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trans-4-Methoxycyclohexan-1-amine
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trans-4-Methoxycyclohexan-1-amine
Catalog Number:
(10671-998)
Supplier:
Bioss
Description:
SH3MD2 acts as a scaffold protein, contributes to Rac-induced signal transduction such as JNKs (MAPK8 and MAPK9) activation and induces apoptosis. Within a signaling complex, it probably recruits protein kinases such as MAP3K10 or MAP3K11 which are in turn activated leading to the sequential activation of MAP2K4, MAP2K7 and JNKs (MAPK8 and MAPK9). SH3MD2 may be involved in targeting of HIV-1 GAG and GAG-POL polyproteins to the plasma membrane. This gene encodes a protein containing an N-terminus RING-finger, four SH3 domains, and a region implicated in binding of the Rho GTPase Rac. Via the RING-finger, the encoded protein has been shown to function as an ubiquitin-protein ligase involved in protein sorting at the trans-Golgi network. The encoded protein may also act as a scaffold for the c-Jun N-terminal kinase signaling pathway, facilitating the formation of a functional signaling module. There are two named isoforms.
Catalog Number:
(10671-996)
Supplier:
Bioss
Description:
SH3MD2 acts as a scaffold protein, contributes to Rac-induced signal transduction such as JNKs (MAPK8 and MAPK9) activation and induces apoptosis. Within a signaling complex, it probably recruits protein kinases such as MAP3K10 or MAP3K11 which are in turn activated leading to the sequential activation of MAP2K4, MAP2K7 and JNKs (MAPK8 and MAPK9). SH3MD2 may be involved in targeting of HIV-1 GAG and GAG-POL polyproteins to the plasma membrane. This gene encodes a protein containing an N-terminus RING-finger, four SH3 domains, and a region implicated in binding of the Rho GTPase Rac. Via the RING-finger, the encoded protein has been shown to function as an ubiquitin-protein ligase involved in protein sorting at the trans-Golgi network. The encoded protein may also act as a scaffold for the c-Jun N-terminal kinase signaling pathway, facilitating the formation of a functional signaling module. There are two named isoforms.
Catalog Number:
(10347-792)
Supplier:
Bioss
Description:
The ankyrin repeat and SOCS box containing (ASB) protein family is comprised of members which each contain "SOCS boxes" but differ from other families of protein in the motifs they contain upstream of the SOCS box. SOCS boxes are carboxy terminal regions of homology found in the suppressor of cytokine signaling family of proteins. The box region is thought to be the point of interaction between SOCS proteins and E3 ubiquitin ligases. The SOCS box serves to couple suppressor of cytokine signalling (SOCS) proteins and their binding partners with the elongin B and C complex, possibly targeting them for degradation. The gene is induced by all trans retinoic acid. In myeloid leukemia cells, the expression of this encoded protein has been shown to induce growth inhibition and chromatin condensation. Multiple alternatively spliced transcript variants have been described for this gene but their full length sequences are not known.
Catalog Number:
(76082-914)
Supplier:
Bioss
Description:
The ankyrin repeat and SOCS box containing (ASB) protein family is comprised of members which each contain "SOCS boxes" but differ from other families of protein in the motifs they contain upstream of the SOCS box. SOCS boxes are carboxy terminal regions of homology found in the suppressor of cytokine signaling family of proteins. The box region is thought to be the point of interaction between SOCS proteins and E3 ubiquitin ligases. The SOCS box serves to couple suppressor of cytokine signalling (SOCS) proteins and their binding partners with the elongin B and C complex, possibly targeting them for degradation. The gene is induced by all trans retinoic acid. In myeloid leukemia cells, the expression of this encoded protein has been shown to induce growth inhibition and chromatin condensation. Multiple alternatively spliced transcript variants have been described for this gene but their full length sequences are not known.
Catalog Number:
(103010-440)
Supplier:
Anaspec Inc
Description:
B-Phycoerythrin (B-PE), a fluorescent protein from phycobiliprotein family, is isolated from cyanobacteria and eukaryotic algae. SMCC activated B-PE is chemically modified with SMCC. SMCC reacts with the primary amine on B-PE and introduces maleimide groups to B-PE. These maleimide groups easily react with thiol groups of target protein without the need for any additional activation, resulting in convenient conjugation of B-PE with proteins. Its primary absorption peak is at 545 nm with secondary peak at 563 nm. B-PE and the closely related R-PE are the most intensely fluorescent phycobiliproteins having orange fluorescence. They are significantly brighter and more photostable than conventional organic fluorophores. B-PE conjugates have been widely used in applications such as flow cytometry and multi-color immunofluorescent staining.
