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(2-Hydroxylpropyl)-\\u03B2-cyclodextrine


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Supplier:  Bioss
Description:   Nucleotides are important extracellular signaling molecules that mediate several events, such as cell proliferation, differentiation, chemotaxis and cytokine release. The P2 receptor family is activated by the binding of nucleotides and is divided into two subfamilies, designated P2X and P2Y. The P2Y receptor family are G protein-coupled receptors that mediate the effects of extracellular nucleotides, primarily through the activation of phospholipase C (PLC). To some extent, the P2Y receptors can also activate potassium channels or, alternatively, inhibit adenylate cyclase and N-type calcium channels in response to extracellular nucleotides. P2Y10 (purinergic receptor P2Y, G-protein coupled, 10), also known as P2RY10, is a 339 amino acid multi-pass membrane protein that is thought to act as a receptor for purines coupled to G-proteins. P2Y10 is found at low levels in blood leukocytes and is upregulated during promyelocytic cell differentiation.

Supplier:  Bioss
Description:   Midline-2 is a 715 amino acid protein encoded by the human gene MID2. Midline-2 belongs to the TRIM/RBCC family and contains two B box-type zinc fingers, one B30.2/SPRY domain, one COS domain, one fibronectin type-III domain and one RING-type zinc finger. Midline-2 is a cytoplasmic protein found as a homodimer or heterodimer with Midline-1. It also interacts with IGBP1 (Lymphocyte signaling protein A4). Dimerization is mediated by the tripartite motif (RBCC; RING- and B box-type zinc fingers and coiled coil domains) and microtubule association is dependent on the C-terminal B30.2 domain. Midline-2 is expressed at low levels in fetal kidney and lung, and in adult prostate, ovary and small intestine.
Supplier:  Bioss
Description:   Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Increases the apparent Ca2+/voltage sensitivity of the KCNMA1 channel. It also modifies KCNMA1 channel kinetics and alters its pharmacological properties. It slows down the activation and the deactivation kinetics of the channel. Acts as a negative regulator of smooth muscle contraction by enhancing the calcium sensitivity to KCNMA1. Its presence is also a requirement for internal binding of the KCNMA1 channel opener dehydrosoyasaponin I (DHS-1) triterpene glycoside and for external binding of the agonist hormone 17-beta-estradiol (E2). Increases the binding activity of charybdotoxin (CTX) toxin to KCNMA1 peptide blocker by increasing the CTX association rate and decreasing the dissociation rate.

Supplier:  Bioss
Description:   Myotubularin and the myotubularin-related proteins (MTMR1-9) belong to a highly conserved family of eukaryotic phosphatases. They are protein tyrosine phosphatases that utilize inositol phospholipids, rather than phosphoproteins, as substrates. MTMR family members hydrolyze both Phosphatidylinositol 3-phosphate (PtdIns3P) and PtdIns(3,5)P2. MTMR2 interacts with MTMR5, an inactive family member that increases the enzymatic activity of MTMR2 and dictates its subcellular localization. Mutations in MTMR2 cause autosomal recessive Charcot-Marie-Tooth type 4B1 (CMT4B1), which is characterized by reduced nerve conduction velocities, focally folded myelin sheaths and demyelination. MTMR3 and MTMR4 can either interact with each other or self associate. MTMR6 regulates the activity of the calcium-activated potassium channel 3.1. MTMR9 regulates the activity of MTMR7 and MTMR8.
Catalog Number: (10269-996)

Supplier:  Bioss
Description:   Nucleotides are important extracellular signaling molecules that mediate several events, such as cell proliferation, differentiation, chemotaxis and cytokine release. The P2 receptor family is activated by the binding of nucleotides and is divided into two subfamilies, designated P2X and P2Y. The P2Y receptor family are G protein-coupled receptors that mediate the effects of extracellular nucleotides, primarily through the activation of phospholipase C (PLC). To some extent, the P2Y receptors can also activate potassium channels or, alternatively, inhibit adenylate cyclase and N-type calcium channels in response to extracellular nucleotides. P2Y10 (purinergic receptor P2Y, G-protein coupled, 10), also known as P2RY10, is a 339 amino acid multi-pass membrane protein that is thought to act as a receptor for purines coupled to G-proteins. P2Y10 is found at low levels in blood leukocytes and is upregulated during promyelocytic cell differentiation.
Catalog Number: (10750-450)

