7267 Results for: "Potassium+Hyaluronate&amp"

Supplier: Abcam

Rabbit monoclonal [EPR10747(B)] to AMPS - BSA and Azide free.

Supplier: Bioss

Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. In cancer cells, may play an important role in invadopodia formation. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis. Altered expression or dysfunction causes numerous pathogenic phenotypes. Great protein heterogeneity due to numerous alternative splicing and post-translational modification events.

Supplier: Bioss

HAPLN2 is a 340 amino acid protein encoded by the human gene HAPLN2. HAPLN2 belongs to the HAPLN family and contains one immunoglobulin (Ig)-like, V-type domain and two link domains. HAPLN2 mediates a firm binding of versican V2 to hyaluronic acid. HAPLN2 is believed to play a pivotal role in the formation of the hyaluronan-associated matrix in the central nervous system (CNS), which facilitates neuronal conduction and general structural stabilization. HAPLN2 may also be involved in the formation of extracellular matrices, contributing to perineuronal nets and facilitating the understanding of a functional role of these extracellular matrices. HAPLN2 is found in several nuclei throughout the midbrain and hindbrain in a perineuronal net pattern.

Supplier: Bioss

HAPLN2 is a 340 amino acid protein encoded by the human gene HAPLN2. HAPLN2 belongs to the HAPLN family and contains one immunoglobulin (Ig)-like, V-type domain and two link domains. HAPLN2 mediates a firm binding of versican V2 to hyaluronic acid. HAPLN2 is believed to play a pivotal role in the formation of the hyaluronan-associated matrix in the central nervous system (CNS), which facilitates neuronal conduction and general structural stabilisation. HAPLN2 may also be involved in the formation of extracellular matrices, contributing to perineuronal nets and facilitating the understanding of a functional role of these extracellular matrices. HAPLN2 is found in several nuclei throughout the midbrain and hindbrain in a perineuronal net pattern.

Supplier: Bioss

HAPLN2 is a 340 amino acid protein encoded by the human gene HAPLN2. HAPLN2 belongs to the HAPLN family and contains one immunoglobulin (Ig)-like, V-type domain and two link domains. HAPLN2 mediates a firm binding of versican V2 to hyaluronic acid. HAPLN2 is believed to play a pivotal role in the formation of the hyaluronan-associated matrix in the central nervous system (CNS), which facilitates neuronal conduction and general structural stabilisation. HAPLN2 may also be involved in the formation of extracellular matrices, contributing to perineuronal nets and facilitating the understanding of a functional role of these extracellular matrices. HAPLN2 is found in several nuclei throughout the midbrain and hindbrain in a perineuronal net pattern.

Supplier: Bioss

HAPLN2 is a 340 amino acid protein encoded by the human gene HAPLN2. HAPLN2 belongs to the HAPLN family and contains one immunoglobulin (Ig)-like, V-type domain and two link domains. HAPLN2 mediates a firm binding of versican V2 to hyaluronic acid. HAPLN2 is believed to play a pivotal role in the formation of the hyaluronan-associated matrix in the central nervous system (CNS), which facilitates neuronal conduction and general structural stabilization. HAPLN2 may also be involved in the formation of extracellular matrices, contributing to perineuronal nets and facilitating the understanding of a functional role of these extracellular matrices. HAPLN2 is found in several nuclei throughout the midbrain and hindbrain in a perineuronal net pattern.

Supplier: Merck Millipore (Calbiochem‎)

Affinity purified proteins. Binds specifically and strongly to hyaluronic acid. Suitable for ELISA and histochemistry.

Supplier: Bioss

Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. In cancer cells, may play an important role in invadopodia formation. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis. Altered expression or dysfunction causes numerous pathogenic phenotypes. Great protein heterogeneity due to numerous alternative splicing and post-translational modification events.

Supplier: Bioss

HAPLN2 is a 340 amino acid protein encoded by the human gene HAPLN2. HAPLN2 belongs to the HAPLN family and contains one immunoglobulin (Ig)-like, V-type domain and two link domains. HAPLN2 mediates a firm binding of versican V2 to hyaluronic acid. HAPLN2 is believed to play a pivotal role in the formation of the hyaluronan-associated matrix in the central nervous system (CNS), which facilitates neuronal conduction and general structural stabilization. HAPLN2 may also be involved in the formation of extracellular matrices, contributing to perineuronal nets and facilitating the understanding of a functional role of these extracellular matrices. HAPLN2 is found in several nuclei throughout the midbrain and hindbrain in a perineuronal net pattern.

Supplier: Bioss

Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. In cancer cells, may play an important role in invadopodia formation. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis. Altered expression or dysfunction causes numerous pathogenic phenotypes. Great protein heterogeneity due to numerous alternative splicing and post-translational modification events.

Supplier: Bioss

Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. In cancer cells, may play an important role in invadopodia formation. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis. Altered expression or dysfunction causes numerous pathogenic phenotypes. Great protein heterogeneity due to numerous alternative splicing and post-translational modification events.

Supplier: Bioss

Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. In cancer cells, may play an important role in invadopodia formation. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis. Altered expression or dysfunction causes numerous pathogenic phenotypes. Great protein heterogeneity due to numerous alternative splicing and post-translational modification events.

Supplier: Bioss

Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. In cancer cells, may play an important role in invadopodia formation. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis. Altered expression or dysfunction causes numerous pathogenic phenotypes. Great protein heterogeneity due to numerous alternative splicing and post-translational modification events.

Supplier: Bioss

Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. In cancer cells, may play an important role in invadopodia formation. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis. Altered expression or dysfunction causes numerous pathogenic phenotypes. Great protein heterogeneity due to numerous alternative splicing and post-translational modification events.

