Du Søgte efter: L-Lysin

Varenummer: (BOSSBS-2737R)

Leverandør: Bioss

Beskrivelse: TREML2 is expressed throughout B cell development in addition to being expressed on macrophages and neutrophils and is the only TREM molecule to be found on lymphocytes. TREML2 is expressed on B lineage cells early in development, and the highest level of expression is detected on those mature peripheral B cell subpopulations that are involved in the initial humoral immune response against bacterial pathogens. TREML2 is unique in that it lacks either the conserved transmembrane lysine residue or ITAM/ITIMs within its own cytoplasmic domain. Thus, TREML2 does not exhibit any of the features associated with classical tyrosine-based signaling. Monocytes in the bone marrow or peripheral blood do not express detectable levels of TREML2, but its expression is up-regulated in conjunction with differentiation into macrophages. TREML2 is present on neutrophils in the bone marrow as well as the periphery, and inflammatory stimuli result in a dramatic increase in the expression of TREML2 on these cells in vivo.TREML2 is a single-pass type I membrane protein, and it contains 1 Ig-like V-type (immunoglobulin-like) domain. It is a cell surface receptor that may play a role in the innate and adaptive immune response. TREML2 is located in a gene cluster on chromosome 6 with the single Ig variable (IgV) domain activating receptors TREM1 and TREM2, but it has distinct structural and functional properties.

UOM: 1 * 100 µl

Tilbud

Varenummer: (PRSI91-155)

Leverandør: ProSci Inc.

Beskrivelse: Small Ubiquitin-Related Modifier 1 (SUMO1) is an Ubiquitin-like protein that belongs to the ubiquitin family with SUMO subfamily. It is a family of small, related proteins that can be enzymatically attached to a target protein by a post-translational modification process termed sumoylation. SUMO1 functions in a manner similar to ubiquitin in that it is bound to target proteins as part of a post-translational modification system. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. SUMO1 is involved in a variety of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability. SUMO1 is not active until the last four amino acids of the carboxy-terminus are cleaved off. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins and may also regulate a network of genes involved in palate development.

UOM: 1 * 1 Each

Tilbud

Varenummer: (PRSI56-558)

Leverandør: ProSci Inc.

Beskrivelse: SUMO4 is a member of the SUMO gene family. This family of small ubiquitin-related modifiers covalently modify target lysines in proteins and control the target proteins' subcellular localization, stability, or activity. Upon oxidative stress, SUMO4 conjugates to various anti-oxidant enzymes, chaperones, and stress defense proteins. This protein may also conjugate to NFKBIA, TFAP2A and FOS, negatively regulating their transcriptional activity, and to NR3C1, positively regulating its transcriptional activity. Covalent attachment to SUMO4 substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I. In contrast to SUMO1, SUMO2 and SUMO3, SUMO4 seems to be insensitive to sentrin-specific proteases due to the presence of Pro-90. This may impair processing to mature form and conjugation to substrates. SUMO4 is located in the cytoplasm and specifically modifies IKBA, leading to negative regulation of NF-kappa-B-dependent transcription of the IL12B gene. The M55V substitution has been associated with type I diabetes.

UOM: 1 * 400 µl

Tilbud

Varenummer: (PRSI56-567)

Leverandør: ProSci Inc.

Beskrivelse: SUMO4 is a member of the SUMO gene family. This family of small ubiquitin-related modifiers covalently modify target lysines in proteins and control the target proteins' subcellular localization, stability, or activity. Upon oxidative stress, SUMO4 conjugates to various anti-oxidant enzymes, chaperones, and stress defense proteins. This protein may also conjugate to NFKBIA, TFAP2A and FOS, negatively regulating their transcriptional activity, and to NR3C1, positively regulating its transcriptional activity. Covalent attachment to SUMO4 substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I. In contrast to SUMO1, SUMO2 and SUMO3, SUMO4 seems to be insensitive to sentrin-specific proteases due to the presence of Pro-90. This may impair processing to mature form and conjugation to substrates. SUMO4 is located in the cytoplasm and specifically modifies IKBA, leading to negative regulation of NF-kappa-B-dependent transcription of the IL12B gene. The M55V substitution has been associated with type I diabetes.

UOM: 1 * 400 µl

Tilbud

Varenummer: (PRSI56-566)

Leverandør: ProSci Inc.

