You Searched For: 4-Carboxy-3-fluorophenylboronic+acid


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Catalog Number: (EDQMY0001168)
Supplier: EDQM
Description: Organic Standard, Potassium clavulanate impurity G, 4-[[(1S)-1-carboxy-2-(4-hydroxyphenyl)ethyl]amino]-4-oxobutanoic acid (N-(hydrogensuccinyl)tyrosine)
UOM: 1 * 5 mg


Catalog Number: (BOSSBS-7533R-FITC)
Supplier: Bioss
Description: Lipin 1 is a member of the Lipin family of nuclear proteins. This family contains three members: Lipin 1, Lipin 2 and Lipin 3, all of which contain a nuclear signal sequence, a highly conserved amino-terminal (NLIP) domain and a carboxy-terminal (CLIP) domain. LPIN1 (Lipin 1) is crucial for normal adipose tissue development and metabolism. LPIN1 selectively activates a subset of PGC1 alpha target pathways, including fatty acid oxidation and mitochondrial oxidative phosphorylation by inducing expression of the nuclear receptor PPARalpha. LPIN1 also inactivates the lipogenic program and suppresses circulating lipid levels. An abundance of LPIN1 promotes fat accumulation and insulin sensitivity, whereas a deficiency in LPIN1 may deter normal adipose tissue development, resulting in insulin resistance and lipodystrophy, a heterogeneous group of disorders characterized by loss of body fat, fatty liver, hypertriglyceridemia and insulin resistance.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13236R-CY5)
Supplier: Bioss
Description: Fyb (Fyn binding protein) and the anchoring proteins SKAP55 (src kinase-associated phosphoprotein) and SKAP55-R (SKAP55-related protein) associate with the tyrosine kinase p59fyn (1–3). SKAP55 and SKAP55-R bind to Fyb through their SH3 domains and function as substrates for p59Fyn in resting T cells (1–3). SKAP55 contains an amino-terminal pleckstrin homology domain and a carboxy-terminal SH3 domain binding motif of adjacent arginine and lysine residues followed by tandem tyrosines (i.e. RKxxYxxY) (4,5). SKAP55-R, similar in overall structure to SKAP55, contains a coiled-coil N-terminal domain (1,2). SKAP55 associates with SLAP-130, another component of the Fyn complex, which plays a role in the regulation of signaling events initiated by lymphocyte antigen receptors leading up to T cell activation (6). The human Fyb gene maps to chromosome 5p13.1 and encodes a 783 amino acid protein (7).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-2835R-A680)
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 leukaemia 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.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-5862R-CY5)
Supplier: Bioss
Description: ADAMTS (A Disintegrin And Metalloproteinase Domain with Thrombospondin type 1 Modules) is a family of zinc-dependent proteases that are implicated in a variety of normal and pathological conditions, including arthritis and cancer. ADAMTS protein family members contain an amino-terminal propeptide domain, a metalloproteinase domain, a disintegrin-like domain and a carboxy-terminus that contains a varying number of Thrombospondin type 1 (TSP-1) motifs. ADAMTS-L2 (ADAMTS-like protein 2) is a 951 amino acid secreted protein that is highly expressed in lung, kidney and liver. Mutations in the gene encoding ADAMTS are the cause of geleophysic dysplasia, an autosomal recessive disorder characterized by cardiac vavular anomalies, short stature, thick skin and brachydactyly. In individuals affected with geleophysic dysplasia, there is a significant increase in total active TGF-beta 1 and nuclear locations of p-SAMD2 in fibroblasts. Interestingly, ADAMTS-L2 interacts with LTBP-1, a glycoprotein that is part of the platelet-derived TGF-beta 1 complex.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-2835R-HRP)
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.
UOM: 1 * 100 µl


Catalog Number: (PRSI7195P)
Supplier: ProSci Inc.
Description: 15 amino acids near the carboxy terminus of human STAT1.
UOM: 1 * 50 µG


Catalog Number: (PRSI7283P)
Supplier: ProSci Inc.
Description: 17 amino acids near the carboxy terminus of human MTERFD2.
UOM: 1 * 50 µG


