2769 Results for: "Benzo[b]thiophene-7-carboxylic+acid&pageNo=89"

Supplier: Cayman Chemical

A selective inhibitor of human collagenase-3, also known as MMP-13, producing 89% inhibition at 10 µg/ml 1 * 25 mg

Supplier: Abcam

Human Myosin light chain 3 ELISA Kit is a single-wash 90-min Simplestep used to quantify Human Myosin light chain 3 with a sensitivity of 89 pg/ml. The assay uses a simple mix-wash-read protocol with just one incubation and one wash step. - Colorimetric Sandwich ELISA - 450 nm readout : works on any standard plate reader.

Supplier: Bioss

The ADP-ribosylation factor (ARF) protein family are structurally and functionally conserved members of the Ras superfamily of regulatory GTP-binding proteins (1–3). ARFs influence vesicle trafficking and signal transduction in eukaryotic cells (1–3). ARF-dependent regulatory mechanisms include the coordination of spectrin interactions with golgi membranes and the association of actin to the golgi via rho family-dependent G-protein localization (Rac, CDC42) and WASP/Arp2/3 complexes (3–7). Additionally, ARFs play a central role in maintenance of organelle integrity, assembly of coat proteins, and activation of phospholipase D (5–7). The ARF proteins are categorized as class I (ARF1, ARF2,and ARF3), class II (ARF4 and ARF5) and class III (ARF6); members of each class share a common gene organization (8,9). The human ARF6 gene maps to chromosome 7q22.1, contains five exons and four introns, and encodes a 175 amino acid protein (8,9).

Supplier: Bioss

The ADP-ribosylation factor (ARF) protein family are structurally and functionally conserved members of the Ras superfamily of regulatory GTP-binding proteins (1–3). ARFs influence vesicle trafficking and signal transduction in eukaryotic cells (1–3). ARF-dependent regulatory mechanisms include the coordination of spectrin interactions with golgi membranes and the association of actin to the golgi via rho family-dependent G-protein localization (Rac, CDC42) and WASP/Arp2/3 complexes (3–7). Additionally, ARFs play a central role in maintenance of organelle integrity, assembly of coat proteins, and activation of phospholipase D (5–7). The ARF proteins are categorized as class I (ARF1, ARF2,and ARF3), class II (ARF4 and ARF5) and class III (ARF6); members of each class share a common gene organization (8,9). The human ARF6 gene maps to chromosome 7q22.1, contains five exons and four introns, and encodes a 175 amino acid protein (8,9).

Supplier: Bioss

The ADP-ribosylation factor (ARF) protein family are structurally and functionally conserved members of the Ras superfamily of regulatory GTP-binding proteins (1–3). ARFs influence vesicle trafficking and signal transduction in eukaryotic cells (1–3). ARF-dependent regulatory mechanisms include the coordination of spectrin interactions with golgi membranes and the association of actin to the golgi via rho family-dependent G-protein localization (Rac, CDC42) and WASP/Arp2/3 complexes (3–7). Additionally, ARFs play a central role in maintenance of organelle integrity, assembly of coat proteins, and activation of phospholipase D (5–7). The ARF proteins are categorized as class I (ARF1, ARF2,and ARF3), class II (ARF4 and ARF5) and class III (ARF6); members of each class share a common gene organization (8,9). The human ARF6 gene maps to chromosome 7q22.1, contains five exons and four introns, and encodes a 175 amino acid protein (8,9).

