You Searched For: Calcium+formate

Catalog Number: (BOSSBS-4938R-A750)

Supplier: Bioss

Description: Chemoattractant active on T-lymphocytes, monocytes, but not neutrophils. Activates the C-X-C chemokine receptor CXCR4 to induce a rapid and transient rise in the level of intracellular calcium ions and chemotaxis. Also binds to atypical chemokine receptor ACKR3, which activates the beta-arrestin pathway and acts as a scavenger receptor for SDF-1. SDF-1-beta(3-72) and SDF-1-alpha(3-67) show a reduced chemotactic activity. Binding to cell surface proteoglycans seems to inhibit formation of SDF-1-alpha(3-67) and thus to preserve activity on local sites. Acts as a positive regulator of monocyte migration and a negative regulator of monocyte adhesion via the LYN kinase. Stimulates migration of monocytes and T-lymphocytes through its receptors, CXCR4 and ACKR3, and decreases monocyte adherence to surfaces coated with ICAM-1, a ligand for beta-2 integrins. SDF1A/CXCR4 signaling axis inhibits beta-2 integrin LFA-1 mediated adhesion of monocytes to ICAM-1 through LYN kinase. Inhibits CXCR4-mediated infection by T-cell line-adapted HIV-1. Plays a protective role after myocardial infarction. Induces down-regulation and internalization of ACKR3 expressed in various cells. Has several critical functions during embryonic development; required for B-cell lymphopoiesis, myelopoiesis in bone marrow and heart ventricular septum formation.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-4938R-FITC)

Supplier: Bioss

Description: Chemoattractant active on T-lymphocytes, monocytes, but not neutrophils. Activates the C-X-C chemokine receptor CXCR4 to induce a rapid and transient rise in the level of intracellular calcium ions and chemotaxis. Also binds to atypical chemokine receptor ACKR3, which activates the beta-arrestin pathway and acts as a scavenger receptor for SDF-1. SDF-1-beta(3-72) and SDF-1-alpha(3-67) show a reduced chemotactic activity. Binding to cell surface proteoglycans seems to inhibit formation of SDF-1-alpha(3-67) and thus to preserve activity on local sites. Acts as a positive regulator of monocyte migration and a negative regulator of monocyte adhesion via the LYN kinase. Stimulates migration of monocytes and T-lymphocytes through its receptors, CXCR4 and ACKR3, and decreases monocyte adherence to surfaces coated with ICAM-1, a ligand for beta-2 integrins. SDF1A/CXCR4 signaling axis inhibits beta-2 integrin LFA-1 mediated adhesion of monocytes to ICAM-1 through LYN kinase. Inhibits CXCR4-mediated infection by T-cell line-adapted HIV-1. Plays a protective role after myocardial infarction. Induces down-regulation and internalization of ACKR3 expressed in various cells. Has several critical functions during embryonic development; required for B-cell lymphopoiesis, myelopoiesis in bone marrow and heart ventricular septum formation.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12359R-A750)

Supplier: Bioss

Description: DMP-1 is a member of the small integrin ligand N-linked glycoprotein family. It is important for the mineralization of bone and dentin. DMP-1 is expressed in bone, tooth and hypertrophic cartilage. It is synthesised by preosteoblasts and contains a large number of acidic domains. DMP-1 localizes to the nucleus of undifferentiated osteoblasts where it functions as a transcriptional regulator for osteoblast-specific gene activation and induces osteoblast differentiation. During osteoblast maturation, DMP-1 undergoes a conformational change and becomes phosphorylated by casein kinase II in response to an influx of calcium ions to the nucleus. DMP-1 is then exported to the extracellular matrix (ECM) where it regulates the nucleation of hydroxyapatite and the formation of calcified tissue. DMP-1 is proteolytically processed into N- and C-terminal fragments in the ECM of bone and dentin. The protein has also been identified in bone as a high molecular weight proteoglycan comprised of the N-terminal DMP-1 fragment and chondroitin sulfate. The loss of DMP-1 can result in hypomineralized bone.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12359R-A488)