Supplier:  Prosci
Description:   LRFN1 Antibody: LRFN1 is one of a family of five transmembrane glycoproteins that are highly expressed in neuronal tissues. LRFN proteins share leucine-rich repeat (LRR)-immunoglobulin-like (Ig)-fibronectin type III (Fn)-transmembrane domain structure with other members of the LRR-Ig-Fn protein superfamily such as the Slitrk family of proteins. Expression of LRFN1, -3, and -4 mRNA was detected in embryonic neuronal cells, while Lrfn2 and Lrfn5 expression was primarily restricted to more mature cells. LRFN1, -2, and -4 bound to PDZ domains of postsynaptic PSD95, re-distributing PSD95 to the cell periphery. It has been suggested that the Lrfn proteins play a role in the developing and/or mature vertebrate nervous system. At least two isoforms of LRFN1 are known to exist.
Catalog Number: (76011-120)

Supplier:  Prosci
Description:   Receptor-activated non-selective cation channel involved in detection of sensations such as coolness, by being activated by cold temperature below 25 degrees Celsius. Activated by icilin, eucalyptol, menthol, cold and modulation of intracellular pH. Involved in menthol sensation. Permeable for monovalent cations sodium, potassium, and cesium and divalent cation calcium. Temperature sensing is tightly linked to voltage-dependent gating. Activated upon depolarization, changes in temperature resulting in graded shifts of its voltage-dependent activation curves. The chemical agonists menthol functions as a gating modifier, shifting activation curves towards physiological membrane potentials. Temperature sensitivity arises from a tenfold difference in the activation energies associated with voltage-dependent opening and closing.

Supplier:  Bioss
Description:   Myotubularin and the myotubularin-related proteins (MTMR1-9) belong to a highly conserved family of eukaryotic phosphatases. They are protein tyrosine phosphatases that utilize inositol phospholipids, rather than phosphoproteins, as substrates. MTMR family members hydrolyze both Phosphatidylinositol 3-phosphate (PtdIns3P) and PtdIns(3,5)P2. MTMR2 interacts with MTMR5, an inactive family member that increases the enzymatic activity of MTMR2 and dictates its subcellular localization. Mutations in MTMR2 cause autosomal recessive Charcot-Marie-Tooth type 4B1 (CMT4B1), which is characterized by reduced nerve conduction velocities, focally folded myelin sheaths and demyelination. MTMR3 and MTMR4 can either interact with each other or self associate. MTMR6 regulates the activity of the calcium-activated potassium channel 3.1. MTMR9 regulates the activity of MTMR7 and MTMR8.

Supplier:  Bioss
Description:   Defects in G6PD are the cause of chronic non-spherocytic hemolytic anemia (CNSHA) . Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of CNSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class-IV have near normal activity.
Supplier:  Bioss
Description:   Defects in G6PD are the cause of chronic non-spherocytic hemolytic anemia (CNSHA) . Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of CNSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class-IV have near normal activity.
Supplier:  Bioss
Description:   Defects in G6PD are the cause of chronic non-spherocytic hemolytic anemia (CNSHA) . Deficiency of G6PD is associated with hemolytic anemia in two different situations. First, in areas in which malaria has been endemic, G6PD-deficiency alleles have reached high frequencies (1% to 50%) and deficient individuals, though essentially asymptomatic in the steady state, have a high risk of acute hemolytic attacks. Secondly, sporadic cases of G6PD deficiency occur at a very low frequencies, and they usually present a more severe phenotype. Several types of CNSHA are recognized. Class-I variants are associated with severe NSHA; class-II have an activity <10% of normal; class-III have an activity of 10% to 60% of normal; class-IV have near normal activity.

