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(S)-3-Amino-5-hexynoic+acid+hydrochloride


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Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-8161R-HRP
Lokale Artikelnummer:: BOSSBS-8161R-HRP
Beschreibung:   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.
VE:  1 * 100 µl

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-8161R-A555
Lokale Artikelnummer:: BOSSBS-8161R-A555
Beschreibung:   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.
VE:  1 * 100 µl

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-7961R-A680
Lokale Artikelnummer:: BOSSBS-7961R-A680
Beschreibung:   Ankyrin is a membrane protein that mediates the attachment of the erythrocyte membrane skeleton to the plasma membrane and interacts with CD44 and inositol triphosphate. It contains three functional domains: a conserved N-terminal ankyrin repeat domain (ARD(consisting of 2224 tandem repeats of 33 amino acids), a spectrin binding domain and a variably sised C-terminal regulatory domain. The ankyrin repeat is a 33-residue motif in proteins consisting of two alpha helices separated by loops. It has been studied using multiple sequence alignment to determine which conserved amino acid residues are critical for folding and stability. Ankyrin-repeat proteins have been associated with a number of human diseases; most notably, the cell cycle inhibitor p16 is associated with cancer and the Notch protein is a key component of cell signaling pathways whose intracellular repeat domain is disrupted in mutations that give rise to the neurological disorder known as CADASIL.
VE:  1 * 100 µl

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-8161R-A488
Lokale Artikelnummer:: BOSSBS-8161R-A488
Beschreibung:   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.
VE:  1 * 100 µl

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-11879R-A680
Lokale Artikelnummer:: BOSSBS-11879R-A680
Beschreibung:   The leucine-rich (LRR) repeat is a 20 to 30 amino acid motif that forms a hydrophobic å/ horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. Leucine-rich glioma-inactivated protein 3 (LGI3), also known as LGI1-like protein 4 (LGIL4) or leucine-rich repeat LGI family member 3, is a 548 amino acid secretory protein. LGI3 contains five LRR repeats and seven EAR repeats. Widely expressed, with highest levels in brain and lung, LGI3 has been shown to colocalize with endocytosis-associated proteins, lipid raft markers, and Syntaxin. The gene encoding LGI3 maps to chromosome 8p21.3.
VE:  1 * 100 µl

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-11944R-A750
Lokale Artikelnummer:: BOSSBS-11944R-A750
Beschreibung:   RILPL2 is a 211 amino acid protein that belongs to the RILPL family. RILPL2 does not regulate lysosomal morphology or distribution. RILPL2 shares 32% and 18% amino acid identity with RILPL1 and RILP, respectively. RILPL2 as a novel interacting partner for the actin-based molecular motor MyoVa, and has a novel role for RILPL2 in controlling neuronal morphogenesis. It has been suggested that there is also a novel role for RILPL2 in the regulation of cellular shape and dendritic-spine morphogenesis, probably via the Rac1-Pak pathway. PCR analysis of human tissues detects highest RILPL2 expression in lung, followed by placenta. Lower expression is detected in liver, kidney, pancreas, heart and brain, but no expression is detected in skeletal muscle. The RILPL2 gene is conserved in chimpanzee, dog, cow, mouse, rat, chicken and zebrafish, and maps to human chromosome 12q24.31.
VE:  1 * 100 µl

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-12312R-A680
Lokale Artikelnummer:: BOSSBS-12312R-A680
Beschreibung:   The leucine-rich (LRR) repeat is a 20 to 30 amino acid motif that forms a hydrophobic / horseshoe fold, allowing it to accommodate several leucine residues within a tightly packed core. All LRR repeats contain a variable segment and a highly conserved segment, the latter of which accounts for 11 or 12 residues of the entire LRR motif. The primary function of these motifs is to provide a versatile structural framework to mediate the formation of protein-protein interactions. LRRs are present in a variety of proteins with diverse structure and function, including innate immunity and nervous system development. Several human diseases are associated with mutations in genes encoding LRR-containing proteins. The leucine-rich repeat-containing protein 39 (LRRC39) is a 335 amino acid protein that contains nine LRR repeats and exists as two alternatively spliced isoforms.
VE:  1 * 100 µl
Lieferant:  Biotium
Beschreibung:   This MAb recognizes full-length MUC1 in a glycosylation-independent manner and can bind to the fully glycosylated protein. The dominant epitope of this MAb is APDTR in the VNTR region. It reacts with the core peptide of the MUC1 protein, which is a member of a family of mucin glycoproteins that are characterized by high carbohydrate content, O-linked oligosaccharides, high molecular weight (>200 kDa) and an amino acid composition rich in serine, threonine, proline and glycine. The core protein contains a domain of 20 amino-acid tandem repeats that functions as multiple epitopes for the MAb. Incomplete glycosylation of some tumor-associated mucins may lead to variable unmasking of the multiple peptide epitopes leading to the observed differences in staining intensity between normal and malignant tissues. This MAb reacts with both normal and malignant epithelia of various tissues including breast and colon.

