphatases is not known. A proposed function of this form of the enzyme is matrix mineralization; however, mice that lack a functional form of this enzyme show normal skeletal development. This enzyme has been linked directly to hypo-phosphatasia, a disorder that is characterized by hypercalcemia and includes skeletal defects. The character of this disorder can vary, however, depending on the specific mutation since this determines age of onset and severity of symptoms. Alternatively spliced transcript variants, which encode the same protein, have been identified for this gene.

Description: There are at least four distinct but related alkaline phosphatases: intestinal, placental, placental-like, and liver/bone/kidney (tissue non-specific). The first three are located together on chromosome 2, while the tissue non-specific form is located on chromosome 1. The product of this gene is a membrane bound glycosylated enzyme that is not expressed in any particular tissue and is, therefore, referred to as the tissue-nonspecific form of the enzyme. The exact physiological function of the alkaline phosphatases is not known. A proposed function of this form of the enzyme is matrix mineralization; however, mice that lack a functional form of this enzyme show normal skeletal development. This enzyme has been linked directly to hypo-phosphatasia, a disorder that is characterized by hypercalcemia and includes skeletal defects. The character of this disorder can vary, however, depending on the specific mutation since this determines age of onset and severity of symptoms. Alternatively spliced transcript variants, which encode the same protein, have been identified for this gene.

Description: There are at least four distinct but related alkaline phosphatases: intestinal, placental, placental-like, and liver/bone/kidney (tissue non-specific). The first three are located together on chromosome 2, while the tissue non-specific form is located on chromosome 1. The product of this gene is a membrane bound glycosylated enzyme that is not expressed in any particular tissue and is, therefore, referred to as the tissue-nonspecific form of the enzyme. The exact physiological function of the alkaline phosphatases is not known. A proposed function of this form of the enzyme is matrix mineralization; however, mice that lack a functional form of this enzyme show normal skeletal development. This enzyme has been linked directly to hypo-phosphatasia, a disorder that is characterized by hypercalcemia and includes skeletal defects. The character of this disorder can vary, however, depending on the specific mutation since this determines age of onset and severity of symptoms. Alternatively spliced transcript variants, which encode the same protein, have been identified for this gene.

Description: There are at least four distinct but related alkaline phosphatases: intestinal, placental, placental-like, and liver/bone/kidney (tissue non-specific). The first three are located together on chromosome 2, while the tissue non-specific form is located on chromosome 1. The product of this gene is a membrane bound glycosylated enzyme that is not expressed in any particular tissue and is, therefore, referred to as the tissue-nonspecific form of the enzyme. The exact physiological function of the alkaline phosphatases is not known. A proposed function of this form of the enzyme is matrix mineralization; however, mice that lack a functional form of this enzyme show normal skeletal development. This enzyme has been linked directly to hypo-phosphatasia, a disorder that is characterized by hypercalcemia and includes skeletal defects. The character of this disorder can vary, however, depending on the specific mutation since this determines age of onset and severity of symptoms. Alternatively spliced transcript variants, which encode the same protein, have been identified for this gene.

Description: PLAP is a tissue specific, trophoblast-derived, 70kDa, glycosyl-phosphatidylinositol (GPI)-anchored, dimeric, Zn2+ metallo-glycoprotein that catalyzes the hydrolysis of phosphomonoesters into an inorganic phosphate and an alcohol. It is present in the placenta and serum of pregnant women and in high frequency in gynecological and testicular cancers and in lower frequency in other tumors. The three tissue-specific AP's in humans, PLAP, germ cell AP (GCAP) and intestinal AP, are 90-98% homologous. Non-tissue specific AP is found in kidney, liver and bone. This mAb binds equally well to all common allelic variants (S, F, FS and I) of PLAP and to some variants of AP from normal human testis. This mAb can be used as tracer antibody in ELISA to detect PLAP in serum of S, F, FS and I phenotypes.

Description: PLAP is a tissue specific, trophoblast-derived, 70kDa, glycosyl-phosphatidylinositol (GPI)-anchored, dimeric, Zn2+ metallo-glycoprotein that catalyzes the hydrolysis of phosphomonoesters into an inorganic phosphate and an alcohol. It is present in the placenta and serum of pregnant women and in high frequency in gynecological and testicular cancers and in lower frequency in other tumors. The three tissue-specific AP's in humans, PLAP, germ cell AP (GCAP) and intestinal AP, are 90-98% homologous. Non-tissue specific AP is found in kidney, liver and bone. This mAb binds equally well to all common allelic variants (S, F, FS and I) of PLAP and to some variants of AP from normal human testis. This mAb can be used as tracer antibody in ELISA to detect PLAP in serum of S, F, FS and I phenotypes.

Description: PLAP is a tissue specific, trophoblast-derived, 70kDa, glycosyl-phosphatidylinositol (GPI)-anchored, dimeric, Zn2+ metallo-glycoprotein that catalyzes the hydrolysis of phosphomonoesters into an inorganic phosphate and an alcohol. It is present in the placenta and serum of pregnant women and in high frequency in gynecological and testicular cancers and in lower frequency in other tumors. The three tissue-specific AP's in humans, PLAP, germ cell AP (GCAP) and intestinal AP, are 90-98% homologous. Non-tissue specific AP is found in kidney, liver and bone. This mAb binds equally well to all common allelic variants (S, F, FS and I) of PLAP and to some variants of AP from normal human testis. This mAb can be used as tracer antibody in ELISA to detect PLAP in serum of S, F, FS and I phenotypes.