Supplier: Bioss

The ADP-ribosylation factor (ARF) protein family are structurally and functionally conserved members of the Ras superfamily of regulatory GTP-binding proteins (1–3). ARFs influence vesicle trafficking and signal transduction in eukaryotic cells (1–3). ARF-dependent regulatory mechanisms include the coordination of spectrin interactions with golgi membranes and the association of actin to the golgi via rho family-dependent G-protein localization (Rac, CDC42) and WASP/Arp2/3 complexes (3–7). Additionally, ARFs play a central role in maintenance of organelle integrity, assembly of coat proteins, and activation of phospholipase D (5–7). The ARF proteins are categorized as class I (ARF1, ARF2,and ARF3), class II (ARF4 and ARF5) and class III (ARF6); members of each class share a common gene organization (8,9). The human ARF6 gene maps to chromosome 7q22.1, contains five exons and four introns, and encodes a 175 amino acid protein (8,9).

Supplier: Bioss

The ADP-ribosylation factor (ARF) protein family are structurally and functionally conserved members of the Ras superfamily of regulatory GTP-binding proteins (1–3). ARFs influence vesicle trafficking and signal transduction in eukaryotic cells (1–3). ARF-dependent regulatory mechanisms include the coordination of spectrin interactions with golgi membranes and the association of actin to the golgi via rho family-dependent G-protein localization (Rac, CDC42) and WASP/Arp2/3 complexes (3–7). Additionally, ARFs play a central role in maintenance of organelle integrity, assembly of coat proteins, and activation of phospholipase D (5–7). The ARF proteins are categorized as class I (ARF1, ARF2,and ARF3), class II (ARF4 and ARF5) and class III (ARF6); members of each class share a common gene organization (8,9). The human ARF6 gene maps to chromosome 7q22.1, contains five exons and four introns, and encodes a 175 amino acid protein (8,9).

Supplier: Bioss

The ADP-ribosylation factor (ARF) protein family are structurally and functionally conserved members of the Ras superfamily of regulatory GTP-binding proteins (1–3). ARFs influence vesicle trafficking and signal transduction in eukaryotic cells (1–3). ARF-dependent regulatory mechanisms include the coordination of spectrin interactions with golgi membranes and the association of actin to the golgi via rho family-dependent G-protein localization (Rac, CDC42) and WASP/Arp2/3 complexes (3–7). Additionally, ARFs play a central role in maintenance of organelle integrity, assembly of coat proteins, and activation of phospholipase D (5–7). The ARF proteins are categorized as class I (ARF1, ARF2,and ARF3), class II (ARF4 and ARF5) and class III (ARF6); members of each class share a common gene organization (8,9). The human ARF6 gene maps to chromosome 7q22.1, contains five exons and four introns, and encodes a 175 amino acid protein (8,9).

Supplier: Bioss

The ADP-ribosylation factor (ARF) protein family are structurally and functionally conserved members of the Ras superfamily of regulatory GTP-binding proteins (1–3). ARFs influence vesicle trafficking and signal transduction in eukaryotic cells (1–3). ARF-dependent regulatory mechanisms include the coordination of spectrin interactions with golgi membranes and the association of actin to the golgi via rho family-dependent G-protein localization (Rac, CDC42) and WASP/Arp2/3 complexes (3–7). Additionally, ARFs play a central role in maintenance of organelle integrity, assembly of coat proteins, and activation of phospholipase D (5–7). The ARF proteins are categorized as class I (ARF1, ARF2,and ARF3), class II (ARF4 and ARF5) and class III (ARF6); members of each class share a common gene organization (8,9). The human ARF6 gene maps to chromosome 7q22.1, contains five exons and four introns, and encodes a 175 amino acid protein (8,9).

Supplier: Bioss

The ADP-ribosylation factor (ARF) protein family are structurally and functionally conserved members of the Ras superfamily of regulatory GTP-binding proteins (1–3). ARFs influence vesicle trafficking and signal transduction in eukaryotic cells (1–3). ARF-dependent regulatory mechanisms include the coordination of spectrin interactions with golgi membranes and the association of actin to the golgi via rho family-dependent G-protein localization (Rac, CDC42) and WASP/Arp2/3 complexes (3–7). Additionally, ARFs play a central role in maintenance of organelle integrity, assembly of coat proteins, and activation of phospholipase D (5–7). The ARF proteins are categorized as class I (ARF1, ARF2,and ARF3), class II (ARF4 and ARF5) and class III (ARF6); members of each class share a common gene organization (8,9). The human ARF6 gene maps to chromosome 7q22.1, contains five exons and four introns, and encodes a 175 amino acid protein (8,9).