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-13719R-A488
Lokale Artikelnummer:: BOSSBS-13719R-A488
Beschreibung:   FERM domains are roughly 150 amino acids in length and are found in a number of cytoskeletal-associated proteins such as Ezrin, Radixin, Moesin and 4.1 (erythrocyte membrane protein band 4.1), where they provide a link between cytoskeletal signals and membrane dynamics. EPB41L5 (erythrocyte membrane protein band 4.1 like 5), also known as BE37 or YMO1, is a 733 amino acid cytoplasmic protein that contains one FERM domain, which it uses to bind CRB1 (crumbs homolog 1). EPB41L5 is a homolog of zebrafish 'mosaic eyes' (moe), and is widely expressed but found at highest levels in ovary, kidney and brain, and is known to colocalize with _-catenin. EPB41L5 may participate in tight junction positioning during the establishment of epithelial cell polarity, and exists as four alternatively spliced isoforms that are encoded by a gene located on human chromosome 2q14.2.
VE:  1 * 100 µl

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-13126R-A750
Lokale Artikelnummer:: BOSSBS-13126R-A750
Beschreibung:   A gene of chromosome 6q23 encodes the 640 amino acid protein, EYA4 (eyes absent) (1). EYA is one of four members of the eyes absent family (1). A 271 amino acid domain at the carboxyl terminal is highly conserved amongst the members of the eyes absent family (1). EYA4 is expressed in the craniofacial mesenchyme, the dermamyotome, and the limb (1). The conserved region in other EYA proteins interacts with SIX, DACH, and G-proteins, which regulate transcription in early embryonic development (1,2,3,4). SIX translocates EYA1-3 to the nucleus, and G-proteins can stop this interaction (3,4). Premature stop codon mutations in EYA4 cause postlingual, progressive autosomal dominant hearing loss in humans (2). This shows that EYA4 is also vital to the mature organ of Corti (2). EYA4 may cause oculo-dento-digital syndrome, based on its expression pattern and map postion (1).
VE:  1 * 100 µl

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-13719R-A555
Lokale Artikelnummer:: BOSSBS-13719R-A555
Beschreibung:   FERM domains are roughly 150 amino acids in length and are found in a number of cytoskeletal-associated proteins such as Ezrin, Radixin, Moesin and 4.1 (erythrocyte membrane protein band 4.1), where they provide a link between cytoskeletal signals and membrane dynamics. EPB41L5 (erythrocyte membrane protein band 4.1 like 5), also known as BE37 or YMO1, is a 733 amino acid cytoplasmic protein that contains one FERM domain, which it uses to bind CRB1 (crumbs homolog 1). EPB41L5 is a homolog of zebrafish 'mosaic eyes' (moe), and is widely expressed but found at highest levels in ovary, kidney and brain, and is known to colocalize with _-catenin. EPB41L5 may participate in tight junction positioning during the establishment of epithelial cell polarity, and exists as four alternatively spliced isoforms that are encoded by a gene located on human chromosome 2q14.2.
VE:  1 * 100 µl
Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-12350R-FITC
Lokale Artikelnummer:: BOSSBS-12350R-FITC
Beschreibung:   The homeobox DNA-binding domain is a 60 amino acid motif that is conserved among many species and functions to bind DNA via a helix-turn-helix structure, thereby playing a role in transcriptional regulation and in the control of gene expression. MIXL1 (Mix1 homeobox-like 1), also known as MIXL, is a 232 amino acid protein that localizes to the nucleus and contains one homeobox DNA-binding domain. Expressed in lymph tissues, MIXL1 functions as a transcription factor that plays an essential role in axial mesendoderm morphogenesis and endoderm formation and is also required for cellular differentiation during blood development. Additionally, MIXL1 is involved in maturation of heart and gut tissue during embryogenesis and may also act as a negative regulator of brachyury expression. Overexpression of MIXL1 is associated with non-Hodgkin and Hodgkin lymphomas, suggesting a role in carcinogenesis.
VE:  1 * 100 µl
Artikel-Nr: (A3480.0025)

