45416 Results for: "L-beta-Homoproline+hydrochloride"

Supplier: ProSci Inc.

THRB is a nuclear hormone receptor for triiodothyronine. It is one of the several receptors for thyroid hormone, and has been shown to mediate the biological activities of thyroid hormone. Knockout studies in mice suggest that the different receptors, while having certain extent of redundancy, may mediate different functions of thyroid hormone. Defects in this gene are known to be a cause of generalized thyroid hormone resistance (GTHR), a syndrome characterized by goiter and high levels of circulating thyroid hormone (T3-T4), with normal or slightly elevated thyroid stimulating hormone (TSH). Several transcript variants have been observed for this gene, but the full-length nature of only one has been determined so far.

Supplier: ProSci Inc.

Nicotinic acetylcholine receptors (nAChRs) are ligand-gated ion channels nAChRs are pentameric structures that are made up of combinations of individual subunits. CHRNB3 is one of the subunits of nAChR. Twelve neuronal nAChR subunits have been described, alpha2-alpha10 and beta2-beta4. CHRNB3 decreased the channel mean open time and burst length. There was also an increase in single channel slope conductance. On the other hand, the calcium permeability and the pharmacological properties of beta3-containing receptors differed little from those of without beta3. Dysfunction of nAChR has been linked to a number of human diseases such as schizophrenia, Alzheimer's and Parkinson's diseases. nAChRs also play a significant role in nicotine addiction.

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ST3gal6 Antibody: Sialyltransferases catalyze the transfer of sialic acid from cytidine 5-prime monophospho-N-acetylneuraminic acid (CMP-NeuAc) to terminal positions of glycoprotein and glycolipid carbohydrate groups. Terminal NeuAc residues are key determinants of carbohydrate structures, such as the sialyl-Lewis X determinants, and are widely distributed in many cell types. However, cancer cells often express more heavily sialylated glycans on their cell surface and this feature sometimes correlates with invasiveness. In contrast, expression of ST3gal6, a member of the sialyltransferase family that sialylates type II lactosamine structures on glycoproteins and glycolipids, was found to be significantly decreased by hypermethylation of the gene in gastrointestinal cancer. At least three isoforms of ST3gal6 are known to exist.

Supplier: ProSci Inc.

NFKB1 (MIM 164011) or NFKB2 (MIM 164012) is bound to REL (MIM 164910), RELA (MIM 164014), or RELB (MIM 604758) to form the NFKB complex. The NFKB complex is inhibited by I-kappa-B proteins (NFKBIA, MIM 164008, or NFKBIB), which inactivate NF-kappa-B by trapping it in the cytoplasm. Phosphorylation of serine residues on the I-kappa-B proteins by kinases (IKBKA, MIM 600664 or IKBKB, MIM 603258) marks them for destruction via the ubiquitination pathway, thereby allowing activation of the NF-kappa-B complex. Activated NFKB complex translocates into the nucleus and binds DNA at kappa-B-binding motifs such as 5-prime GGGRNNYYCC 3-prime or 5-prime HGGARNYYCC 3-prime (where H is A, C, or T; R is an A or G purine; and Y is a C or T pyrimidine).

Supplier: ProSci Inc.

NFKB1 (MIM 164011) or NFKB2 (MIM 164012) is bound to REL (MIM 164910), RELA (MIM 164014), or RELB (MIM 604758) to form the NFKB complex. The NFKB complex is inhibited by I-kappa-B proteins (NFKBIA, MIM 164008, or NFKBIB), which inactivate NF-kappa-B by trapping it in the cytoplasm. Phosphorylation of serine residues on the I-kappa-B proteins by kinases (IKBKA, MIM 600664 or IKBKB, MIM 603258) marks them for destruction via the ubiquitination pathway, thereby allowing activation of the NF-kappa-B complex. Activated NFKB complex translocates into the nucleus and binds DNA at kappa-B-binding motifs such as 5-prime GGGRNNYYCC 3-prime or 5-prime HGGARNYYCC 3-prime (where H is A, C, or T; R is an A or G purine; and Y is a C or T pyrimidine).

Supplier: ProSci Inc.

