The role of soluble urokinase plasminogen activator receptor (suPAR) in the diagnostics of diabetic foot infection.
Background: To investigate the role of soluble urokinase plasminogen activator receptor (Supar) in the diagnosis of diabetic foot infection and to determine whether it is superior to other markers of infection such as leukocytes, neutrophils, erythrocyte sedimentation rate, c-reactive protein and procalcitonin.
Methods: This prospective study comprised of four groups: group 1, healthy volunteers (n = 38); Group 2 patients without diabetic foot ulcers (n = 40); Group 3, diabetic patients with foot ulcers that are not infected (n = 33); and Group 4, patients with diabetic foot infections (n = 48). In each group, leukocytes, neutrophils, erythrocyte sedimentation rate, c-reactive protein and procalcitonin and Supar level checked. The results were then statistically compared. Additionally, patients in Group 4 are further divided according to their infection is mild, moderate, and severe. Also osteomyelitis evaluated in Group 4 and statistics compared.
Results: All markers of infection was significantly higher in the group of 4 patients than those in the other three groups (p <0.05). Similarly, all markers of infection in the group of severe diabetic foot infection were statistically higher than the group of mild diabetic foot infection (p <0.05); However, only Supar and the erythrocyte sedimentation rate was significantly higher in cases with osteomyelitis (p <0.05).
In a receiver operating characteristic analysis, the optimal cut-off value for Supar determined to be 2.8 ng / ml, and the sensitivity and specificity above this value was 95.8% and 82.8%, respectively.
Conclusions: This study shows that Supar power is used as a support diagnostic methods for the diagnosis of diabetic foot infection.
The role of soluble urokinase plasminogen activator receptor (suPAR) in the diagnostics of diabetic foot infection.
Expression of Urokinase Plasminogen Activator reverse Established Lung Fibrosis.
Disorders plasminogen activation (PA) is causally related to the development of lung fibrosis. previous studies have shown that PA is enhanced in limiting the severity of lung scarring following injury and in vitro studies suggest that PA promotes matrix degradation and fibroblast apoptosis. These findings led us to hypothesize that the increased PA in vivo models will improve the resolution of pulmonary fibrosis was established in conjunction with an increase in myofibroblast apoptosis.
Transgenic C57BL / 6 mice with lung-specific induced urokinase plasminogen activator (uPA) expression doxycycline or treated littermate controls (day 0) with bleomycin or saline. Doxycycline started on day 1, 9, 14, or 21. Lung fibrosis, stiffness, apoptosis, epithelial barrier integrity, and inflammation was assessed. Protection of fibrosis with uPA upregulation of day 1 to day 28 was associated with reduced parenchymal stiffness as determined by atomic force microscopy.
Initiation of uPA expression begins at the end of inflammation or fibrosis initial phase of reduced stiffness and fibrosis on day 28. Induction of uPA activity in mice with established fibrosis lung collagen reduction and stiffness while increasing lung myofibroblast apoptosis. Upregulation of uPA not alter lung inflammation but are associated with increased epithelial cell homeostasis. Returns intrapulmonary PA activity decreased lung fibrogenesis and improve the resolution of established fibrosis of the lungs. This resolution PA-mediated myofibroblast apoptosis is associated with increased and improved epithelial cell homeostasis.
Description: Caldesmon is an actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity). [UniProt]
Description: Caldesmon is an actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity). [UniProt]
Description: Caldesmon is an actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity). [UniProt]
Description: Caldesmon is an actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity). [UniProt]
Description: Recognizes a protein of 150kDa, which is identified as the high molecular weight variant of Caldesmon. Two closely related variants of human caldesmon have been identified which are different in their electrophoretic mobility and cellular distribution. The h-caldesmon variant (120-150kDa) is predominantly expressed in smooth muscle whereas l-caldesmon (70-80kDa) is found in non- muscle tissue and cells. Neither of the two variants has been detected in skeletal muscle. Caldesmon is a developmentally regulated protein involved in smooth muscle and non-muscle contraction.