Supplier: Bioss

Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. In cancer cells, may play an important role in invadopodia formation. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis. Altered expression or dysfunction causes numerous pathogenic phenotypes. Great protein heterogeneity due to numerous alternative splicing and post-translational modification events.

Supplier: Bioss

Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. In cancer cells, may play an important role in invadopodia formation. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis. Altered expression or dysfunction causes numerous pathogenic phenotypes. Great protein heterogeneity due to numerous alternative splicing and post-translational modification events.

Supplier: Bioss

HAPLN2 is a 340 amino acid protein encoded by the human gene HAPLN2. HAPLN2 belongs to the HAPLN family and contains one immunoglobulin (Ig)-like, V-type domain and two link domains. HAPLN2 mediates a firm binding of versican V2 to hyaluronic acid. HAPLN2 is believed to play a pivotal role in the formation of the hyaluronan-associated matrix in the central nervous system (CNS), which facilitates neuronal conduction and general structural stabilization. HAPLN2 may also be involved in the formation of extracellular matrices, contributing to perineuronal nets and facilitating the understanding of a functional role of these extracellular matrices. HAPLN2 is found in several nuclei throughout the midbrain and hindbrain in a perineuronal net pattern.

Supplier: ENZO LIFE SCIENCES

Ultra-sensitive (7 pg/ml)Amp'd® HSP70 high sensitivity ELISA kit enabling the ability to use less sample and detect both baseline and upregulated levels of human, mouse and rat Hsp70 (Hsp72), a major chaperone, cancer biomarker, and key cell stress regulator.

Supplier: Abcam

Rabbit monoclonal [EPR10746(B)] to AMPS.

Supplier: Abcam

Rabbit monoclonal [EPR10746(B)] to AMPS - BSA and Azide free.

Supplier: Bioss

Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. In cancer cells, may play an important role in invadopodia formation. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis. Altered expression or dysfunction causes numerous pathogenic phenotypes. Great protein heterogeneity due to numerous alternative splicing and post-translational modification events.

Supplier: Bioss

Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. In cancer cells, may play an important role in invadopodia formation. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis. Altered expression or dysfunction causes numerous pathogenic phenotypes. Great protein heterogeneity due to numerous alternative splicing and post-translational modification events.

Supplier: Bioss

Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. In cancer cells, may play an important role in invadopodia formation. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis. Altered expression or dysfunction causes numerous pathogenic phenotypes. Great protein heterogeneity due to numerous alternative splicing and post-translational modification events.

Supplier: Bioss

Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. In cancer cells, may play an important role in invadopodia formation. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis. Altered expression or dysfunction causes numerous pathogenic phenotypes. Great protein heterogeneity due to numerous alternative splicing and post-translational modification events.

Supplier: Bioss

HAPLN2 is a 340 amino acid protein encoded by the human gene HAPLN2. HAPLN2 belongs to the HAPLN family and contains one immunoglobulin (Ig)-like, V-type domain and two link domains. HAPLN2 mediates a firm binding of versican V2 to hyaluronic acid. HAPLN2 is believed to play a pivotal role in the formation of the hyaluronan-associated matrix in the central nervous system (CNS), which facilitates neuronal conduction and general structural stabilization. HAPLN2 may also be involved in the formation of extracellular matrices, contributing to perineuronal nets and facilitating the understanding of a functional role of these extracellular matrices. HAPLN2 is found in several nuclei throughout the midbrain and hindbrain in a perineuronal net pattern.

Supplier: Bioss

HAPLN2 is a 340 amino acid protein encoded by the human gene HAPLN2. HAPLN2 belongs to the HAPLN family and contains one immunoglobulin (Ig)-like, V-type domain and two link domains. HAPLN2 mediates a firm binding of versican V2 to hyaluronic acid. HAPLN2 is believed to play a pivotal role in the formation of the hyaluronan-associated matrix in the central nervous system (CNS), which facilitates neuronal conduction and general structural stabilization. HAPLN2 may also be involved in the formation of extracellular matrices, contributing to perineuronal nets and facilitating the understanding of a functional role of these extracellular matrices. HAPLN2 is found in several nuclei throughout the midbrain and hindbrain in a perineuronal net pattern.

Supplier: Bioss

Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. In cancer cells, may play an important role in invadopodia formation. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis. Altered expression or dysfunction causes numerous pathogenic phenotypes. Great protein heterogeneity due to numerous alternative splicing and post-translational modification events.

Supplier: Bioss

Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. In cancer cells, may play an important role in invadopodia formation. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis. Altered expression or dysfunction causes numerous pathogenic phenotypes. Great protein heterogeneity due to numerous alternative splicing and post-translational modification events.

Supplier: Bioss

Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. In cancer cells, may play an important role in invadopodia formation. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis. Altered expression or dysfunction causes numerous pathogenic phenotypes. Great protein heterogeneity due to numerous alternative splicing and post-translational modification events.

Supplier: Bioss

Receptor for hyaluronic acid (HA). Mediates cell-cell and cell-matrix interactions through its affinity for HA, and possibly also through its affinity for other ligands such as osteopontin, collagens, and matrix metalloproteinases (MMPs). Adhesion with HA plays an important role in cell migration, tumor growth and progression. In cancer cells, may play an important role in invadopodia formation. Also involved in lymphocyte activation, recirculation and homing, and in hematopoiesis. Altered expression or dysfunction causes numerous pathogenic phenotypes. Great protein heterogeneity due to numerous alternative splicing and post-translational modification events.