You Searched For: Chromotrope+2B

Catalog Number: (BOSSBS-13647R-A488)

Supplier: Bioss

Description: c-Jun NH2-terminal kinases (JNKs) are distant members of the MAP kinase family (1). JNK1 is activated by dual phosphorylation at a Thr-Pro-Tyr motif in response to ultraviolet (UV) light, and it functions to phosphorylate c-Jun at amino terminal serine regulatory sites, Ser-63 and Ser-73, resulting in transcriptional activation (2-5). Two additional JNK family members have been identified as JNK2 and JNK3 (3). JIP-1 (for JNK interacting protein-1) has been identified as a cytoplasmic inhibitor of JNK that retains JNK in the cytoplasm, thereby inhibiting JNK-regulated gene expression. Evidence suggests that JNK1 and JNK2 bind to JIP-1 with greater affinity than to ATF-2 and c-Jun, which are targets of the JNK signaling pathway. JIP-1 contains an amino terminal JNK binding domain and a carboxy terminal SH3 domain. ATF-2 and c-Jun also contain the JNK binding domain and are thought to compete with JIP-1 for JNK binding (6). Multiple splice variants if JIP-1, including JIP-1b, JIP-1c (also designated islet-brain 1 or IB-1), JIP-2a, JIP-2b and JIP-3, have been identified in brain (7).

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-13647R-FITC)

Supplier: Bioss

Description: c-Jun NH2-terminal kinases (JNKs) are distant members of the MAP kinase family (1). JNK1 is activated by dual phosphorylation at a Thr-Pro-Tyr motif in response to ultraviolet (UV) light, and it functions to phosphorylate c-Jun at amino terminal serine regulatory sites, Ser-63 and Ser-73, resulting in transcriptional activation (2-5). Two additional JNK family members have been identified as JNK2 and JNK3 (3). JIP-1 (for JNK interacting protein-1) has been identified as a cytoplasmic inhibitor of JNK that retains JNK in the cytoplasm, thereby inhibiting JNK-regulated gene expression. Evidence suggests that JNK1 and JNK2 bind to JIP-1 with greater affinity than to ATF-2 and c-Jun, which are targets of the JNK signaling pathway. JIP-1 contains an amino terminal JNK binding domain and a carboxy terminal SH3 domain. ATF-2 and c-Jun also contain the JNK binding domain and are thought to compete with JIP-1 for JNK binding (6). Multiple splice variants if JIP-1, including JIP-1b, JIP-1c (also designated islet-brain 1 or IB-1), JIP-2a, JIP-2b and JIP-3, have been identified in brain (7).

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-13647R-HRP)

Supplier: Bioss

Description: c-Jun NH2-terminal kinases (JNKs) are distant members of the MAP kinase family (1). JNK1 is activated by dual phosphorylation at a Thr-Pro-Tyr motif in response to ultraviolet (UV) light, and it functions to phosphorylate c-Jun at amino terminal serine regulatory sites, Ser-63 and Ser-73, resulting in transcriptional activation (2-5). Two additional JNK family members have been identified as JNK2 and JNK3 (3). JIP-1 (for JNK interacting protein-1) has been identified as a cytoplasmic inhibitor of JNK that retains JNK in the cytoplasm, thereby inhibiting JNK-regulated gene expression. Evidence suggests that JNK1 and JNK2 bind to JIP-1 with greater affinity than to ATF-2 and c-Jun, which are targets of the JNK signaling pathway. JIP-1 contains an amino terminal JNK binding domain and a carboxy terminal SH3 domain. ATF-2 and c-Jun also contain the JNK binding domain and are thought to compete with JIP-1 for JNK binding (6). Multiple splice variants if JIP-1, including JIP-1b, JIP-1c (also designated islet-brain 1 or IB-1), JIP-2a, JIP-2b and JIP-3, have been identified in brain (7).

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-13647R)

Supplier: Bioss

Description: c-Jun NH2-terminal kinases (JNKs) are distant members of the MAP kinase family (1). JNK1 is activated by dual phosphorylation at a Thr-Pro-Tyr motif in response to ultraviolet (UV) light, and it functions to phosphorylate c-Jun at amino terminal serine regulatory sites, Ser-63 and Ser-73, resulting in transcriptional activation (2-5). Two additional JNK family members have been identified as JNK2 and JNK3 (3). JIP-1 (for JNK interacting protein-1) has been identified as a cytoplasmic inhibitor of JNK that retains JNK in the cytoplasm, thereby inhibiting JNK-regulated gene expression. Evidence suggests that JNK1 and JNK2 bind to JIP-1 with greater affinity than to ATF-2 and c-Jun, which are targets of the JNK signaling pathway. JIP-1 contains an amino terminal JNK binding domain and a carboxy terminal SH3 domain. ATF-2 and c-Jun also contain the JNK binding domain and are thought to compete with JIP-1 for JNK binding (6). Multiple splice variants if JIP-1, including JIP-1b, JIP-1c (also designated islet-brain 1 or IB-1), JIP-2a, JIP-2b and JIP-3, have been identified in brain (7).