Supplier: Bioss

The ADP-ribosylation factor (ARF) protein family are structurally and functionally conserved members of the Ras superfamily of regulatory GTP-binding proteins (1–3). ARFs influence vesicle trafficking and signal transduction in eukaryotic cells (1–3). ARF-dependent regulatory mechanisms include the coordination of spectrin interactions with golgi membranes and the association of actin to the golgi via rho family-dependent G-protein localization (Rac, CDC42) and WASP/Arp2/3 complexes (3–7). Additionally, ARFs play a central role in maintenance of organelle integrity, assembly of coat proteins, and activation of phospholipase D (5–7). The ARF proteins are categorized as class I (ARF1, ARF2,and ARF3), class II (ARF4 and ARF5) and class III (ARF6); members of each class share a common gene organization (8,9). The human ARF6 gene maps to chromosome 7q22.1, contains five exons and four introns, and encodes a 175 amino acid protein (8,9).

Supplier: Biotium

Expression of NKX2.2 has been found in neuroendocrine tumors of the gut, making it a potential marker for the study of gastrointestinal neuroendocrine tumors. More recently, NKX2.2 protein was identified as a target of EWS-FLI-1, the fusion protein specific to Ewing sarcoma, and was shown to be differentially upregulated in Ewing sarcoma on the basis of array-based gene expression analysis. It acts as a valuable marker for Ewing sarcoma, with a sensitivity of 93% and a specificity of 89%, and aids in the differential diagnosis of small round cell tumors.

Supplier: Biotium

Expression of NKX2.2 has been found in neuroendocrine tumors of the gut, making it a potential marker for the study of gastrointestinal neuroendocrine tumors. More recently, NKX2.2 protein was identified as a target of EWS-FLI-1, the fusion protein specific to Ewing sarcoma, and was shown to be differentially upregulated in Ewing sarcoma on the basis of array-based gene expression analysis. It acts as a valuable marker for Ewing sarcoma, with a sensitivity of 93% and a specificity of 89%, and aids in the differential diagnosis of small round cell tumors.

Supplier: Abcam

Human P-Selectin ELISA kit (CD62P) is a single-wash 90-min Simplestep used to quantify Human P-Selectin (CD62P) with a sensitivity of 89 pg/ml. The assay uses a simple mix-wash-read protocol with just one incubation and one wash step. - Colorimetric sandwich ELISA - 450 nm readout : works on any standard plate reader - Design your own immunoassay: we also offer the conjugation-ready antibody pair.

Supplier: Biotium

Expression of NKX2.2 has been found in neuroendocrine tumors of the gut, making it a potential marker for the study of gastrointestinal neuroendocrine tumors. More recently, NKX2.2 protein was identified as a target of EWS-FLI-1, the fusion protein specific to Ewing sarcoma, and was shown to be differentially upregulated in Ewing sarcoma on the basis of array-based gene expression analysis. It acts as a valuable marker for Ewing sarcoma, with a sensitivity of 93% and a specificity of 89%, and aids in the differential diagnosis of small round cell tumors.

Supplier: Biotium

Expression of NKX2.2 has been found in neuroendocrine tumors of the gut, making it a potential marker for the study of gastrointestinal neuroendocrine tumors. More recently, NKX2.2 protein was identified as a target of EWS-FLI-1, the fusion protein specific to Ewing sarcoma, and was shown to be differentially upregulated in Ewing sarcoma on the basis of array-based gene expression analysis. It acts as a valuable marker for Ewing sarcoma, with a sensitivity of 93% and a specificity of 89%, and aids in the differential diagnosis of small round cell tumors.

