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Potassium+hexacyanoferrate(III)


13,372  results were found

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Supplier:  Bioss
Description:   Contactin 2 is a neuronal cell adhesion molecule (CAM) that influences the formation of axon connections in the developing nervous system. Contactin 2 is a member of the immunoglobulin superfamily (IgSF) and contains a glycosylphosphatidylinositol-anchor, six immunogobulin (Ig)-like and four Fibronectin type III (FNIII)-like domains. Contactin 2 is expressed predominantly during neural development on the cell membrane of axons in nerve fiber tracts in order to guide commissural axons without promoting their growth. Contactin 2 binds with NgCAM in the plane of the same membrane (cis-binding). The Contactin 2 heterophilic (Contactin 2/NgCAM and Contactin 2/NrCAM) binding sites are localized to the first four Ig domains. The Contactin 2 homophilic (Contactin 2/Contactin 2) binding site is localized to the FNIII domain.
Catalog Number: (76010-922)

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.
Catalog Number: (10813-990)

Supplier:  Prosci
Description:   FLT3 encodes a class III receptor tyrosine kinase that regulates hematopoiesis. The receptor consists of an extracellular domain composed of five immunoglobulin-like domains, one transmembrane region, and a cytoplasmic kinase domain split into two parts by a kinase-insert domain. The receptor is activated by binding of the fms-related tyrosine kinase 3 ligand to the extracellular domain, which induces homodimer formation in the plasma membrane leading to autophosphorylation of the receptor. The activated receptor kinase subsequently phosphorylates and activates multiple cytoplasmic effector molecules in pathways involved in apoptosis, proliferation, and differentiation of hematopoietic cells in bone marrow. Mutations that result in the constitutive activation of this receptor result in acute myeloid leukemia and acute lymphoblastic leukemia.
Catalog Number: (75929-676)

Supplier:  Rockland Immunochemical
Description:   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.

Supplier:  Bioss
Description:   Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity.
Catalog Number: (10291-976)

Supplier:  Bioss
Description:   FSD1L is a 530 amino acid protein containing one B30.2/SPRY domain, one COS domain, and a fibronectin type-III domain. Existing as three alternatively spliced isoforms, FSD1L is expressed primarily in brain, with lower levels of expression found in thymus, pituitary and testis. FSD1L may function in microtubule binding during interphase and is encoded by a gene that maps to human chromosome 9q31.2. Chromosome 9 consists of about 145 million bases andd comprises approximately 4% of the human genome and encodes nearly 900 genes. Considered to play a role in gender determination, deletion of the distal portion of 9p can lead to development of male to female sex reversal, the phenotype of a female with a male X,Y genotype.

Supplier:  Biotium
Description:   This antibody recognizes a protein of 50-65 kDa, identified as CD16 (Workshop IV; Code N39 ) (also known low affinity Fc receptor III for IgG (FcRIII) or Leu 11). CD16 exists as a polypepetide-anchored from (FCRIIIA or CD16A) on human natural killer (NK) cells and monocytes/ macrophages and as a glycosylphosphatidylinositol (GPI)-anchored form (FcRIIIB or CD16B) on neutrophils. CD16B is polymorphic and the two alleles are termed NA1 and NA2.3 CD16 plays a role in signal transduction, NK cell activation and antibody-dependent cellular cytotoxicity. This MAb has been showed to inhibit the binding of immune complex to NK cells, inhibit cytotoxicity of NK cells, and induce calcium fluxes in NK cells and neutrophils.
Supplier:  Biotium
Description:   This antibody recognizes a protein of 50-65 kDa, identified as CD16 (Workshop IV; Code N39 ) (also known low affinity Fc receptor III for IgG (FcRIII) or Leu 11). CD16 exists as a polypepetide-anchored from (FCRIIIA or CD16A) on human natural killer (NK) cells and monocytes/ macrophages and as a glycosylphosphatidylinositol (GPI)-anchored form (FcRIIIB or CD16B) on neutrophils. CD16B is polymorphic and the two alleles are termed NA1 and NA2.3 CD16 plays a role in signal transduction, NK cell activation and antibody-dependent cellular cytotoxicity. This MAb has been showed to inhibit the binding of immune complex to NK cells, inhibit cytotoxicity of NK cells, and induce calcium fluxes in NK cells and neutrophils.