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-13647R-A647)

Supplier: Bioss

Description: c-Jun NH2-terminal kinases (JNKs) are distant members of the MAP kinase family (1). JNK1 is activated by dual phosphorylation at a Thr-Pro-Tyr motif in response to ultraviolet (UV) light, and it functions to phosphorylate c-Jun at amino terminal serine regulatory sites, Ser-63 and Ser-73, resulting in transcriptional activation (2-5). Two additional JNK family members have been identified as JNK2 and JNK3 (3). JIP-1 (for JNK interacting protein-1) has been identified as a cytoplasmic inhibitor of JNK that retains JNK in the cytoplasm, thereby inhibiting JNK-regulated gene expression. Evidence suggests that JNK1 and JNK2 bind to JIP-1 with greater affinity than to ATF-2 and c-Jun, which are targets of the JNK signaling pathway. JIP-1 contains an amino terminal JNK binding domain and a carboxy terminal SH3 domain. ATF-2 and c-Jun also contain the JNK binding domain and are thought to compete with JIP-1 for JNK binding (6). Multiple splice variants if JIP-1, including JIP-1b, JIP-1c (also designated islet-brain 1 or IB-1), JIP-2a, JIP-2b and JIP-3, have been identified in brain (7).

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-13647R-A350)

Supplier: Bioss

Description: c-Jun NH2-terminal kinases (JNKs) are distant members of the MAP kinase family (1). JNK1 is activated by dual phosphorylation at a Thr-Pro-Tyr motif in response to ultraviolet (UV) light, and it functions to phosphorylate c-Jun at amino terminal serine regulatory sites, Ser-63 and Ser-73, resulting in transcriptional activation (2-5). Two additional JNK family members have been identified as JNK2 and JNK3 (3). JIP-1 (for JNK interacting protein-1) has been identified as a cytoplasmic inhibitor of JNK that retains JNK in the cytoplasm, thereby inhibiting JNK-regulated gene expression. Evidence suggests that JNK1 and JNK2 bind to JIP-1 with greater affinity than to ATF-2 and c-Jun, which are targets of the JNK signaling pathway. JIP-1 contains an amino terminal JNK binding domain and a carboxy terminal SH3 domain. ATF-2 and c-Jun also contain the JNK binding domain and are thought to compete with JIP-1 for JNK binding (6). Multiple splice variants if JIP-1, including JIP-1b, JIP-1c (also designated islet-brain 1 or IB-1), JIP-2a, JIP-2b and JIP-3, have been identified in brain (7).

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-13647R-CY5)

Supplier: Bioss

Description: c-Jun NH2-terminal kinases (JNKs) are distant members of the MAP kinase family (1). JNK1 is activated by dual phosphorylation at a Thr-Pro-Tyr motif in response to ultraviolet (UV) light, and it functions to phosphorylate c-Jun at amino terminal serine regulatory sites, Ser-63 and Ser-73, resulting in transcriptional activation (2-5). Two additional JNK family members have been identified as JNK2 and JNK3 (3). JIP-1 (for JNK interacting protein-1) has been identified as a cytoplasmic inhibitor of JNK that retains JNK in the cytoplasm, thereby inhibiting JNK-regulated gene expression. Evidence suggests that JNK1 and JNK2 bind to JIP-1 with greater affinity than to ATF-2 and c-Jun, which are targets of the JNK signaling pathway. JIP-1 contains an amino terminal JNK binding domain and a carboxy terminal SH3 domain. ATF-2 and c-Jun also contain the JNK binding domain and are thought to compete with JIP-1 for JNK binding (6). Multiple splice variants if JIP-1, including JIP-1b, JIP-1c (also designated islet-brain 1 or IB-1), JIP-2a, JIP-2b and JIP-3, have been identified in brain (7).