Description: Recognizes a protein of 150kDa, which is identified as the high molecular weight variant of Caldesmon. Two closely related variants of human caldesmon have been identified which are different in their electrophoretic mobility and cellular distribution. The h-caldesmon variant (120-150kDa) is predominantly expressed in smooth muscle whereas l-caldesmon (70-80kDa) is found in non- muscle tissue and cells. Neither of the two variants has been detected in skeletal muscle. Caldesmon is a developmentally regulated protein involved in smooth muscle and non-muscle contraction.
Description: Recognizes a protein of 150kDa, which is identified as the high molecular weight variant of Caldesmon. Two closely related variants of human caldesmon have been identified which are different in their electrophoretic mobility and cellular distribution. The h-caldesmon variant (120-150kDa) is predominantly expressed in smooth muscle whereas l-caldesmon (70-80kDa) is found in non- muscle tissue and cells. Neither of the two variants has been detected in skeletal muscle. Caldesmon is a developmentally regulated protein involved in smooth muscle and non-muscle contraction.
Description: Recognizes a protein of 150kDa, which is identified as the high molecular weight variant of Caldesmon. Two closely related variants of human caldesmon have been identified which are different in their electrophoretic mobility and cellular distribution. The h-caldesmon variant (120-150kDa) is predominantly expressed in smooth muscle whereas l-caldesmon (70-80kDa) is found in non- muscle tissue and cells. Neither of the two variants has been detected in skeletal muscle. Caldesmon is a developmentally regulated protein involved in smooth muscle and non-muscle contraction.
Description: Recognizes a protein of 150kDa, which is identified as the high molecular weight variant of Caldesmon. Two closely related variants of human caldesmon have been identified which are different in their electrophoretic mobility and cellular distribution. The h-caldesmon variant (120-150kDa) is predominantly expressed in smooth muscle whereas l-caldesmon (70-80kDa) is found in non- muscle tissue and cells. Neither of the two variants has been detected in skeletal muscle. This mAb recognizes only the 150kDa variant (h-caldesmon) in Western blots of human aortic media extracts and is unreactive with fibroblast extracts from cultivated human foreskin. Caldesmon is a developmentally regulated protein involved in smooth muscle and non-muscle contraction.
Description: Recognizes a protein of 150kDa, which is identified as the high molecular weight variant of Caldesmon. Two closely related variants of human caldesmon have been identified which are different in their electrophoretic mobility and cellular distribution. The h-caldesmon variant (120-150kDa) is predominantly expressed in smooth muscle whereas l-caldesmon (70-80kDa) is found in non- muscle tissue and cells. Neither of the two variants has been detected in skeletal muscle. This mAb recognizes only the 150kDa variant (h-caldesmon) in Western blots of human aortic media extracts and is unreactive with fibroblast extracts from cultivated human foreskin. Caldesmon is a developmentally regulated protein involved in smooth muscle and non-muscle contraction.
Description: Recognizes a protein of 150kDa, which is identified as the high molecular weight variant of Caldesmon. Two closely related variants of human caldesmon have been identified which are different in their electrophoretic mobility and cellular distribution. The h-caldesmon variant (120-150kDa) is predominantly expressed in smooth muscle whereas l-caldesmon (70-80kDa) is found in non- muscle tissue and cells. Neither of the two variants has been detected in skeletal muscle. This mAb recognizes only the 150kDa variant (h-caldesmon) in Western blots of human aortic media extracts and is unreactive with fibroblast extracts from cultivated human foreskin. Caldesmon is a developmentally regulated protein involved in smooth muscle and non-muscle contraction.
Description: Recognizes a protein of 150kDa, which is identified as the high molecular weight variant of Caldesmon. Two closely related variants of human caldesmon have been identified which are different in their electrophoretic mobility and cellular distribution. The h-caldesmon variant (120-150kDa) is predominantly expressed in smooth muscle whereas l-caldesmon (70-80kDa) is found in non- muscle tissue and cells. Neither of the two variants has been detected in skeletal muscle. This mAb recognizes only the 150kDa variant (h-caldesmon) in Western blots of human aortic media extracts and is unreactive with fibroblast extracts from cultivated human foreskin. Caldesmon is a developmentally regulated protein involved in smooth muscle and non-muscle contraction.
