You Searched For: L-Lysine

Catalog Number: (BIRBORB76580-0.1)

Supplier: Biorbyt

Description: Anti-Lysine Mouse Monoclonal Antibody

UOM: 1 * 0,1 mL

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Catalog Number: (BOSSBS-9384R-A680)

Supplier: Bioss

Description: CNOT2 (CCR4-NOT transcription complex subunit 2) is a ubiquitous protein encoded by the human gene CNOT2. CNOT2 belongs to the CNOT2/3/5 family and is part of the CCR4-NOT complex. The CCR4-NOT complex is an evolutionarily conserved, multi-component complex known to be involved in transcription as well as mRNA degradation. Various subunits (e.g. CNOT1, CNOT2) are involved in influencing nuclear hormone receptor activities. The CCR4-NOT complex is also involved in the regulation of Histone H3 lysine 4 methylation through a ubiquitin-dependent pathway that likely involves the proteasome. Increased expression of the CNOT2 subunit acts to strongly repress transcription by RNA polymerase II. This repressive effect is mediated by a conserved NOT-Box, which is located at the C-terminus of CNOT2 proteins. Repression by the NOT-Box is sensitive to treatment with the histone deacetylase (HDAC) inhibitor trichostatin A.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-5387R-CY7)

Supplier: Bioss

Description: Reversible acetylation of highly conserved lysine residues within the N-terminal tail domains of core histones, plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone acetylation is a dynamic process determined by the net activities of histone acetyltransferases (HATs) and the competing enzymes histone deacetylases (HDACs). Histone deacetylases activities are often, but not always, associated with transcriptional repression and nucleosomal condensations. Recruitment of the multiprotein complexes to promoter sites occurs by many sequence specific DNA-binding proteins such as unliganded nuclear hormone receptors, DP1-E2F, YY1 and Rb family of transcription factors, transcriptional repressors and tumor suppressors (e.g. BRCA1). Aberrant recruitment of HDACs by certain oncoproteins may occur in certain neoplastic diseases. Belongs to the histone deacetylase family.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13236R-CY7)

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-13236R-CY3)

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-2811R-A555)

Supplier: Bioss

Description: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Plays a central role in microtubule-dependent cell motility via deacetylation of tubulin. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and target them to the aggresome, facilitating their clearance by autophagy.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13236R-A680)

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: (BOSSBS-2811R-CY7)

Supplier: Bioss

Description: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Plays a central role in microtubule-dependent cell motility via deacetylation of tubulin. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that recognizes polyubiquitinated misfolded proteins and target them to the aggresome, facilitating their clearance by autophagy.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-0964R-CY7)

Supplier: Bioss

Description: Tripartite motif-containing protein 32 (TRIM32) belongs to the tripartite motif (TRIM) protein family. TRIM32, like all TRIM proteins, contains a domain structure composed of a B-box, a RING-finger and a coiled-coil motif. Additionally, TRIM32 has six C-terminal NHL domains; it is expressed mainly in the skeletal muscle. The TRIM32 gene encodes an E3 ubiquitin ligase, a protein that attaches ubiquitin to a lysine residue on a target protein and acts in conjunction with ubiquitin-conjugating enzymes UbcH5a, UbcH5c and UbcH6. Mutations in the TRIM32 gene cause two forms of autosomal recessive muscular dystrophy designated limb girdle muscular dystrophy type 2H (LGMD2H) and sarcotubular myopathy (STM). TRIM32 mutations can also result in Bardet-Biedl syndrome (BBS), an autosomal recessive disorder characterized by pigmentary retinopathy, polydactyly, hypogenitalism, renal abnormalities, learning disabilities and obesity.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-0964R)