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12055R)

Supplier: Bioss

Description: SR-5B, also designated 5-hydroxytryptamine (serotonin) receptor 5B (5-HT5B) and G protein-coupled receptor 134 (GPR134) is a receptor for the monoamine ligand serotonin (5-hydroxytryptamine, 5-HT). Serotonin is a neurotransmitter derived from serotonergic neurons in the central nervous system and enterochromaffin cells in the gastrointestinal tract. Serotonin actions are mediated by receptors that influence the biochemistry of depression, anxiety, sexuality and appetite. Rat SR-5B is present in serotonergic neurons in dorsal raphe (DR) and central superior nucleus (CS, median raphe nucleus). DR cell bodies showing SR-5B mRNA expression are abundant in the medial portions of the nucleus. CS coexpression of SR-5B receptor mRNA with serotonin transporter mRNA is high in the intermediate portions of the nucleus. Serotonin receptors include SR-1–7 (5HT1–7). Subtypes within the SR-1 group include SR-1A, -1B, -1D, -1E and -1F. Subtypes within the SR-2 group include SR-2A, -2B and -2C. Subtypes within the SR-5 group include SR-5A and -5B. SR receptors can couple to G proteins that act on either adenylate cyclase or phospholipase C (PLC). The SR-3 class of receptors are ion channels.32234.

UOM: 1 * 100 µl

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Catalog Number: (PRSI33-361)

Supplier: ProSci Inc.

Description: This mAb recognises a protein of ~30 kDa, identified as CELA3B (Chymotrypsin like elastase family member 3B), or Elastase 3B. Elastases form a subfamily of serine proteases that hydrolyze many proteins in addition to elastin. Humans have six genes which encode the structurally similar proteins: Elastase 1, 2, 2A, 2B, 3A, and 3B. Unlike other elastases, 3B has little elastolytic activity. Like most of the human elastases, 3B is secreted from the pancreas as a zymogen and, like other serine proteases such as trypsin, chymotrypsin and kallikrein; it has a digestive function in the intestine. Elastase 3B preferentially cleaves proteins after alanine residues. It may also function in the intestinal transport and metabolism of cholesterol. Elastases 3A/B have been referred to as Protease E and as Elastase 1, and excretion of this protein in fecal material is frequently used as a measure of pancreatic function in clinical assays.

UOM: 1 * 100 µG

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Catalog Number: (PRSI33-794)

Supplier: ProSci Inc.

Description: This mAb recognises a protein of ~30 kDa, identified as CELA3B (Chymotrypsin like elastase family member 3B), or Elastase 3B. Elastases form a subfamily of serine proteases that hydrolyze many proteins in addition to elastin. Humans have six genes which encode the structurally similar proteins: Elastase 1, 2, 2A, 2B, 3A, and 3B. Unlike other elastases, 3B has little elastolytic activity. Like most of the human elastases, 3B is secreted from the pancreas as a zymogen and, like other serine proteases such as trypsin, chymotrypsin and kallikrein; it has a digestive function in the intestine. Elastase 3B preferentially cleaves proteins after alanine residues. It may also function in the intestinal transport and metabolism of cholesterol. Elastases 3A/B have been referred to as Protease E and as Elastase 1, and excretion of this protein in fecal material is frequently used as a measure of pancreatic function in clinical assays.

UOM: 1 * 100 µG

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Catalog Number: (BOSSBS-13647R-CY3)

Supplier: Bioss

Description: c-Jun NH2-terminal kinases (JNKs) are distant members of the MAP kinase family (1). JNK1 is activated by dual phosphorylation at a Thr-Pro-Tyr motif in response to ultraviolet (UV) light, and it functions to phosphorylate c-Jun at amino terminal serine regulatory sites, Ser-63 and Ser-73, resulting in transcriptional activation (2-5). Two additional JNK family members have been identified as JNK2 and JNK3 (3). JIP-1 (for JNK interacting protein-1) has been identified as a cytoplasmic inhibitor of JNK that retains JNK in the cytoplasm, thereby inhibiting JNK-regulated gene expression. Evidence suggests that JNK1 and JNK2 bind to JIP-1 with greater affinity than to ATF-2 and c-Jun, which are targets of the JNK signaling pathway. JIP-1 contains an amino terminal JNK binding domain and a carboxy terminal SH3 domain. ATF-2 and c-Jun also contain the JNK binding domain and are thought to compete with JIP-1 for JNK binding (6). Multiple splice variants if JIP-1, including JIP-1b, JIP-1c (also designated islet-brain 1 or IB-1), JIP-2a, JIP-2b and JIP-3, have been identified in brain (7).