Supplier:  Bioss
Description:   Nucleotides are important extracellular signaling molecules that mediate several events, such as cell proliferation, differentiation, chemotaxis and cytokine release. The P2 receptor family is activated by the binding of nucleotides and is divided into two subfamilies, designated P2X and P2Y. The P2Y receptor family are G protein-coupled receptors that mediate the effects of extracellular nucleotides, primarily through the activation of phospholipase C (PLC). To some extent, the P2Y receptors can also activate potassium channels or, alternatively, inhibit adenylate cyclase and N-type calcium channels in response to extracellular nucleotides. P2Y10 (purinergic receptor P2Y, G-protein coupled, 10), also known as P2RY10, is a 339 amino acid multi-pass membrane protein that is thought to act as a receptor for purines coupled to G-proteins. P2Y10 is found at low levels in blood leukocytes and is upregulated during promyelocytic cell differentiation.
Supplier:  Bioss
Description:   Nucleotides are important extracellular signaling molecules that mediate several events, such as cell proliferation, differentiation, chemotaxis and cytokine release. The P2 receptor family is activated by the binding of nucleotides and is divided into two subfamilies, designated P2X and P2Y. The P2Y receptor family are G protein-coupled receptors that mediate the effects of extracellular nucleotides, primarily through the activation of phospholipase C (PLC). To some extent, the P2Y receptors can also activate potassium channels or, alternatively, inhibit adenylate cyclase and N-type calcium channels in response to extracellular nucleotides. P2Y10 (purinergic receptor P2Y, G-protein coupled, 10), also known as P2RY10, is a 339 amino acid multi-pass membrane protein that is thought to act as a receptor for purines coupled to G-proteins. P2Y10 is found at low levels in blood leukocytes and is upregulated during promyelocytic cell differentiation.
Catalog Number: (10110-898)

Supplier:  Prosci
Description:   HSPA1L is a 70kDa heat shock protein. In conjunction with other heat shock proteins, this protein stabilizes existing proteins against aggregation and mediates the folding of newly translated proteins in the cytosol and in organelles. This gene encodes a 70kDa heat shock protein. In conjunction with other heat shock proteins, this protein stabilizes existing proteins against aggregation and mediates the folding of newly translated proteins in the cytosol and in organelles. The gene is located in the major histocompatibility complex class III region, in a cluster with two closely related genes which also encode isoforms of the 70kDa heat shock protein. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.
Catalog Number: (10099-572)

Supplier:  Prosci
Description:   ATF6B (CREBL1) is a transcription factor in the unfolded protein response (UPR) pathway during ER stress. Either as a homodimer or as a heterodimer with ATF6-alpha, the protein binds to the ER stress response element, interacting with nuclear transcription factor Y to activate UPR target genes. ATF6B is normally found in the membrane of the endoplasmic reticulum; however, under ER stress, the N-terminal cytoplasmic domain is cleaved from the rest of the protein and translocates to the nucleus. Two transcript variants encoding different isoforms have been found for this gene.The protein encoded by this gene bears sequence similarity with the Creb/ATF subfamily of the bZip superfamily of transcription factors. It localizes to both the cytoplasm and the nucleus. The gene localizes to the major histocompatibility complex (MHC) class III region on chromosome 6.

Supplier:  Bioss
Description:   Myotubularin and the myotubularin-related proteins (MTMR1-9) belong to a highly conserved family of eukaryotic phosphatases. They are protein tyrosine phosphatases that utilize inositol phospholipids, rather than phosphoproteins, as substrates. MTMR family members hydrolyze both Phosphatidylinositol 3-phosphate (PtdIns3P) and PtdIns(3,5)P2. MTMR2 interacts with MTMR5, an inactive family member that increases the enzymatic activity of MTMR2 and dictates its subcellular localization. Mutations in MTMR2 cause autosomal recessive Charcot-Marie-Tooth type 4B1 (CMT4B1), which is characterized by reduced nerve conduction velocities, focally folded myelin sheaths and demyelination. MTMR3 and MTMR4 can either interact with each other or self associate. MTMR6 regulates the activity of the calcium-activated potassium channel 3.1. MTMR9 regulates the activity of MTMR7 and MTMR8.
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