Description: Caldesmon is an actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity). [UniProt]
Description: Caldesmon is an actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity). [UniProt]
Description: Caldesmon is an actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity). [UniProt]
Description: Caldesmon is an actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity). [UniProt]
Description: Caldesmon is an actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity). [UniProt]
Description: Caldesmon is an actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity). [UniProt]
Description: Caldesmon is an actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity). [UniProt]
Description: Caldesmon is an actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, inhibits the actomyosin ATPase by binding to F-actin. This inhibition is attenuated by calcium-calmodulin and is potentiated by tropomyosin. Interacts with actin, myosin, two molecules of tropomyosin and with calmodulin. Also play an essential role during cellular mitosis and receptor capping. Involved in Schwann cell migration during peripheral nerve regeneration (By similarity). [UniProt]
Description: Caldesmon (CAD, CALD, CALD1) is an actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). [UniProt]
Description: Caldesmon (CAD, CALD, CALD1) is an actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). [UniProt]
Description: Caldesmon (CAD, CALD, CALD1) is an actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). [UniProt]
Description: Caldesmon (CAD, CALD, CALD1) is an actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). [UniProt]
Description: Recognizes a protein of 150kDa, which is identified as the high molecular weight variant of Caldesmon. Two closely related variants of human caldesmon have been identified which are different in their electrophoretic mobility and cellular distribution. The h-caldesmon variant (120-150kDa) is predominantly expressed in smooth muscle whereas l-caldesmon (70-80kDa) is found in non- muscle tissue and cells. Neither of the two variants has been detected in skeletal muscle. This MAb recognizes only the 150kDa variant (h-caldesmon) in Western blots of human aortic media extracts and is unreactive with fibroblast extracts from cultivated human foreskin. Caldesmon is a developmentally regulated protein involved in smooth muscle and non-muscle contraction.
Description: Recognizes a protein of 150kDa, which is identified as the high molecular weight variant of Caldesmon. Two closely related variants of human caldesmon have been identified which are different in their electrophoretic mobility and cellular distribution. The h-caldesmon variant (120-150kDa) is predominantly expressed in smooth muscle whereas l-caldesmon (70-80kDa) is found in non- muscle tissue and cells. Neither of the two variants has been detected in skeletal muscle. This MAb recognizes only the 150kDa variant (h-caldesmon) in Western blots of human aortic media extracts and is unreactive with fibroblast extracts from cultivated human foreskin. Caldesmon is a developmentally regulated protein involved in smooth muscle and non-muscle contraction.
Description: Recognizes a protein of 150kDa, which is identified as the high molecular weight variant of Caldesmon. Two closely related variants of human caldesmon have been identified which are different in their electrophoretic mobility and cellular distribution. The h-caldesmon variant (120-150kDa) is predominantly expressed in smooth muscle whereas l-caldesmon (70-80kDa) is found in non- muscle tissue and cells. Neither of the two variants has been detected in skeletal muscle. This MAb recognizes only the 150kDa variant (h-caldesmon) in Western blots of human aortic media extracts and is unreactive with fibroblast extracts from cultivated human foreskin. Caldesmon is a developmentally regulated protein involved in smooth muscle and non-muscle contraction.
Description: Two closely related variants of human caldesmon have been identified which are different in their electrophoretic mobility and cellular distribution. The h-caldesmon variant (120-150kDa) is predominantly expressed in smooth muscle whereas l-caldesmon (70-80kDa) is found in non- muscle tissue and cells. Neither of the two variants has been detected in skeletal muscle. Caldesmon is a developmentally regulated protein involved in smooth muscle and non-muscle contraction.
Description: Two closely related variants of human caldesmon have been identified which are different in their electrophoretic mobility and cellular distribution. The h-caldesmon variant (120-150kDa) is predominantly expressed in smooth muscle whereas l-caldesmon (70-80kDa) is found in non- muscle tissue and cells. Neither of the two variants has been detected in skeletal muscle. Caldesmon is a developmentally regulated protein involved in smooth muscle and non-muscle contraction.
Description: Two closely related variants of human caldesmon have been identified which are different in their electrophoretic mobility and cellular distribution. The h-caldesmon variant (120-150kDa) is predominantly expressed in smooth muscle whereas l-caldesmon (70-80kDa) is found in non- muscle tissue and cells. Neither of the two variants has been detected in skeletal muscle. Caldesmon is a developmentally regulated protein involved in smooth muscle and non-muscle contraction.