Supplier:  Bioss
Description:   RIMS-binding proteins (RIM-BPs) serve as adaptors during vesicle fusion and release by forming links between synaptic-vesicle fusion apparatuses and calcium channels. Specifically, RIM-BP2 (RIMS binding protein 2), also known as RBP2, is a 1,052 amino acid protein that links L-type Ca++ CP Alpha1D, N-type Ca++ CP Alpha1B, Rim1 and Rim2 during synaptic transmission. RIM-BP2 contains three fibronectin type-III domains and three SH3 domains, which are used to mediate binding to a proline-rich motifs. Existing as three alternatively spliced isoforms, RIM-BP2 is encoded by a gene that maps to human chromosome 12q24.33 and mouse chromosome 5 G1.3.
Supplier:  Bioss
Description:   Myotubularin-related protein 14 (MTMR14), also known as Jumpy, is a myotubularin-related phosphoinositol-3-phosphate (PI3P) phosphatase (1). Mutations in the MTMR14 gene have been associated with centronuclear myopathy (1). MTMR14 deficiency in mice leads to altered calcium homeostasis and muscle disorders (2). MTMR14 has also been shown to play a role in autophagy, a process that is highly regulated by phosphatidylinositides through the type III PI3K, Vps34 (3). MTMR14 was localized to autophagic isolation membranes and early autophagosomes (3). In these studies, MTMR14 inhibited autophagy and mutations of MTMR14 associated with centronuclear myopathy were also defective in autophagy inhibition. In zebrafish, MTMR14 knockdown was shown to increase the number of autophagosomes, suggesting that its activity is associated with an inhibition of autophagy (4).

Supplier:  Bioss
Description:   Cell adhesion molecules influence cell growth, differentiation, embryogenesis, immune response and cancer metastasis by networking information from the extracellular matrix to the cell. Sidekick-1 (SDK1) is a 2,213 amino acid single-pass membrane protein that functions as a cell adhesion molecule by guiding axonal terminals to specific synapses in developing neurons. Existing as three alternatively spliced isoforms, Sidekick-1 is expressed in retinal neurons and contains thirteen fibronectin type-III domains and six Ig-like C2-type (immunoglobulin-like) domains. Sidekick-1 expression is upregulated in glomeruli of patients with HIV-associated nephropathy, where it leads to podocyte dysfunction. The gene encoding Sidekick-1 maps to human chromosome 7p22.2 and murine chromosome 5 G2.
Supplier:  Biotium
Description:   This antibody recognizes a cell surface glycoprotein of 95/115/135 kDa (depending upon the extent of glycosylation), identified as CD43 (Workshop III). 70-90% of T-cell lymphomas and from 22-37% of B-cell lymphomas express CD43. No reactivity has been observed with reactive B-cells. So a B-lineage population that co-expresses CD43 is highly likely to be a malignant lymphoma, especially a low-grade lymphoma, rather than a reactive B-cell population. When CD43 antibody is used in combination with anti-CD20, effective immunophenotyping of the lymphomas in formalin-fixed tissues can be obtained. Co-staining of a lymphoid infiltrate with anti-CD20 and anti-CD43 argues against a reactive process and favors a diagnosis of lymphoma.
Supplier:  Bioss
Description:   Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity.
Catalog Number: (10335-510)

Supplier:  Bioss
Description:   Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity.
Supplier:  Bioss
Description:   Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on each monomer. Physiological concentrations of potassium ion antagonize the binding of both divalent cations, especially affecting high-affinity calcium-binding sites. Binds to and initiates the activation of STK38 by releasing autoinhibitory intramolecular interactions within the kinase. Interaction with AGER after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling. Could assist ATAD3A cytoplasmic processing, preventing aggregation and favoring mitochondrial localization. May mediate calcium-dependent regulation on many physiological processes by interacting with other proteins, such as TPR-containing proteins, and modulating their activity.
Supplier:  Bioss
Description:   Contactin 2 is a neuronal cell adhesion molecule (CAM) that influences the formation of axon connections in the developing nervous system. Contactin 2 is a member of the immunoglobulin superfamily (IgSF) and contains a glycosylphosphatidylinositol-anchor, six immunogobulin (Ig)-like and four Fibronectin type III (FNIII)-like domains. Contactin 2 is expressed predominantly during neural development on the cell membrane of axons in nerve fiber tracts in order to guide commissural axons without promoting their growth. Contactin 2 binds with NgCAM in the plane of the same membrane (cis-binding). The Contactin 2 heterophilic (Contactin 2/NgCAM and Contactin 2/NrCAM) binding sites are localized to the first four Ig domains. The Contactin 2 homophilic (Contactin 2/Contactin 2) binding site is localized to the FNIII domain.
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