ST3GAL2 is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The protein is normally found in the Golgi but can be proteolytically processed to a soluble form. This protein, which is a member of glycosyltransferase family 29, can use the same acceptor substrates as does sialyltransferase 4A.The protein encoded by this gene is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The encoded protein is normally found in the Golgi but can be proteolytically processed to a soluble form. This protein, which is a member of glycosyltransferase family 29, can use the same acceptor substrates as does sialyltransferase 4A.

Supplier: Bioss

Nail-patella syndrome (NPS) is an autosomal dominant disorder characterized by dyplasia of finger nails, skeletal anomalies and, frequently, renal disease. NPS is caused by putative loss-of-function mutations in the transcription factor LMX1B. LMX1B belongs to the LIM-homeodomain family, members of which are known to be important for pattern formation during development. Twenty-two novel mutations may occur in the gene encoding LMX1B and the type and distribution of the mutations support the hypothesis that NPS is the result of haploinsufficiency for LMX1B. LMX1B is also necessary for normal development of the eye and in regulating dopaminergic neurogenesis and may be involved in developmental glaucoma and the aetiology of idiopathic Parkinson’s disease. Specifically, LMX1B along with LIM1 control the initial trajectory of motor axons in the developing mammalian limb. In addition, LMX1B directly regulates the coordinated expression of alpha 3(IV) and alpha 4(IV) collagen required for normal glomerular basement membrane (GBM) morphogenesis, and the dysregulation of LMX1B in GBM contributes to the renal pathology and nephrosis in NPS.

Supplier: Bioss

Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. The protein encoded by this gene is one of the PKC family members. This protein kinase has been reported to be involved in many different cellular functions, such as B cell activation, apoptosis induction, endothelial cell proliferation, and intestinal sugar absorption. Studies in mice also suggest that this kinase may also regulate neuronal functions and correlate fear-induced conflict behavior after stress. Alternatively spliced transcript variants encoding distinct isoforms have been reported. [provided by RefSeq, Jul 2008]

Supplier: Bioss

Nail-patella syndrome (NPS) is an autosomal dominant disorder characterized by dyplasia of finger nails, skeletal anomalies and, frequently, renal disease. NPS is caused by putative loss-of-function mutations in the transcription factor LMX1B. LMX1B belongs to the LIM-homeodomain family, members of which are known to be important for pattern formation during development. Twenty-two novel mutations may occur in the gene encoding LMX1B and the type and distribution of the mutations support the hypothesis that NPS is the result of haploinsufficiency for LMX1B. LMX1B is also necessary for normal development of the eye and in regulating dopaminergic neurogenesis and may be involved in developmental glaucoma and the aetiology of idiopathic Parkinson’s disease. Specifically, LMX1B along with LIM1 control the initial trajectory of motor axons in the developing mammalian limb. In addition, LMX1B directly regulates the coordinated expression of alpha 3(IV) and alpha 4(IV) collagen required for normal glomerular basement membrane (GBM) morphogenesis, and the dysregulation of LMX1B in GBM contributes to the renal pathology and nephrosis in NPS.

Supplier: Bioss

Subunit of both mTORC1 and mTORC2, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino-acids. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino-acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation.Tissue specificity:Broadly expressed, with highest levels in skeletal muscle, heart and kidney.

Supplier: Bioss

Subunit of both mTORC1 and mTORC2, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino-acids. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino-acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation.Tissue specificity:Broadly expressed, with highest levels in skeletal muscle, heart and kidney.

Supplier: Bioss

Crystallins are the major proteins of the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. Crystallins are divided into a, b, and g families, and the b- and g-crystallins also comprise a superfamily. Crystallins usually contain seven distinctive protein regions, including four homologous motifs, a connecting peptide, and N- and C-terminal extensions. b-crystallins constitute the major lens structural proteins. They associate into dimers, tetramers, and higher order aggregates. The b-crystallin subfamily is composed of several gene products, including bA1-, bA2-, bA3-, bA4-, bB1-, bB2- and bB3-crystallin. The bA1- and bA3-crystallin proteins are encoded by a single mRNA. They differ by only 17 amino acids, and bA1-crystallin is generated by use of an alternate translation initiation site. The genes for bA4-, bB1-, bB2- and bB3-crystallin are clustered on human chromosome 22q11, while the genes for bA3/A1- and bA2-crystallin map to human chromosomes 17q11 and 2q34, respectively.