Description: Two closely related variants of human caldesmon have been identified which are different in their electrophoretic mobility and cellular distribution. The h-caldesmon variant (120-150kDa) is predominantly expressed in smooth muscle whereas l-caldesmon (70-80kDa) is found in non- muscle tissue and cells. Neither of the two variants has been detected in skeletal muscle. Caldesmon is a developmentally regulated protein involved in smooth muscle and non-muscle contraction.
Description: Recognizes a protein of 150kDa, which is identified as the high molecular weight variant of Caldesmon. Two closely related variants of human caldesmon have been identified which are different in their electrophoretic mobility and cellular distribution. The h-caldesmon variant (120-150kDa) is predominantly expressed in smooth muscle whereas l-caldesmon (70-80kDa) is found in non- muscle tissue and cells. Neither of the two variants has been detected in skeletal muscle. This MAb recognizes only the 150kDa variant (h-caldesmon) in Western blots of human aortic media extracts and is unreactive with fibroblast extracts from cultivated human foreskin. Caldesmon is a developmentally regulated protein involved in smooth muscle and non-muscle contraction.
Description: Recognizes a protein of 150kDa, which is identified as the high molecular weight variant of Caldesmon. Two closely related variants of human caldesmon have been identified which are different in their electrophoretic mobility and cellular distribution. The h-caldesmon variant (120-150kDa) is predominantly expressed in smooth muscle whereas l-caldesmon (70-80kDa) is found in non- muscle tissue and cells. Neither of the two variants has been detected in skeletal muscle. This MAb recognizes only the 150kDa variant (h-caldesmon) in Western blots of human aortic media extracts and is unreactive with fibroblast extracts from cultivated human foreskin. Caldesmon is a developmentally regulated protein involved in smooth muscle and non-muscle contraction.
Description: Recognizes a protein of 150kDa, which is identified as the high molecular weight variant of Caldesmon. Two closely related variants of human caldesmon have been identified which are different in their electrophoretic mobility and cellular distribution. The h-caldesmon variant (120-150kDa) is predominantly expressed in smooth muscle whereas l-caldesmon (70-80kDa) is found in non- muscle tissue and cells. Neither of the two variants has been detected in skeletal muscle. This MAb recognizes only the 150kDa variant (h-caldesmon) in Western blots of human aortic media extracts and is unreactive with fibroblast extracts from cultivated human foreskin. Caldesmon is a developmentally regulated protein involved in smooth muscle and non-muscle contraction.
Description: This antibody is specific to cytokeratin 13, 14, 15 and 16. This antibody stains squamous carcinomas and adeno-squamous carcinomas but does not stain adenocarcinoma. This antibody is useful in differential staining of squamous carcinomas from adenocarcinomas and to differentiate benign and malignant tumors of prostate glands.
Description: This antibody is specific to cytokeratin 13, 14, 15 and 16. This antibody stains squamous carcinomas and adeno-squamous carcinomas but does not stain adenocarcinoma. This antibody is useful in differential staining of squamous carcinomas from adenocarcinomas and to differentiate benign and malignant tumors of prostate glands.
Description: This antibody is specific to cytokeratin 13, 14, 15 and 16. This antibody stains squamous carcinomas and adeno-squamous carcinomas but does not stain adenocarcinoma. This antibody is useful in differential staining of squamous carcinomas from adenocarcinomas and to differentiate benign and malignant tumors of prostate glands.
Description: This MAb recognizes basic (Type II or HMW) cytokeratins, which include 67kDa (CK1); 64kDa (CK3); 59kDa (CK4); 58kDa (CK5); 56kDa (CK6); 52kDa (CK8). Twenty human keratins are resolved with two-dimensional gel electrophoresis into acidic (pI 6.0) subfamilies. The acidic keratins have molecular weights (MW) of 56.5, 55, 51, 50, 50, 48, 46, 45, and 40kDa. This MAb recognizes the 65-67, 64, 59, 58, 56, and 52kDa keratins of basic subfamily. Many studies have shown the usefulness of keratins as markers in cancer research and tumor diagnosis. SPM115/SPM116 is a broad spectrum anti pan-keratin antibody cocktail, which differentiates epithelial tumors from non-epithelial tumors e.g. squamous vs. adenocarcinoma of the lung, liver carcinoma, breast cancer, and esophageal cancer.