Catalog Number: (BOSSBS-5862R-A680)
Supplier: Bioss
Description: ADAMTS (A Disintegrin And Metalloproteinase Domain with Thrombospondin type 1 Modules) is a family of zinc-dependent proteases that are implicated in a variety of normal and pathological conditions, including arthritis and cancer. ADAMTS protein family members contain an amino-terminal propeptide domain, a metalloproteinase domain, a disintegrin-like domain and a carboxy-terminus that contains a varying number of Thrombospondin type 1 (TSP-1) motifs. ADAMTS-L2 (ADAMTS-like protein 2) is a 951 amino acid secreted protein that is highly expressed in lung, kidney and liver. Mutations in the gene encoding ADAMTS are the cause of geleophysic dysplasia, an autosomal recessive disorder characterised by cardiac vavular anomalies, short stature, thick skin and brachydactyly. In individuals affected with geleophysic dysplasia, there is a significant increase in total active TGF-beta 1 and nuclear locations of p-SAMD2 in fibroblasts. Interestingly, ADAMTS-L2 interacts with LTBP-1, a glycoprotein that is part of the platelet-derived TGF-beta 1 complex.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-5862R-A647)
Supplier: Bioss
Description: ADAMTS (A Disintegrin And Metalloproteinase Domain with Thrombospondin type 1 Modules) is a family of zinc-dependent proteases that are implicated in a variety of normal and pathological conditions, including arthritis and cancer. ADAMTS protein family members contain an amino-terminal propeptide domain, a metalloproteinase domain, a disintegrin-like domain and a carboxy-terminus that contains a varying number of Thrombospondin type 1 (TSP-1) motifs. ADAMTS-L2 (ADAMTS-like protein 2) is a 951 amino acid secreted protein that is highly expressed in lung, kidney and liver. Mutations in the gene encoding ADAMTS are the cause of geleophysic dysplasia, an autosomal recessive disorder characterized by cardiac vavular anomalies, short stature, thick skin and brachydactyly. In individuals affected with geleophysic dysplasia, there is a significant increase in total active TGF-beta 1 and nuclear locations of p-SAMD2 in fibroblasts. Interestingly, ADAMTS-L2 interacts with LTBP-1, a glycoprotein that is part of the platelet-derived TGF-beta 1 complex.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13741R-A488)
Supplier: Bioss
Description: Vinexin is a 671 amino acid protein that is expressed as two isoforms, designated Vinexin alpha and Vinexin beta. Localized to cell junctions in both the cytoplasm and the cytoskeleton, Vinexin alpha functions to promote Actin stress fiber formation, playing an important role in modification of the Actin cytoskeleton. Like Vinexin alpha, Vinexin beta is localized to cell junctions in the cytoplasm, but is also found in the nucleus where it plays an important role in cell spreading and in activation of the JNK pathway in response to EGF stimulation. Although Vinexin alpha and Vinexin beta have different roles within the cell, both proteins contain three SH3 domains in their carboxy terminus and are expressed in a variety of tissues, including placenta, heart, liver, brain, pancreas and skeletal muscle. Together, Vinexin alpha and Vinexin beta are involved in cell-cell adhesion, signal transduction and cytoskeletal organization throughout the cell.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13741R-A647)
Supplier: Bioss
Description: Vinexin is a 671 amino acid protein that is expressed as two isoforms, designated Vinexin alpha and Vinexin beta. Localized to cell junctions in both the cytoplasm and the cytoskeleton, Vinexin alpha functions to promote Actin stress fiber formation, playing an important role in modification of the Actin cytoskeleton. Like Vinexin alpha, Vinexin beta is localized to cell junctions in the cytoplasm, but is also found in the nucleus where it plays an important role in cell spreading and in activation of the JNK pathway in response to EGF stimulation. Although Vinexin alpha and Vinexin beta have different roles within the cell, both proteins contain three SH3 domains in their carboxy terminus and are expressed in a variety of tissues, including placenta, heart, liver, brain, pancreas and skeletal muscle. Together, Vinexin alpha and Vinexin beta are involved in cell-cell adhesion, signal transduction and cytoskeletal organization throughout the cell.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13236R-A750)
Supplier: Bioss
Description: Fyb (Fyn binding protein) and the anchoring proteins SKAP55 (src kinase-associated phosphoprotein) and SKAP55-R (SKAP55-related protein) associate with the tyrosine kinase p59fyn (13). SKAP55 and SKAP55-R bind to Fyb through their SH3 domains and function as substrates for p59Fyn in resting T cells (13). SKAP55 contains an amino-terminal pleckstrin homology domain and a carboxy-terminal SH3 domain binding motif of adjacent arginine and lysine residues followed by tandem tyrosines (i.e. RKxxYxxY) (4,5). SKAP55-R, similar in overall structure to SKAP55, contains a coiled-coil N-terminal domain (1,2). SKAP55 associates with SLAP-130, another component of the Fyn complex, which plays a role in the regulation of signaling events initiated by lymphocyte antigen receptors leading up to T cell activation (6). The human Fyb gene maps to chromosome 5p13.1 and encodes a 783 amino acid protein (7).
UOM: 1 * 100 µl


Catalog Number: (MOLEM37939444)
Supplier: Molekula
Description: Thiazolidine-2-carboxylic acid
UOM: 1 * 5 g

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Catalog Number: (BOSSBS-13236R-HRP)
Supplier: Bioss
Description: Fyb (Fyn binding protein) and the anchoring proteins SKAP55 (src kinase-associated phosphoprotein) and SKAP55-R (SKAP55-related protein) associate with the tyrosine kinase p59fyn (1–3). SKAP55 and SKAP55-R bind to Fyb through their SH3 domains and function as substrates for p59Fyn in resting T cells (1–3). SKAP55 contains an amino-terminal pleckstrin homology domain and a carboxy-terminal SH3 domain binding motif of adjacent arginine and lysine residues followed by tandem tyrosines (i.e. RKxxYxxY) (4,5). SKAP55-R, similar in overall structure to SKAP55, contains a coiled-coil N-terminal domain (1,2). SKAP55 associates with SLAP-130, another component of the Fyn complex, which plays a role in the regulation of signaling events initiated by lymphocyte antigen receptors leading up to T cell activation (6). The human Fyb gene maps to chromosome 5p13.1 and encodes a 783 amino acid protein (7).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9907R-A750)
Supplier: Bioss
Description: CPN2 is a zinc metalloprotease, and cleaves carboxy-terminal arginines and lysines from peptides found in the bloodstream such as complement anaphylatoxins, kinins, and creatine kinase MM (CK-MM). By removing only one amino acid, CPN has the ability to change peptide activity and receptor binding. It is a 280 kDa tetrameric glycoprotein that is synthesised by the liver and secreted into the plasma. It consists of 2 identical 83 kDa regulatory subunits (CPN2) and 2 identical 50 kDa catalytic subunits (CPN1). CPN2, the 83 kDa subunit, binds and stabilizes the catalytic subunit at 37 degrees Celsius and keeps it in circulation. Under some circumstances it may be an allosteric modifier of the catalytic subunit. CPN is a member of a larger family of carboxypeptidases, many of which also cleave arginine and lysine. Because of the highly conserved active sites and the possible redundant functions of carboxypeptidases, it has been difficult to elucidate the role of CPN in disease processes.
UOM: 1 * 100 µl


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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222.
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