You Searched For: D-Lysine

Catalog Number: (BOSSBS-10024R-A350)

Supplier: Bioss

Description: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4), and some other non-histone substrates. 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. Participates in the BCL6 transcriptional repressor activity by deacetylating the H3 'Lys-27' (H3K27) on enhancer elements, antagonizing EP300 acetyltransferase activity and repressing proximal gene expression. Probably participates in the regulation of transcription through its binding to the zinc-finger transcription factor YY1; increases YY1 repression activity. Required to repress transcription of the POU1F1 transcription factor. Acts as a molecular chaperone for shuttling phosphorylated NR2C1 to PML bodies for sumoylation.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-13673R-A488)

Supplier: Bioss

Description: Fyb (Fyn binding protein) and the anchoring proteins SKAP55 and SKAP55-R (SKAP55-related protein) associate with the tyrosine kinase p59fyn. SKAP55 and SKAP55-R bind to Fyb through their SH3 domains and function as substrates for p59Fyn in resting T cells. SKAP55 contains an N-terminal pleckstrin homology domain and a C-terminal SH3 domain binding motif of adjacent arginine and lysine residues followed by tandem tyrosines (i.e. RKxxYxxY). SKAP55-R, similar in overall structure to SKAP55, contains a coiled-coil N-terminal domain. 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. The human SKAP55 gene maps to chromosome 17q21.32 and encodes a 359 amino acid protein.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-10024R-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), and some other non-histone substrates. 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. Participates in the BCL6 transcriptional repressor activity by deacetylating the H3 'Lys-27' (H3K27) on enhancer elements, antagonizing EP300 acetyltransferase activity and repressing proximal gene expression. Probably participates in the regulation of transcription through its binding to the zinc-finger transcription factor YY1; increases YY1 repression activity. Required to repress transcription of the POU1F1 transcription factor. Acts as a molecular chaperone for shuttling phosphorylated NR2C1 to PML bodies for sumoylation.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-5387R-A680)

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

Supplier: MP Biomedicals

Description: Poly-L-Lysine is typically used as a coating substrate for culture dishes, slides, etc.

Catalog Number: (BOSSBS-3824R-CY5)

Supplier: Bioss

Description: JMJD1B (jumonji domain containing 1B), also known as KDM3B, 5qNCA (5q Nuclear Co-Activator) or C5orf7, is a member of the JHDM2 histone demethylase family of proteins. Expressed in a wide variety of tissues, JMJD1B localizes to the nucleus and contains one JMJC domain and a C-terminal zinc finger motif. JMJD1B functions as a histone demethylase and, using iron as a cofactor, demethylates lysine-9 of Histone H3. This suggests that JMJD1B plays a central role in the histone code. The gene encoding human JMJD1B is located within the 5q region of the genome that is often deleted in myeloid leukemias and myelodysplasias. This implies that JMJD1B may function as a tumor suppressor of myeloid leukemia. Eptopic expression of JMJD1B exhibits growth suppressive activities, further supporting a role for JMJD1B in tumor suppression.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-3824R-CY7)

Supplier: Bioss

Description: JMJD1B (jumonji domain containing 1B), also known as KDM3B, 5qNCA (5q Nuclear Co-Activator) or C5orf7, is a member of the JHDM2 histone demethylase family of proteins. Expressed in a wide variety of tissues, JMJD1B localizes to the nucleus and contains one JMJC domain and a C-terminal zinc finger motif. JMJD1B functions as a histone demethylase and, using iron as a cofactor, demethylates lysine-9 of Histone H3. This suggests that JMJD1B plays a central role in the histone code. The gene encoding human JMJD1B is located within the 5q region of the genome that is often deleted in myeloid leukemias and myelodysplasias. This implies that JMJD1B may function as a tumor suppressor of myeloid leukemia. Eptopic expression of JMJD1B exhibits growth suppressive activities, further supporting a role for JMJD1B in tumor suppression.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-2811R)

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-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-2811R-A488)

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

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.

Catalog Number: (BOSSBS-0964R-A350)

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-A680)

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 characterised by pigmentary retinopathy, polydactyly, hypogenitalism, renal abnormalities, learning disabilities and obesity.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-3216R-A488)

Supplier: Bioss

Description: HDAC7 is a member of the class II mammalian histone deacetylases, which plays an important role in modulating the eukaryotic chromatin structure. Human HDAC7 is composed of 912 amino acid residues. Although HDAC7 is localized mostly to the cell nucleus, it is also found in the cytoplasm, suggesting nucleo-cytoplasmic shuttling. The histone deacetylase activity of HDAC7 maps to a carboxy-terminal domain and is dependent on interaction with class I HDACs in the nucleus. It is an active component of different transcriptional corepressor complexes that can be recruited to specific promoter regions via interactions with a growing number of sequence specific transcriptional factors. HDAC7 catalyzes removal of acetyl-groups from acetyl-lysines of histones and promotes compaction of chromatin in these regions, leading to the inhibition of gene transcription.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-3216R-A680)

Supplier: Bioss

Description: HDAC7 is a member of the class II mammalian histone deacetylases, which plays an important role in modulating the eukaryotic chromatin structure. Human HDAC7 is composed of 912 amino acid residues. Although HDAC7 is localised mostly to the cell nucleus, it is also found in the cytoplasm, suggesting nucleo-cytoplasmic shuttling. The histone deacetylase activity of HDAC7 maps to a carboxy-terminal domain and is dependent on interaction with class I HDACs in the nucleus. It is an active component of different transcriptional corepressor complexes that can be recruited to specific promoter regions via interactions with a growing number of sequence specific transcriptional factors. HDAC7 catalyses removal of acetyl-groups from acetyl-lysines of histones and promotes compaction of chromatin in these regions, leading to the inhibition of gene transcription.

UOM: 1 * 100 µl

Catalog Number: (BOSSBS-3824R-A680)

Supplier: Bioss

Description: JMJD1B (jumonji domain containing 1B), also known as KDM3B, 5qNCA (5q Nuclear Co-Activator) or C5orf7, is a member of the JHDM2 histone demethylase family of proteins. Expressed in a wide variety of tissues, JMJD1B localises to the nucleus and contains one JMJC domain and a C-terminal zinc finger motif. JMJD1B functions as a histone demethylase and, using iron as a cofactor, demethylates lysine-9 of Histone H3. This suggests that JMJD1B plays a central role in the histone code. The gene encoding human JMJD1B is located within the 5q region of the genome that is often deleted in myeloid leukaemias and myelodysplasias. This implies that JMJD1B may function as a tumor suppressor of myeloid leukaemia. Eptopic expression of JMJD1B exhibits growth suppressive activities, further supporting a role for JMJD1B in tumor suppression.

UOM: 1 * 100 µl