Supplier: Biotium

Expression of NKX2.2 has been found in neuroendocrine tumors of the gut, making it a potential marker for the study of gastrointestinal neuroendocrine tumors. More recently, NKX2.2 protein was identified as a target of EWS-FLI-1, the fusion protein specific to Ewing sarcoma, and was shown to be differentially upregulated in Ewing sarcoma on the basis of array-based gene expression analysis. It acts as a valuable marker for Ewing sarcoma, with a sensitivity of 93% and a specificity of 89%, and aids in the differential diagnosis of small round cell tumors.

Supplier: Biotium

Expression of NKX2.2 has been found in neuroendocrine tumors of the gut, making it a potential marker for the study of gastrointestinal neuroendocrine tumors. More recently, NKX2.2 protein was identified as a target of EWS-FLI-1, the fusion protein specific to Ewing sarcoma, and was shown to be differentially upregulated in Ewing sarcoma on the basis of array-based gene expression analysis. It acts as a valuable marker for Ewing sarcoma, with a sensitivity of 93% and a specificity of 89%, and aids in the differential diagnosis of small round cell tumors.

Supplier: Biotium

Expression of NKX2.2 has been found in neuroendocrine tumors of the gut, making it a potential marker for the study of gastrointestinal neuroendocrine tumors. More recently, NKX2.2 protein was identified as a target of EWS-FLI-1, the fusion protein specific to Ewing sarcoma, and was shown to be differentially upregulated in Ewing sarcoma on the basis of array-based gene expression analysis. It acts as a valuable marker for Ewing sarcoma, with a sensitivity of 93% and a specificity of 89%, and aids in the differential diagnosis of small round cell tumors.

Supplier: Biotium

Expression of NKX2.2 has been found in neuroendocrine tumors of the gut, making it a potential marker for the study of gastrointestinal neuroendocrine tumors. More recently, NKX2.2 protein was identified as a target of EWS-FLI-1, the fusion protein specific to Ewing sarcoma, and was shown to be differentially upregulated in Ewing sarcoma on the basis of array-based gene expression analysis. It acts as a valuable marker for Ewing sarcoma, with a sensitivity of 93% and a specificity of 89%, and aids in the differential diagnosis of small round cell tumors.

Supplier: Biotium

Expression of NKX2.2 has been found in neuroendocrine tumors of the gut, making it a potential marker for the study of gastrointestinal neuroendocrine tumors. More recently, NKX2.2 protein was identified as a target of EWS-FLI-1, the fusion protein specific to Ewing sarcoma, and was shown to be differentially upregulated in Ewing sarcoma on the basis of array-based gene expression analysis. It acts as a valuable marker for Ewing sarcoma, with a sensitivity of 93% and a specificity of 89%, and aids in the differential diagnosis of small round cell tumors.

Supplier: Bioss

KLHL3 protein contains a poxvirus and zinc finger domain at the N-terminus and six tandem repeats (kelch repeats) at the C-terminus. At the amino acid level, KLHL3 shares 77% similarity with Drosophila kelch and 89% similarity with Mayven (KLHL2), another human kelch homolog. At least three isoforms are produced and may be the result of alternative promoter usage. The KLHL3 maps within the smallest commonly deleted segment in myeloid leukemias characterized by a deletion of 5q; however, no inactivating mutations of KLHL3 could be detected in malignant myeloid disorders with loss of 5q.

Supplier: Bioss

KLHL3 protein contains a poxvirus and zinc finger domain at the N-terminus and six tandem repeats (kelch repeats) at the C-terminus. At the amino acid level, KLHL3 shares 77% similarity with Drosophila kelch and 89% similarity with Mayven (KLHL2), another human kelch homolog. At least three isoforms are produced and may be the result of alternative promoter usage. The KLHL3 maps within the smallest commonly deleted segment in myeloid leukemias characterized by a deletion of 5q; however, no inactivating mutations of KLHL3 could be detected in malignant myeloid disorders with loss of 5q.