Supplier: Bioss

Description: DMP-1 is a member of the small integrin ligand N-linked glycoprotein family. It is important for the mineralization of bone and dentin. DMP-1 is expressed in bone, tooth and hypertrophic cartilage. It is synthesized by preosteoblasts and contains a large number of acidic domains. DMP-1 localizes to the nucleus of undifferentiated osteoblasts where it functions as a transcriptional regulator for osteoblast-specific gene activation and induces osteoblast differentiation. During osteoblast maturation, DMP-1 undergoes a conformational change and becomes phosphorylated by casein kinase II in response to an influx of calcium ions to the nucleus. DMP-1 is then exported to the extracellular matrix (ECM) where it regulates the nucleation of hydroxyapatite and the formation of calcified tissue. DMP-1 is proteolytically processed into N- and C-terminal fragments in the ECM of bone and dentin. The protein has also been identified in bone as a high molecular weight proteoglycan comprised of the N-terminal DMP-1 fragment and chondroitin sulfate.The loss of DMP-1 can result in hypomineralized bone.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12359R)

Supplier: Bioss

Description: DMP-1 is a member of the small integrin ligand N-linked glycoprotein family. It is important for the mineralization of bone and dentin. DMP-1 is expressed in bone, tooth and hypertrophic cartilage. It is synthesized by preosteoblasts and contains a large number of acidic domains. DMP-1 localizes to the nucleus of undifferentiated osteoblasts where it functions as a transcriptional regulator for osteoblast-specific gene activation and induces osteoblast differentiation. During osteoblast maturation, DMP-1 undergoes a conformational change and becomes phosphorylated by casein kinase II in response to an influx of calcium ions to the nucleus. DMP-1 is then exported to the extracellular matrix (ECM) where it regulates the nucleation of hydroxyapatite and the formation of calcified tissue. DMP-1 is proteolytically processed into N- and C-terminal fragments in the ECM of bone and dentin. The protein has also been identified in bone as a high molecular weight proteoglycan comprised of the N-terminal DMP-1 fragment and chondroitin sulfate.The loss of DMP-1 can result in hypomineralized bone.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12359R-CY5)

Supplier: Bioss

Description: DMP-1 is a member of the small integrin ligand N-linked glycoprotein family. It is important for the mineralization of bone and dentin. DMP-1 is expressed in bone, tooth and hypertrophic cartilage. It is synthesized by preosteoblasts and contains a large number of acidic domains. DMP-1 localizes to the nucleus of undifferentiated osteoblasts where it functions as a transcriptional regulator for osteoblast-specific gene activation and induces osteoblast differentiation. During osteoblast maturation, DMP-1 undergoes a conformational change and becomes phosphorylated by casein kinase II in response to an influx of calcium ions to the nucleus. DMP-1 is then exported to the extracellular matrix (ECM) where it regulates the nucleation of hydroxyapatite and the formation of calcified tissue. DMP-1 is proteolytically processed into N- and C-terminal fragments in the ECM of bone and dentin. The protein has also been identified in bone as a high molecular weight proteoglycan comprised of the N-terminal DMP-1 fragment and chondroitin sulfate.The loss of DMP-1 can result in hypomineralized bone.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12359R-A555)

Supplier: Bioss

Description: DMP-1 is a member of the small integrin ligand N-linked glycoprotein family. It is important for the mineralization of bone and dentin. DMP-1 is expressed in bone, tooth and hypertrophic cartilage. It is synthesized by preosteoblasts and contains a large number of acidic domains. DMP-1 localizes to the nucleus of undifferentiated osteoblasts where it functions as a transcriptional regulator for osteoblast-specific gene activation and induces osteoblast differentiation. During osteoblast maturation, DMP-1 undergoes a conformational change and becomes phosphorylated by casein kinase II in response to an influx of calcium ions to the nucleus. DMP-1 is then exported to the extracellular matrix (ECM) where it regulates the nucleation of hydroxyapatite and the formation of calcified tissue. DMP-1 is proteolytically processed into N- and C-terminal fragments in the ECM of bone and dentin. The protein has also been identified in bone as a high molecular weight proteoglycan comprised of the N-terminal DMP-1 fragment and chondroitin sulfate.The loss of DMP-1 can result in hypomineralized bone.