Supplier: Bioss

Nail-patella syndrome (NPS) is an autosomal dominant disorder characterized by dyplasia of finger nails, skeletal anomalies and, frequently, renal disease. NPS is caused by putative loss-of-function mutations in the transcription factor LMX1B. LMX1B belongs to the LIM-homeodomain family, members of which are known to be important for pattern formation during development. Twenty-two novel mutations may occur in the gene encoding LMX1B and the type and distribution of the mutations support the hypothesis that NPS is the result of haploinsufficiency for LMX1B. LMX1B is also necessary for normal development of the eye and in regulating dopaminergic neurogenesis and may be involved in developmental glaucoma and the aetiology of idiopathic Parkinson’s disease. Specifically, LMX1B along with LIM1 control the initial trajectory of motor axons in the developing mammalian limb. In addition, LMX1B directly regulates the coordinated expression of alpha 3(IV) and alpha 4(IV) collagen required for normal glomerular basement membrane (GBM) morphogenesis, and the dysregulation of LMX1B in GBM contributes to the renal pathology and nephrosis in NPS.

Supplier: Bioss

Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) containing a single core motif half-site 5'-AGGTCA-3' preceded by a short A-T-rich sequence. Considered to have intrinsic transcriptional activity, have some natural ligands such as all-trans retinoic acid (ATRA) and other retinoids which act as inverse agonists repressing the transcriptional activity. Required for normal postnatal development of rod and cone photoreceptor cells. Modulates rod photoreceptors differentiation at least by inducing the transcription factor NRL-mediated pathway. In cone photoreceptor cells, regulates transcription of OPN1SW. Involved in the regulation of the period length and stability of the circadian rhythm. May control cytoarchitectural patterning of neocortical neurons during development. May act in a dose-dependent manner to regulate barrel formation upon innervation of layer IV neurons by thalamocortical axons. May play a role in the suppression of osteoblastic differentiation through the inhibition of RUNX2 transcriptional activity (By similarity)

Supplier: Bioss

CCT2 is one of eight largely unrelated subunit proteins found in a protein chaperone complex known as the chaperonin-containing TCP-1 (CCT) or TRiC complex. The CCT complex is an abundanct cytoslic component that is credited with helping newly synthesized polypeptides adopt the correct conformation (1). Proteins that fold and assemble with the help of CCT include the cytoskeletal proteins actin and tubulin as well as up to 15% of newly synthesized eukaryotic proteins (2). CCT2 is the β-subunit of the chaperone complex and is one of several CCT proteins that exhibit increased expression in response to stress. This implies that the CCT complex helps cells recover from protein damage by assisting in protein folding and assembly (3). CCT subunit levels also change throughout the cell cycle, with lower proteins levels (and reduced chaperone activity) found during induced cell cycle arrest during at M phase (4). Each CCT subunit is thought to perform a specific function during protein folding and assembly (5); CCT2 exhibits both actin and tubulin binding activities (6,3) but the exact molecular function on this subunit remains uncertain.

Supplier: Bioss

Crystallins are the major proteins of the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. Crystallins are divided into a, b, and g families, and the b- and g-crystallins also comprise a superfamily. Crystallins usually contain seven distinctive protein regions, including four homologous motifs, a connecting peptide, and N- and C-terminal extensions. b-crystallins constitute the major lens structural proteins. They associate into dimers, tetramers, and higher order aggregates. The b-crystallin subfamily is composed of several gene products, including bA1-, bA2-, bA3-, bA4-, bB1-, bB2- and bB3-crystallin. The bA1- and bA3-crystallin proteins are encoded by a single mRNA. They differ by only 17 amino acids, and bA1-crystallin is generated by use of an alternate translation initiation site. The genes for bA4-, bB1-, bB2- and bB3-crystallin are clustered on human chromosome 22q11, while the genes for bA3/A1- and bA2-crystallin map to human chromosomes 17q11 and 2q34, respectively.

Supplier: Bioss

Crystallins are the major proteins of the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. Crystallins are divided into a, b, and g families, and the b- and g-crystallins also comprise a superfamily. Crystallins usually contain seven distinctive protein regions, including four homologous motifs, a connecting peptide, and N- and C-terminal extensions. b-crystallins constitute the major lens structural proteins. They associate into dimers, tetramers, and higher order aggregates. The b-crystallin subfamily is composed of several gene products, including bA1-, bA2-, bA3-, bA4-, bB1-, bB2- and bB3-crystallin. The bA1- and bA3-crystallin proteins are encoded by a single mRNA. They differ by only 17 amino acids, and bA1-crystallin is generated by use of an alternate translation initiation site. The genes for bA4-, bB1-, bB2- and bB3-crystallin are clustered on human chromosome 22q11, while the genes for bA3/A1- and bA2-crystallin map to human chromosomes 17q11 and 2q34, respectively.