Supplier: Cayman Chemical

A kaempferol glycoside that selectively inhibits RSK2 with an IC50 value of 89 nM (Ki = 1 M) without interfering with upstream acti vators of RSK, including ERK, MEK, EGFR, and PKC 1 * 10 mg

Supplier: Bioss

KLHL3 protein contains a poxvirus and zinc finger domain at the N-terminus and six tandem repeats (kelch repeats) at the C-terminus. At the amino acid level, KLHL3 shares 77% similarity with Drosophila kelch and 89% similarity with Mayven (KLHL2), another human kelch homolog. At least three isoforms are produced and may be the result of alternative promoter usage. The KLHL3 maps within the smallest commonly deleted segment in myeloid leukemias characterized by a deletion of 5q; however, no inactivating mutations of KLHL3 could be detected in malignant myeloid disorders with loss of 5q.

Supplier: Bioss

KLHL3 protein contains a poxvirus and zinc finger domain at the N-terminus and six tandem repeats (kelch repeats) at the C-terminus. At the amino acid level, KLHL3 shares 77% similarity with Drosophila kelch and 89% similarity with Mayven (KLHL2), another human kelch homolog. At least three isoforms are produced and may be the result of alternative promoter usage. The KLHL3 maps within the smallest commonly deleted segment in myeloid leukemias characterized by a deletion of 5q; however, no inactivating mutations of KLHL3 could be detected in malignant myeloid disorders with loss of 5q.

Supplier: Bioss

KLHL3 protein contains a poxvirus and zinc finger domain at the N-terminus and six tandem repeats (kelch repeats) at the C-terminus. At the amino acid level, KLHL3 shares 77% similarity with Drosophila kelch and 89% similarity with Mayven (KLHL2), another human kelch homolog. At least three isoforms are produced and may be the result of alternative promoter usage. The KLHL3 maps within the smallest commonly deleted segment in myeloid leukemias characterized by a deletion of 5q; however, no inactivating mutations of KLHL3 could be detected in malignant myeloid disorders with loss of 5q.

Supplier: Bioss

KLHL3 protein contains a poxvirus and zinc finger domain at the N-terminus and six tandem repeats (kelch repeats) at the C-terminus. At the amino acid level, KLHL3 shares 77% similarity with Drosophila kelch and 89% similarity with Mayven (KLHL2), another human kelch homolog. At least three isoforms are produced and may be the result of alternative promoter usage. The KLHL3 maps within the smallest commonly deleted segment in myeloid leukemias characterized by a deletion of 5q; however, no inactivating mutations of KLHL3 could be detected in malignant myeloid disorders with loss of 5q.

Supplier: Bioss

KLHL3 protein contains a poxvirus and zinc finger domain at the N-terminus and six tandem repeats (kelch repeats) at the C-terminus. At the amino acid level, KLHL3 shares 77% similarity with Drosophila kelch and 89% similarity with Mayven (KLHL2), another human kelch homolog. At least three isoforms are produced and may be the result of alternative promoter usage. The KLHL3 maps within the smallest commonly deleted segment in myeloid leukemias characterised by a deletion of 5q; however, no inactivating mutations of KLHL3 could be detected in malignant myeloid disorders with loss of 5q.

Supplier: Bioss

KLHL3 protein contains a poxvirus and zinc finger domain at the N-terminus and six tandem repeats (kelch repeats) at the C-terminus. At the amino acid level, KLHL3 shares 77% similarity with Drosophila kelch and 89% similarity with Mayven (KLHL2), another human kelch homolog. At least three isoforms are produced and may be the result of alternative promoter usage. The KLHL3 maps within the smallest commonly deleted segment in myeloid leukemias characterized by a deletion of 5q; however, no inactivating mutations of KLHL3 could be detected in malignant myeloid disorders with loss of 5q.