Description: This MAb recognizes basic (Type II or HMW) cytokeratins, which include 67kDa (CK1); 64kDa (CK3); 59kDa (CK4); 58kDa (CK5); 56kDa (CK6); 52kDa (CK8). Twenty human keratins are resolved with two-dimensional gel electrophoresis into acidic (pI 6.0) subfamilies. The acidic keratins have molecular weights (MW) of 56.5, 55, 51, 50, 50, 48, 46, 45, and 40kDa. This MAb recognizes the 65-67, 64, 59, 58, 56, and 52kDa keratins of basic subfamily. Many studies have shown the usefulness of keratins as markers in cancer research and tumor diagnosis. SPM115/SPM116 is a broad spectrum anti pan-keratin antibody cocktail, which differentiates epithelial tumors from non-epithelial tumors e.g. squamous vs. adenocarcinoma of the lung, liver carcinoma, breast cancer, and esophageal cancer.
Description: This MAb recognizes basic (Type II or HMW) cytokeratins, which include 67kDa (CK1); 64kDa (CK3); 59kDa (CK4); 58kDa (CK5); 56kDa (CK6); 52kDa (CK8). Twenty human keratins are resolved with two-dimensional gel electrophoresis into acidic (pI 6.0) subfamilies. The acidic keratins have molecular weights (MW) of 56.5, 55, 51, 50, 50, 48, 46, 45, and 40kDa. This MAb recognizes the 65-67, 64, 59, 58, 56, and 52kDa keratins of basic subfamily. Many studies have shown the usefulness of keratins as markers in cancer research and tumor diagnosis. SPM115/SPM116 is a broad spectrum anti pan-keratin antibody cocktail, which differentiates epithelial tumors from non-epithelial tumors e.g. squamous vs. adenocarcinoma of the lung, liver carcinoma, breast cancer, and esophageal cancer.
Description: This MAb recognizes basic (Type II or HMW) cytokeratins, which include 67kDa (CK1); 64kDa (CK3); 59kDa (CK4); 58kDa (CK5); 56kDa (CK6); 52kDa (CK8). Twenty human keratins are resolved with two-dimensional gel electrophoresis into acidic (pI 6.0) subfamilies. The acidic keratins have molecular weights (MW) of 56.5, 55, 51, 50, 50, 48, 46, 45, and 40kDa. This MAb recognizes the 65-67, 64, 59, 58, 56, and 52kDa keratins of basic subfamily. Many studies have shown the usefulness of keratins as markers in cancer research and tumor diagnosis. SPM115/SPM116 is a broad spectrum anti pan-keratin antibody cocktail, which differentiates epithelial tumors from non-epithelial tumors e.g. squamous vs. adenocarcinoma of the lung, liver carcinoma, breast cancer, and esophageal cancer.
Description: This antibody recognizes HMW Keratin 1, 5, 10 and 14. In normal epithelia, it stains stratified epithelia, myoepithelial cells and basal cells in the prostate gland and bronchi. The HMW Cytokeratin antibody shows no reactivity with hepatocytes, pancreatic acinar cells, proximal renal tubules, or endometrial glands; there is no reactivity with cells derived from simple epithelia. Mesenchymal tumors, lymphomas, melanomas, neural tumors, and neuroendocrine tumors are negative with this mAb. It stains myoepithelial cells and has been shown to be useful in distinguishing prostate adenocarcinoma from benign prostate. It has also been useful in separating benign from malignant intraductal breast proliferations.
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These studies support the potential capacity of the lungs to scar finish in murine models.A promising molecular target for aggressive cancer urokinase receptor (Upar). A fully human, recombinant antibodies that bind Upar to form a stable compound that blocks the interaction of uPA-Upar (2G10) and internalized mainly through endocytosis shown efficacy in mouse xenograft models, triple negative breast cancer that is very aggressive (TNBC).