Supplier: Bioss

Description: Tripartite motif-containing protein 32 (TRIM32) belongs to the tripartite motif (TRIM) protein family. TRIM32, like all TRIM proteins, contains a domain structure composed of a B-box, a RING-finger and a coiled-coil motif. Additionally, TRIM32 has six C-terminal NHL domains; it is expressed mainly in the skeletal muscle. The TRIM32 gene encodes an E3 ubiquitin ligase, a protein that attaches ubiquitin to a lysine residue on a target protein and acts in conjunction with ubiquitin-conjugating enzymes UbcH5a, UbcH5c and UbcH6. Mutations in the TRIM32 gene cause two forms of autosomal recessive muscular dystrophy designated limb girdle muscular dystrophy type 2H (LGMD2H) and sarcotubular myopathy (STM). TRIM32 mutations can also result in Bardet-Biedl syndrome (BBS), an autosomal recessive disorder characterized by pigmentary retinopathy, polydactyly, hypogenitalism, renal abnormalities, learning disabilities and obesity.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-2811R-A750)

Supplier: Bioss

Description: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Plays a central role in microtubule-dependent cell motility via deacetylation of tubulin. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that Recognises polyubiquitinated misfolded proteins and target them to the aggresome, facilitating their clearance by autophagy.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-2811R-A680)

Supplier: Bioss

Description: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes (By similarity). Plays a central role in microtubule-dependent cell motility via deacetylation of tubulin. Involved in the MTA1-mediated epigenetic regulation of ESR1 expression in breast cancer. In addition to its protein deacetylase activity, plays a key role in the degradation of misfolded proteins: when misfolded proteins are too abundant to be degraded by the chaperone refolding system and the ubiquitin-proteasome, mediates the transport of misfolded proteins to a cytoplasmic juxtanuclear structure called aggresome. Probably acts as an adapter that Recognises polyubiquitinated misfolded proteins and target them to the aggresome, facilitating their clearance by autophagy.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-5387R-A488)

Supplier: Bioss

Description: Reversible acetylation of highly conserved lysine residues within the N-terminal tail domains of core histones, plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone acetylation is a dynamic process determined by the net activities of histone acetyltransferases (HATs) and the competing enzymes histone deacetylases (HDACs). Histone deacetylases activities are often, but not always, associated with transcriptional repression and nucleosomal condensations. Recruitment of the multiprotein complexes to promoter sites occurs by many sequence specific DNA-binding proteins such as unliganded nuclear hormone receptors, DP1-E2F, YY1 and Rb family of transcription factors, transcriptional repressors and tumor suppressors (e.g. BRCA1). Aberrant recruitment of HDACs by certain oncoproteins may occur in certain neoplastic diseases. Belongs to the histone deacetylase family.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-5387R-HRP)

Supplier: Bioss

Description: Reversible acetylation of highly conserved lysine residues within the N-terminal tail domains of core histones, plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone acetylation is a dynamic process determined by the net activities of histone acetyltransferases (HATs) and the competing enzymes histone deacetylases (HDACs). Histone deacetylases activities are often, but not always, associated with transcriptional repression and nucleosomal condensations. Recruitment of the multiprotein complexes to promoter sites occurs by many sequence specific DNA-binding proteins such as unliganded nuclear hormone receptors, DP1-E2F, YY1 and Rb family of transcription factors, transcriptional repressors and tumor suppressors (e.g. BRCA1). Aberrant recruitment of HDACs by certain oncoproteins may occur in certain neoplastic diseases. Belongs to the histone deacetylase family.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13236R-A350)

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

Supplier: Biotium

Description: Recognizes a 77-85 kDa protein, identified as cellular or tissue transglutaminase II (TGase II). Transglutaminases are enzymes that catalyze the crosslinking of proteins by epsilon-gamma glutamyl lysine isopeptide bonds. While the primary structure of transglutaminases is not conserved, they all have the same amino acid sequence at their active sites and their activity is calcium-dependent. The protein encoded by this gene acts as a monomer, is induced by retinoic acid, and appears to be involved in apoptosis. Finally, the encoded protein is the autoantigen implicated in celiac disease. The identification of transglutaminase as the main antigen of endomysium antibodies allows a new diagnostic approach to celiac disease (CD), a genetic, immunologically mediated small bowel enteropathy that causes malabsorption. TGase II is implicated in programmed cell death, signal transduction, drug-resistance, cell growth, endocytosis, insulin secretion, cell adhesion, cataract formation, and wound healing.