UOM: 1 * 100 µl

Supplier: Biotium

Description: Recognizes a 77-85 kDa protein, identified as cellular or tissue transglutaminase II (TGase II). Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. Finally, the encoded protein is the autoantigen implicated in celiac disease. The identification of transglutaminase as the main antigen of endomysium antibodies allows a new diagnostic approach to celiac disease (CD), a genetic, immunologically mediated small bowel enteropathy that causes malabsorption. TGase II is implicated in programmed cell death, signal transduction, drug-resistance, cell growth, endocytosis, insulin secretion, cell adhesion, cataract formation, and wound healing.

Supplier: Biotium

Description: Recognizes a 77-85 kDa protein, identified as cellular or tissue transglutaminase II (TGase II). Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. Finally, the encoded protein is the autoantigen implicated in celiac disease. The identification of transglutaminase as the main antigen of endomysium antibodies allows a new diagnostic approach to celiac disease (CD), a genetic, immunologically mediated small bowel enteropathy that causes malabsorption. TGase II is implicated in programmed cell death, signal transduction, drug-resistance, cell growth, endocytosis, insulin secretion, cell adhesion, cataract formation, and wound healing.

Catalog Number: (BOSSBS-12359R-A680)

Supplier: Bioss

Description: DMP-1 is a member of the small integrin ligand N-linked glycoprotein family. It is important for the mineralization of bone and dentin. DMP-1 is expressed in bone, tooth and hypertrophic cartilage. It is synthesised by preosteoblasts and contains a large number of acidic domains. DMP-1 localizes to the nucleus of undifferentiated osteoblasts where it functions as a transcriptional regulator for osteoblast-specific gene activation and induces osteoblast differentiation. During osteoblast maturation, DMP-1 undergoes a conformational change and becomes phosphorylated by casein kinase II in response to an influx of calcium ions to the nucleus. DMP-1 is then exported to the extracellular matrix (ECM) where it regulates the nucleation of hydroxyapatite and the formation of calcified tissue. DMP-1 is proteolytically processed into N- and C-terminal fragments in the ECM of bone and dentin. The protein has also been identified in bone as a high molecular weight proteoglycan comprised of the N-terminal DMP-1 fragment and chondroitin sulfate. The loss of DMP-1 can result in hypomineralized bone.

UOM: 1 * 100 µl

Supplier: Biotium

Description: Recognizes a 77-85 kDa protein, identified as cellular or tissue transglutaminase II (TGase II). Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. Finally, the encoded protein is the autoantigen implicated in celiac disease. The identification of transglutaminase as the main antigen of endomysium antibodies allows a new diagnostic approach to celiac disease (CD), a genetic, immunologically mediated small bowel enteropathy that causes malabsorption. TGase II is implicated in programmed cell death, signal transduction, drug-resistance, cell growth, endocytosis, insulin secretion, cell adhesion, cataract formation, and wound healing.

Catalog Number: (BOSSBS-4938R-CY3)

Supplier: Bioss

Description: Chemoattractant active on T-lymphocytes, monocytes, but not neutrophils. Activates the C-X-C chemokine receptor CXCR4 to induce a rapid and transient rise in the level of intracellular calcium ions and chemotaxis. Also binds to atypical chemokine receptor ACKR3, which activates the beta-arrestin pathway and acts as a scavenger receptor for SDF-1. SDF-1-beta(3-72) and SDF-1-alpha(3-67) show a reduced chemotactic activity. Binding to cell surface proteoglycans seems to inhibit formation of SDF-1-alpha(3-67) and thus to preserve activity on local sites. Acts as a positive regulator of monocyte migration and a negative regulator of monocyte adhesion via the LYN kinase. Stimulates migration of monocytes and T-lymphocytes through its receptors, CXCR4 and ACKR3, and decreases monocyte adherence to surfaces coated with ICAM-1, a ligand for beta-2 integrins. SDF1A/CXCR4 signaling axis inhibits beta-2 integrin LFA-1 mediated adhesion of monocytes to ICAM-1 through LYN kinase. Inhibits CXCR4-mediated infection by T-cell line-adapted HIV-1. Plays a protective role after myocardial infarction. Induces down-regulation and internalization of ACKR3 expressed in various cells. Has several critical functions during embryonic development; required for B-cell lymphopoiesis, myelopoiesis in bone marrow and heart ventricular septum formation.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13059R-A647)