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-13647R-CY7)

Supplier: Bioss

Description: c-Jun NH2-terminal kinases (JNKs) are distant members of the MAP kinase family (1). JNK1 is activated by dual phosphorylation at a Thr-Pro-Tyr motif in response to ultraviolet (UV) light, and it functions to phosphorylate c-Jun at amino terminal serine regulatory sites, Ser-63 and Ser-73, resulting in transcriptional activation (2-5). Two additional JNK family members have been identified as JNK2 and JNK3 (3). JIP-1 (for JNK interacting protein-1) has been identified as a cytoplasmic inhibitor of JNK that retains JNK in the cytoplasm, thereby inhibiting JNK-regulated gene expression. Evidence suggests that JNK1 and JNK2 bind to JIP-1 with greater affinity than to ATF-2 and c-Jun, which are targets of the JNK signaling pathway. JIP-1 contains an amino terminal JNK binding domain and a carboxy terminal SH3 domain. ATF-2 and c-Jun also contain the JNK binding domain and are thought to compete with JIP-1 for JNK binding (6). Multiple splice variants if JIP-1, including JIP-1b, JIP-1c (also designated islet-brain 1 or IB-1), JIP-2a, JIP-2b and JIP-3, have been identified in brain (7).

UOM: 1 * 100 µl

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Catalog Number: (PRSI92-683)

Supplier: ProSci Inc.

Description: Triggering receptor expressed on myeloid cells-2 (TREM-2) is a cell surface receptor primarily expressed on macrophages, osteoclasts, microglia and dendritic cells. TREM-2 is one member of the TREM family, inhibiting the releasing of inflammatory mediators, so it is an important in vivo anti-inflammatory receptor. TREM-2 consists of an 18 aa signal sequence, a 153 aa extracellular domain (ECD) with one V-type Ig-like domain, a 21 aa transmembrane (TM) domain, and a 35 aa cytoplasmic tail. A soluble form of TREM-2 (TREM-2b) created by alternate splicing diverges at aa 161. TREM-2 transduces intracellular signals through the adaptor DAP12. After binding of TREM-2 with ligand, the TREM-2/DAP12 (dead-cell-activated-receptor-associated protein)-mediated signal transduction pathway causes a series of intracellular protein tyrosine phosphorylation reactions and enzymatic reactions, which then activate the myeloid cells and participate T cell responses.

UOM: 1 * 50 µG

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Catalog Number: (PRSI92-682)

Supplier: ProSci Inc.

Description: Triggering receptor expressed on myeloid cells-2 (TREM-2) is a cell surface receptor primarily expressed on macrophages, osteoclasts, microglia and dendritic cells. TREM-2 is one member of the TREM family, inhibiting the releasing of inflammatory mediators, so it is an important in vivo anti-inflammatory receptor. TREM-2 consists of an 18 aa signal sequence, a 153 aa extracellular domain (ECD) with one V-type Ig-like domain, a 21 aa transmembrane (TM) domain, and a 35 aa cytoplasmic tail. A soluble form of TREM-2 (TREM-2b) created by alternate splicing diverges at aa 161. TREM-2 transduces intracellular signals through the adaptor DAP12. After binding of TREM-2 with ligand, the TREM-2/DAP12 (dead-cell-activated-receptor-associated protein)-mediated signal transduction pathway causes a series of intracellular protein tyrosine phosphorylation reactions and enzymatic reactions, which then activate the myeloid cells and participate T cell responses.

UOM: 1 * 50 µG

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Catalog Number: (1.10107.0005)

Supplier: Merck

Description: Arsenazo III, Millipore®

UOM: 1 * 5 g

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Catalog Number: (BSBTPB9975)

Supplier: Boster Bio

Description: Activin receptor type-2B is a protein that in humans is encoded by the ACVR2B gene. Activins are dimeric growth and differentiation factors which belong to the transforming growth factor-beta (TGF-beta) superfamily of structurally related signaling proteins. Activins signal through a heteromeric complex of receptor serine kinases which include at least two type I (I and IB) and two type II (II and IIB) receptors. These receptors are all transmembrane proteins, composed of a ligand-binding extracellular domain with cysteine-rich region, a transmembrane domain, and a cytoplasmic domain with predicted serine/threonine specificity. Type I receptors are essential for signaling; and type II receptors are required for binding ligands and for expression of type I receptors. Type I and II receptors form a stable complex after ligand binding, resulting in phosphorylation of type I receptors by type II receptors. Type II receptors are considered to be constitutively active kinases. This ACVR2B gene encodes activin A type IIB receptor, which displays a 3- to 4-fold higher affinity for the ligand than activin A type II receptor.

UOM: 1 * 100 µG

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