Supplier: Bioss

Nail-patella syndrome (NPS) is an autosomal dominant disorder characterized by dyplasia of finger nails, skeletal anomalies and, frequently, renal disease. NPS is caused by putative loss-of-function mutations in the transcription factor LMX1B. LMX1B belongs to the LIM-homeodomain family, members of which are known to be important for pattern formation during development. Twenty-two novel mutations may occur in the gene encoding LMX1B and the type and distribution of the mutations support the hypothesis that NPS is the result of haploinsufficiency for LMX1B. LMX1B is also necessary for normal development of the eye and in regulating dopaminergic neurogenesis and may be involved in developmental glaucoma and the aetiology of idiopathic Parkinson’s disease. Specifically, LMX1B along with LIM1 control the initial trajectory of motor axons in the developing mammalian limb. In addition, LMX1B directly regulates the coordinated expression of alpha 3(IV) and alpha 4(IV) collagen required for normal glomerular basement membrane (GBM) morphogenesis, and the dysregulation of LMX1B in GBM contributes to the renal pathology and nephrosis in NPS.

Supplier: Bioss

Nail-patella syndrome (NPS) is an autosomal dominant disorder characterized by dyplasia of finger nails, skeletal anomalies and, frequently, renal disease. NPS is caused by putative loss-of-function mutations in the transcription factor LMX1B. LMX1B belongs to the LIM-homeodomain family, members of which are known to be important for pattern formation during development. Twenty-two novel mutations may occur in the gene encoding LMX1B and the type and distribution of the mutations support the hypothesis that NPS is the result of haploinsufficiency for LMX1B. LMX1B is also necessary for normal development of the eye and in regulating dopaminergic neurogenesis and may be involved in developmental glaucoma and the aetiology of idiopathic Parkinson’s disease. Specifically, LMX1B along with LIM1 control the initial trajectory of motor axons in the developing mammalian limb. In addition, LMX1B directly regulates the coordinated expression of alpha 3(IV) and alpha 4(IV) collagen required for normal glomerular basement membrane (GBM) morphogenesis, and the dysregulation of LMX1B in GBM contributes to the renal pathology and nephrosis in NPS.

Supplier: Bioss

Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. The protein encoded by this gene is one of the PKC family members. This protein kinase has been reported to be involved in many different cellular functions, such as B cell activation, apoptosis induction, endothelial cell proliferation, and intestinal sugar absorption. Studies in mice also suggest that this kinase may also regulate neuronal functions and correlate fear-induced conflict behavior after stress. Alternatively spliced transcript variants encoding distinct isoforms have been reported. [provided by RefSeq, Jul 2008]

Supplier: Bioss

5 to 10^8 cells/test. It is recommended that the antibody be carefully titrated for optimal performance in the assay of interest. Excitation: 488-561 nm; Emission: 578 nm; Laser: Blue Laser, Green Laser, Yellow-Green Laser This complex is recognized by invariant natural killer T (iNKT) cells, a subset of T lymphocytes that expresses the invariant TCR alpha chain Va14Ja18. Activation of iNKT cells leads to production of Th1 and Th2-associated cytokines as well as dendritic cell maturation.

Supplier: Bioss

Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. The protein encoded by this gene is one of the PKC family members. This protein kinase has been reported to be involved in many different cellular functions, such as B cell activation, apoptosis induction, endothelial cell proliferation, and intestinal sugar absorption. Studies in mice also suggest that this kinase may also regulate neuronal functions and correlate fear-induced conflict behavior after stress. Alternatively spliced transcript variants encoding distinct isoforms have been reported. [provided by RefSeq, Jul 2008]

Supplier: Bioss

Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. The protein encoded by this gene is one of the PKC family members. This protein kinase has been reported to be involved in many different cellular functions, such as B cell activation, apoptosis induction, endothelial cell proliferation, and intestinal sugar absorption. Studies in mice also suggest that this kinase may also regulate neuronal functions and correlate fear-induced conflict behavior after stress. Alternatively spliced transcript variants encoding distinct isoforms have been reported. [provided by RefSeq, Jul 2008]

Supplier: Bioss

Subunit of both mTORC1 and mTORC2, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino-acids. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino-acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation.Tissue specificity:Broadly expressed, with highest levels in skeletal muscle, heart and kidney.