Catalog Number:
(10252-182)
Supplier:
Bioss
Description:
Adaptins are heterotetrameric subunits of adaptors, which are complexes involved in the formation of Clathrin-coated pits for vesicle-mediated endocytosis. Clathrin and its associated heterotetrameric protein complexes make up the main protein components of the coat surrounding the cytoplasmic face of coated vesicles. The Adaptin family, comprising a, b, and g classes, is also responsible for the transport of ligand-receptor complexes from plasma membranes and the trans-Golgi network to lysosomes. Two main types of adaptor proteins (APs), AP-1 and AP-2, are found in Clathrin-coated structures located at the Golgi complex and the plasma membrane of mammalian cells, respectively. Adaptor protein complex 2 (AP-2) is composed of two large Adaptins (a1A/AP2A1 and b1/AP2B1), a medium Adaptin (m2/AP-2m1) and a small Adaptin (s2 long/AP2S1). AP-2m1, a 435 amino acid protein, links Clathrin to receptors in coated vesicles.
Catalog Number:
(10263-832)
Supplier:
Bioss
Description:
Clathrin-coated pits and vesicles are assembled for receptor-mediated endocytosis through interaction with clathrin associated protein complexes. Vesicle transport is mediated from the trans-Golgi network by the adapter complex AP-1 and from the plasma membrane by the AP-2 complex. The AP-1 and AP-2 adapter protein complexes consist of clathrin binding adaptin proteins and two smaller subunits known as AP50 and AP17. The Alpha- and Beta-Adaptin chains have a similar two-domain organization with C-terminal domains that vary in both sequence and length. Alpha-Adaptin splice variants A and C display variable relative expression levels and differential distribution in different tissues. AP180 (also designated AP-3 or F1-20) is a synapse-specific clathrin assembly protein. The protein CALM (clathrin assembly protein lymphoid myeloid leukemia) is highly homologous to AP180 and may also be involved in clathrin assembly.
Catalog Number:
(10282-980)
Supplier:
Bioss
Description:
Clathrin-mediated endocytosis is the pathway by which many receptors for nutrients and hormones are internalized to be recycled or down-regulated. During formation of clathrin coated membranes, clathrin co-assembles with heterotetrameric molecules known as assembly polypeptides (APs) or adaptors which form a layer of protein coat between the clathrin lattice and the membrane. There are two characterized adaptors AP1 and AP2. AP1 is associated with clathrin coated vesicles at the trans-Golgi network and AP2 is associated with the endocytic clathrin coated vesicles at the plasma membrane and has been shown to specifically interact with Shc and EGF receptor. AP2 is composed of four subunits, two separate 100 kDa gene products with similar domain structures (alpha and beta adaptin) and a 50 and 17 kDa subunit. There are two alpha-adaptin genes, alpha A and alpha C which have a tissue specific pattern of expression.
Catalog Number:
(10263-838)
Supplier:
Bioss
Description:
Clathrin-coated pits and vesicles are assembled for receptor-mediated endocytosis through interaction with clathrin associated protein complexes. Vesicle transport is mediated from the trans-Golgi network by the adapter complex AP-1 and from the plasma membrane by the AP-2 complex. The AP-1 and AP-2 adapter protein complexes consist of clathrin binding adaptin proteins and two smaller subunits known as AP50 and AP17. The Alpha- and Beta-Adaptin chains have a similar two-domain organization with C-terminal domains that vary in both sequence and length. Alpha-Adaptin splice variants A and C display variable relative expression levels and differential distribution in different tissues. AP180 (also designated AP-3 or F1-20) is a synapse-specific clathrin assembly protein. The protein CALM (clathrin assembly protein lymphoid myeloid leukemia) is highly homologous to AP180 and may also be involved in clathrin assembly.
Catalog Number:
(10252-172)
Supplier:
Bioss
Description:
Adaptins are heterotetrameric subunits of adaptors, which are complexes involved in the formation of Clathrin-coated pits for vesicle-mediated endocytosis. Clathrin and its associated heterotetrameric protein complexes make up the main protein components of the coat surrounding the cytoplasmic face of coated vesicles. The Adaptin family, comprising a, b, and g classes, is also responsible for the transport of ligand-receptor complexes from plasma membranes and the trans-Golgi network to lysosomes. Two main types of adaptor proteins (APs), AP-1 and AP-2, are found in Clathrin-coated structures located at the Golgi complex and the plasma membrane of mammalian cells, respectively. Adaptor protein complex 2 (AP-2) is composed of two large Adaptins (a1A/AP2A1 and b1/AP2B1), a medium Adaptin (m2/AP-2m1) and a small Adaptin (s2 long/AP2S1). AP-2m1, a 435 amino acid protein, links Clathrin to receptors in coated vesicles.
Catalog Number:
(10265-390)
Supplier:
Bioss
Description:
The Drosophila atonal gene produces a protein with basic helix loop helix (bHLH) domains that plays an essential role in the development of the Drosophila nervous system. Mammalian atonal homolog 2 (MATH-2) is a helix-loop-helix (HLH) transcription factor that is structurally homologous to the product of Drosophila atonal gene. MATH-2 is a 337 amino acid protein with an atonal-related basic HLH domain. In mice, expression of MATH-2 takes place by embryonic day 11.5 and initially localizes to the wall of brain vesicles and in the spinal cord. It is expressed in the cortical plate and the mantle layer in the developing central nervous system, and is limited to the nervous system in adults. Adult mouse cerebrums produce a high level of MATH-2 RNA with lower levels in other neuronal tissues. Research studies suggest that MATH-2 may function as a trans-acting factor involved in the development and maintenance of the mammalian nervous system.