Description: PLAP is a tissue specific, trophoblast-derived, 70kDa, glycosyl-phosphatidylinositol (GPI)-anchored, dimeric, Zn2+ metallo-glycoprotein that catalyzes the hydrolysis of phosphomonoesters into an inorganic phosphate and an alcohol. It is present in the placenta and serum of pregnant women and in high frequency in gynecological and testicular cancers and in lower frequency in other tumors. The three tissue-specific AP's in humans, PLAP, germ cell AP (GCAP) and intestinal AP, are 90-98% homologous. Non-tissue specific AP is found in kidney, liver and bone. This mAb binds equally well to all common allelic variants (S, F, FS and I) of PLAP and to some variants of AP from normal human testis. This mAb can be used as tracer antibody in ELISA to detect PLAP in serum of S, F, FS and I phenotypes.

Description: Reacts with a 70kDa membrane-bound isozyme (Regan and Nagao type) of Placental Alkaline Phosphatase (PLAP) occurring in the placenta during the 3rd trimester of gestation. Anti-PLAP reacts with germ cell tumors and can discriminate between these and other neoplasms. Somatic neoplasms e.g. breast, gastrointestinal, prostatic, and urinary cancers may also immunoreact with antibodies to PLAP. Anti-PLAP positivity in conjunction with anti-keratin negativity favors seminoma over carcinoma. Germ cell tumors are usually anti-keratin positive, but they regularly fail to stain with anti-EMA, whereas most carcinomas stain with anti-EMA. Anti-PLAP has been useful in the diagnosis of gestational trophoblastic disease.

Description: Reacts with a 70kDa membrane-bound isozyme (Regan and Nagao type) of Placental Alkaline Phosphatase (PLAP) occurring in the placenta during the 3rd trimester of gestation. Anti-PLAP reacts with germ cell tumors and can discriminate between these and other neoplasms. Somatic neoplasms e.g. breast, gastrointestinal, prostatic, and urinary cancers may also immunoreact with antibodies to PLAP. Anti-PLAP positivity in conjunction with anti-keratin negativity favors seminoma over carcinoma. Germ cell tumors are usually anti-keratin positive, but they regularly fail to stain with anti-EMA, whereas most carcinomas stain with anti-EMA. Anti-PLAP has been useful in the diagnosis of gestational trophoblastic disease.

Description: Reacts with a 70kDa membrane-bound isozyme (Regan and Nagao type) of Placental Alkaline Phosphatase (PLAP) occurring in the placenta during the 3rd trimester of gestation. Anti-PLAP reacts with germ cell tumors and can discriminate between these and other neoplasms. Somatic neoplasms e.g. breast, gastrointestinal, prostatic, and urinary cancers may also immunoreact with antibodies to PLAP. Anti-PLAP positivity in conjunction with anti-keratin negativity favors seminoma over carcinoma. Germ cell tumors are usually anti-keratin positive, but they regularly fail to stain with anti-EMA, whereas most carcinomas stain with anti-EMA. Anti-PLAP has been useful in the diagnosis of gestational trophoblastic disease.

Description: Reacts with a 70kDa membrane-bound isozyme (Regan and Nagao type) of Placental Alkaline Phosphatase (PLAP) occurring in the placenta during the 3rd trimester of gestation. Anti-PLAP reacts with germ cell tumors and can discriminate between these and other neoplasms. Somatic neoplasms e.g. breast, gastrointestinal, prostatic, and urinary cancers may also immunoreact with antibodies to PLAP. Anti-PLAP positivity in conjunction with anti-keratin negativity favors seminoma over carcinoma. Germ cell tumors are usually anti-keratin positive, but they regularly fail to stain with anti-EMA, whereas most carcinomas stain with anti-EMA. Anti-PLAP has been useful in the diagnosis of gestational trophoblastic disease.

Description: Alkaline phosphatase, placental type also known as placental alkaline phosphatase (PLAP) is an allosteric enzyme that in humans is encoded by the ALPP gene. The protein encoded by this gene is an alkaline phosphatase, a metalloenzyme that catalyzes the hydrolysis of phosphoric acid monoesters. It belongs to a multigene family composed of four alkaline phosphatase isoenzymes. The enzyme functions as a homodimer and has a catalytic site containing one magnesium and two zinc ions, which are required for its enzymatic function. The protein is primarily expressed in placental and endometrial tissue; however, strong ectopic expression has been detected in ovarian adenocarcinoma, serous cystadenocarcinoma, and other ovarian cancer cells.

Description: Recombinant Human Alkaline phosphatase, placental type(ALPP),partial expressed in E.coli

Description: Recombinant Human Alkaline phosphatase, placental type(ALPP),partial expressed in Baculovirus

Description: A sandwich ELISA kit for detection of Alkaline Phosphatase, Placental from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids.

Description: Method of detection: Double Antibody, Sandwich ELISA;Reacts with: Homo sapiens;Sensitivity: 9.375pg/ml

Description: A sandwich ELISA kit for quantitative measurement of Human PLAP/ALPP (Placental Alkaline Phosphatase) in samples from Serum, Plasma, Cell supernatant