Supplier: Bioss

Description: Fibulin proteins contribute to normal development of elastic fiber systems in various types of organs that require elasticity, such as vasculature, lung and skin. Fibulin-4, also known as EFEMP2 (EGF-containing fibulin-like extracellular matrix protein 2), MBP1 or UPH1 is a 443 amino acid secreted protein that contains six EGF-like calcium-binding domains and belongs to the fibulin family. Expressed ubiquitously with highest expression in heart, Fibulin-4 is essential for connective tissue development and elastic fiber formation, and may also play an important role in vascular patterning and collagen biosynthesis. Defects in the gene encoding Fibulin-4 are associated with autosomal recessive cutis laxa type I (CL type I), a connective tissue disorder that is inherited in both an autosomal dominant and an autosomal recessive manner and is characterized by inelastic tissue in all affected areas of the body.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13059R-A350)

Supplier: Bioss

Description: Fibulin proteins contribute to normal development of elastic fiber systems in various types of organs that require elasticity, such as vasculature, lung and skin. Fibulin-4, also known as EFEMP2 (EGF-containing fibulin-like extracellular matrix protein 2), MBP1 or UPH1 is a 443 amino acid secreted protein that contains six EGF-like calcium-binding domains and belongs to the fibulin family. Expressed ubiquitously with highest expression in heart, Fibulin-4 is essential for connective tissue development and elastic fiber formation, and may also play an important role in vascular patterning and collagen biosynthesis. Defects in the gene encoding Fibulin-4 are associated with autosomal recessive cutis laxa type I (CL type I), a connective tissue disorder that is inherited in both an autosomal dominant and an autosomal recessive manner and is characterized by inelastic tissue in all affected areas of the body.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-12359R-FITC)

Supplier: Bioss

Description: DMP-1 is a member of the small integrin ligand N-linked glycoprotein family. It is important for the mineralization of bone and dentin. DMP-1 is expressed in bone, tooth and hypertrophic cartilage. It is synthesized by preosteoblasts and contains a large number of acidic domains. DMP-1 localizes to the nucleus of undifferentiated osteoblasts where it functions as a transcriptional regulator for osteoblast-specific gene activation and induces osteoblast differentiation. During osteoblast maturation, DMP-1 undergoes a conformational change and becomes phosphorylated by casein kinase II in response to an influx of calcium ions to the nucleus. DMP-1 is then exported to the extracellular matrix (ECM) where it regulates the nucleation of hydroxyapatite and the formation of calcified tissue. DMP-1 is proteolytically processed into N- and C-terminal fragments in the ECM of bone and dentin. The protein has also been identified in bone as a high molecular weight proteoglycan comprised of the N-terminal DMP-1 fragment and chondroitin sulfate.The loss of DMP-1 can result in hypomineralized bone.

UOM: 1 * 100 µl

Supplier: Biotium

Description: Recognizes a 77-85 kDa protein, identified as cellular or tissue transglutaminase II (TGase II). Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. Finally, the encoded protein is the autoantigen implicated in celiac disease. The identification of transglutaminase as the main antigen of endomysium antibodies allows a new diagnostic approach to celiac disease (CD), a genetic, immunologically mediated small bowel enteropathy that causes malabsorption. TGase II is implicated in programmed cell death, signal transduction, drug-resistance, cell growth, endocytosis, insulin secretion, cell adhesion, cataract formation, and wound healing.