Catalog Number:
(10799-956)
Supplier:
Rockland Immunochemical
Description:
Aldh3A2 is a member of the aldehyde dehydrogenase superfamily, a group of NAD(P)(+)-dependent enzymes that catalyze the oxidation of a wide spectrum of aliphatic and aromatic aldehydes. Aldehyde dehydrogenase enzymes are thought to play a major role in the detoxification of aldehydes generated by alcohol metabolism and lipid peroxidation. Aldh3A2 catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Mutations in the Aldh3A2 gene cause Sjogren-Larrson syndrome, an inherited neurocutaneous disorder. Patients with this disorder display ichthyosis, mental retardation and spastic diplegia. The pathogenesis of the cutaneous and neurological symptoms is thought to result from abnormal lipid accumulation in the membranes of skin and brain, the formation of aldehyde Schiff base adducts with amine-containing lipids or proteins, or defective eicosanoid metabolism.
Catalog Number:
(10748-748)
Supplier:
Prosci
Description:
Aldh3A2 Antibody: Aldh3A2 is a member of the aldehyde dehydrogenase superfamily, a group of NAD(P)(+)-dependent enzymes that catalyze the oxidation of a wide spectrum of aliphatic and aromatic aldehydes. Aldehyde dehydrogenase enzymes are thought to play a major role in the detoxification of aldehydes generated by alcohol metabolism and lipid peroxidation. Aldh3A2 catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Mutations in the Aldh3A2 gene cause Sjogren-Larrson syndrome, an inherited neurocutaneous disorder. Patients with this disorder display ichthyosis, mental retardation and spastic diplegia. The pathogenesis of the cutaneous and neurological symptoms is thought to result from abnormal lipid accumulation in the membranes of skin and brain, the formation of aldehyde Schiff base adducts with amine-containing lipids or proteins, or defective eicosanoid metabolism.
Catalog Number:
(10263-834)
Supplier:
Bioss
Description:
Clathrin-coated pits and vesicles are assembled for receptor-mediated endocytosis through interaction with clathrin associated protein complexes. Vesicle transport is mediated from the trans-Golgi network by the adapter complex AP-1 and from the plasma membrane by the AP-2 complex. The AP-1 and AP-2 adapter protein complexes consist of clathrin binding adaptin proteins and two smaller subunits known as AP50 and AP17. The Alpha- and Beta-Adaptin chains have a similar two-domain organization with C-terminal domains that vary in both sequence and length. Alpha-Adaptin splice variants A and C display variable relative expression levels and differential distribution in different tissues. AP180 (also designated AP-3 or F1-20) is a synapse-specific clathrin assembly protein. The protein CALM (clathrin assembly protein lymphoid myeloid leukemia) is highly homologous to AP180 and may also be involved in clathrin assembly.
Catalog Number:
(10277-742)
Supplier:
Bioss
Description:
Clathrin-mediated endocytosis is the pathway by which many receptors for nutrients and hormones are internalized to be recycled or down-regulated. During formation of clathrin coated membranes, clathrin co-assembles with heterotetrameric molecules known as assembly polypeptides (APs) or adaptors which form a layer of protein coat between the clathrin lattice and the membrane. There are two characterized adaptors AP1 and AP2. AP1 is associated with clathrin coated vesicles at the trans-Golgi network and AP2 is associated with the endocytic clathrin coated vesicles at the plasma membrane and has been shown to specifically interact with Shc and EGF receptor. AP2 is composed of four subunits, two separate 100 kDa gene products with similar domain structures (alpha and beta adaptin) and a 50 and 17 kDa subunit. There are two alpha-adaptin genes, alpha A and alpha C which have a tissue specific pattern of expression.
Catalog Number:
(10252-178)
Supplier:
Bioss
Description:
Adaptins are heterotetrameric subunits of adaptors, which are complexes involved in the formation of Clathrin-coated pits for vesicle-mediated endocytosis. Clathrin and its associated heterotetrameric protein complexes make up the main protein components of the coat surrounding the cytoplasmic face of coated vesicles. The Adaptin family, comprising a, b, and g classes, is also responsible for the transport of ligand-receptor complexes from plasma membranes and the trans-Golgi network to lysosomes. Two main types of adaptor proteins (APs), AP-1 and AP-2, are found in Clathrin-coated structures located at the Golgi complex and the plasma membrane of mammalian cells, respectively. Adaptor protein complex 2 (AP-2) is composed of two large Adaptins (a1A/AP2A1 and b1/AP2B1), a medium Adaptin (m2/AP-2m1) and a small Adaptin (s2 long/AP2S1). AP-2m1, a 435 amino acid protein, links Clathrin to receptors in coated vesicles.
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