Lieferant:  PanReac AppliChem
Hersteller-Artikelnummer:: A3480.0025
Lokale Artikelnummer:: APLIA3480.0025
Beschreibung:   Coomassie Brillantblau G 250
VE:  1 * 25 g
Artikel-Nr: (BOSSBS-6792R-CY3)

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-6792R-CY3
Lokale Artikelnummer:: BOSSBS-6792R-CY3
Beschreibung:   The mammalian homologues of the key cell death gene CED 4 in C. elegans has been identified recently from human and mouse and designated Apaf1 (for apoptosis protease activating factor 1). Apaf1 binds to cytochrome c (Apaf2) and caspase 9 (Apaf3), which leads to caspase 9 activation. Activated caspase 9 in turn cleaves and activates caspase 3 that is one of the key proteases, being responsible for the proteolytic cleavage of many key proteins in apoptosis. A new Apaf1 Interacting Protein (APIP) also known as CG129 and MMRP19, has been identified as a negative regulator of ischemic injury. APIP competes with Caspase 9 binding site of Apaf1. APIP is predicted to code for a 204 amino acid. An isoform of APIP, APIP2 encodes a 242 amino acid protein, which is an alternative splicing variant differing in its N terminus from APIP. APIP transcript is ubiquitously expressed in most adult tissue with high expression in skeletal muscle, heart, and kidney.
VE:  1 * 100 µl

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-7961R-CY3
Lokale Artikelnummer:: BOSSBS-7961R-CY3
Beschreibung:   Ankyrin is a membrane protein that mediates the attachment of the erythrocyte membrane skeleton to the plasma membrane and interacts with CD44 and inositol triphosphate. It contains three functional domains: a conserved N-terminal ankyrin repeat domain (ARD(consisting of 22–24 tandem repeats of 33 amino acids), a spectrin binding domain and a variably sized C-terminal regulatory domain. The ankyrin repeat is a 33-residue motif in proteins consisting of two alpha helices separated by loops. It has been studied using multiple sequence alignment to determine which conserved amino acid residues are critical for folding and stability. Ankyrin-repeat proteins have been associated with a number of human diseases; most notably, the cell cycle inhibitor p16 is associated with cancer and the Notch protein is a key component of cell signaling pathways whose intracellular repeat domain is disrupted in mutations that give rise to the neurological disorder known as CADASIL.
VE:  1 * 100 µl
Artikel-Nr: (BOSSBS-13189R-CY7)

Lieferant:  Bioss
Hersteller-Artikelnummer:: BS-13189R-CY7
Lokale Artikelnummer:: BOSSBS-13189R-CY7
Beschreibung:   Amines, including those present on proteins, spontaneously react with glucose to make fructosamines in a reaction termed glycation. Fructosamine 3-kinase (FN3K), a 309-amino acid enzyme initially identified in erythrocytes, catalyzes the ATP-dependent phosphorylation of the third carbon on both D- and L-fructosamines, leading to their destabilization and eventually, their removal from the protein. FN3K is a monomer that is ubiquitously expressed in mammalian tissue and phosphorylates both low molecular mass and protein-bound fructosamines which are formed as a result of glycation of glucose with primary amines. FN3K protects proteins from the harmful effects of nonenzymatic glycation, and may also be involved in peptide repair and cell metabolism. FN3KRP (fructosamine-3-kinase-related protein) is a 309 amino acid protein that is expressed in erythrocytes, bone marrow, spleen, brain and kidney and belongs to the fructosamine kinase family. FN3KRP functions to phosphorylate psicoamines and ribulosamines on the third carbon of their sugar moiety, thereby leading to the deglycation of the target amines.
VE:  1 * 100 µl
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