Supplier: Bioss

Nail-patella syndrome (NPS) is an autosomal dominant disorder characterized by dyplasia of finger nails, skeletal anomalies and, frequently, renal disease. NPS is caused by putative loss-of-function mutations in the transcription factor LMX1B. LMX1B belongs to the LIM-homeodomain family, members of which are known to be important for pattern formation during development. Twenty-two novel mutations may occur in the gene encoding LMX1B and the type and distribution of the mutations support the hypothesis that NPS is the result of haploinsufficiency for LMX1B. LMX1B is also necessary for normal development of the eye and in regulating dopaminergic neurogenesis and may be involved in developmental glaucoma and the aetiology of idiopathic Parkinson’s disease. Specifically, LMX1B along with LIM1 control the initial trajectory of motor axons in the developing mammalian limb. In addition, LMX1B directly regulates the coordinated expression of alpha 3(IV) and alpha 4(IV) collagen required for normal glomerular basement membrane (GBM) morphogenesis, and the dysregulation of LMX1B in GBM contributes to the renal pathology and nephrosis in NPS.

Supplier: Bioss

Subunit of both mTORC1 and mTORC2, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino-acids. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino-acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation.Tissue specificity:Broadly expressed, with highest levels in skeletal muscle, heart and kidney.

Supplier: Bioss

Nuclear receptor that binds DNA as a monomer to ROR response elements (RORE) containing a single core motif half-site 5'-AGGTCA-3' preceded by a short A-T-rich sequence. Considered to have intrinsic transcriptional activity, have some natural ligands such as all-trans retinoic acid (ATRA) and other retinoids which act as inverse agonists repressing the transcriptional activity. Required for normal postnatal development of rod and cone photoreceptor cells. Modulates rod photoreceptors differentiation at least by inducing the transcription factor NRL-mediated pathway. In cone photoreceptor cells, regulates transcription of OPN1SW. Involved in the regulation of the period length and stability of the circadian rhythm. May control cytoarchitectural patterning of neocortical neurons during development. May act in a dose-dependent manner to regulate barrel formation upon innervation of layer IV neurons by thalamocortical axons. May play a role in the suppression of osteoblastic differentiation through the inhibition of RUNX2 transcriptional activity (By similarity)

Supplier: Abcam

Recombinant Human Alpha-synuclein protein monomer (Active) is a Human Full Length SNCA protein, in the 1 to 140 aa range with >95% purity, <5 EU/ml endotoxin level and suitable for western blot, Functional studies and SDS-PAGE. The predicted molecular weight of recombinant protein is 14,5 kDa. - Suitable for Thioflavin T Fluorescence assay - Save time and ensure accurate results - use recombinant Alpha-synuclein (SNCA) protein - Optimal protein bioactivity, stability and reproducibility.

Supplier: Bioss

Subunit of both mTORC1 and mTORC2, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino-acids. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino-acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation.Tissue specificity:Broadly expressed, with highest levels in skeletal muscle, heart and kidney.

Supplier: Bioss

CCT2 is one of eight largely unrelated subunit proteins found in a protein chaperone complex known as the chaperonin-containing TCP-1 (CCT) or TRiC complex. The CCT complex is an abundanct cytoslic component that is credited with helping newly synthesized polypeptides adopt the correct conformation (1). Proteins that fold and assemble with the help of CCT include the cytoskeletal proteins actin and tubulin as well as up to 15% of newly synthesized eukaryotic proteins (2). CCT2 is the β-subunit of the chaperone complex and is one of several CCT proteins that exhibit increased expression in response to stress. This implies that the CCT complex helps cells recover from protein damage by assisting in protein folding and assembly (3). CCT subunit levels also change throughout the cell cycle, with lower proteins levels (and reduced chaperone activity) found during induced cell cycle arrest during at M phase (4). Each CCT subunit is thought to perform a specific function during protein folding and assembly (5); CCT2 exhibits both actin and tubulin binding activities (6,3) but the exact molecular function on this subunit remains uncertain.