Beskrivelse: SUMO4 is a member of the SUMO gene family. This family of small ubiquitin-related modifiers covalently modify target lysines in proteins and control the target proteins' subcellular localization, stability, or activity. Upon oxidative stress, SUMO4 conjugates to various anti-oxidant enzymes, chaperones, and stress defense proteins. This protein may also conjugate to NFKBIA, TFAP2A and FOS, negatively regulating their transcriptional activity, and to NR3C1, positively regulating its transcriptional activity. Covalent attachment to SUMO4 substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I. In contrast to SUMO1, SUMO2 and SUMO3, SUMO4 seems to be insensitive to sentrin-specific proteases due to the presence of Pro-90. This may impair processing to mature form and conjugation to substrates. SUMO4 is located in the cytoplasm and specifically modifies IKBA, leading to negative regulation of NF-kappa-B-dependent transcription of the IL12B gene. The M55V substitution has been associated with type I diabetes.

UOM: 1 * 400 µl

Tilbud

Varenummer: (PRSI5215)

Leverandør: ProSci Inc.

Beskrivelse: SHOC2 Antibody: SHOC2 protein participates in protein binding / transferase activity in the fibroblast growth factor receptor signaling pathway and Ras protein signal transduction. It is a widely expressed protein composed almost entirely of leucine-rich repeats (LRR), with a lysine-rich sequence at the amino terminus and cytoplasmically localized. SHOC2 acts as a positive modulator of the RAS-MAPK signaling cascade, which is elicited by EGL-15 and LET-23 and mediated by LET-60. SHOC2 together with protein phosphatase 1c (PP1c) forms a highly specific M-Ras effector complex and is essential for activation of the MAPK pathway by growth factors. Furthermore, in tumor cells with Ras gene mutations, inhibition of SHOC2 expression inhibits MAPK, but not PI3K activity. The SHOC2-PP1c holoenzyme provides an attractive therapeutic target for inhibition of the MAPK pathway in cancer. Recent studies show that aberrantly acquired N-myristoylation of SHOC2 causes human disease Noonan-like syndrome with loose anagen hair.

UOM: 1 * 1 Each

Tilbud

Varenummer: (PRSI49-282)

Leverandør: ProSci Inc.

Beskrivelse: Histone deacetylase (HDAC) and histone acetyltransferase (HAT) are enzymes that regulate transcription by selectively deacetylating or acetylating the eta-amino groups of lysines located near the amino termini of core histone proteins. Eight members of HDAC family have been identified in the past several years. These HDAC family members are divided into two classes, I and II. Class I of the HDAC family comprises four members, HDAC-1, 2, 3, and 8, each of which contains a deacetylase domain exhibiting from 45 to 93% identity in amino acid sequence. Class II of the HDAC family comprises HDAC-4, 5, 6, and 7, the molecular weights of which are all about twofold larger than those of the class I members, and the deacetylase domains are present within the C-terminal regions, except that HDAC-6 contains two copies of the domain, one within each of the N-terminal and C-terminal regions. Human HDAC-1, 2 and 3 were expressed in various tissues, but the others (HDAC-4, 5, 6, and 7) showed tissue-specific expression patterns. These results suggested that each member of the HDAC family exhibits a different, individual substrate specificity and function in vivo.

UOM: 1 * 1 Each

Tilbud

Varenummer: (PRSI55-610)

Leverandør: ProSci Inc.

Beskrivelse: Histone deacetylase (HDAC) and histone acetyltransferase (HAT) are enzymes that regulate transcription by selectively deacetylating or acetylating the eta-amino groups of lysines located near the amino termini of core histone proteins (1). Eight members of HDAC family have been identified in the past several years (2,3). These HDAC family members are divided into two classes, I and II. Class I of the HDAC family comprises four members, HDAC-1, 2, 3, and 8, each of which contains a deacetylase domain exhibiting from 45 to 93% identity in amino acid sequence. Class II of the HDAC family comprises HDAC-4, 5, 6, and 7, the molecular weights of which are all about two-fold larger than those of the class I members, and the deacetylase domains are present within the C-terminal regions, except that HDAC-6 contains two copies of the domain, one within each of the N-terminal and C-terminal regions. Human HDAC-1, 2 and 3 were expressed in various tissues, but the others (HDAC-4, 5, 6, and 7) showed tissue-specific expression patterns (3). These results suggested that each member of the HDAC family exhibits a different, individual substrate specificity and function in vivo.

UOM: 1 * 400 µl

Tilbud

Varenummer: (ICNA0219469680)

Leverandør: MP Biomedicals

Beskrivelse: L-LYSINE 1 * 100 g

UOM: 1 * 100 g

Tilbud

Varenummer: (PIERA35393)

Leverandør: Thermo Fisher Scientific

Beskrivelse: Thermo Scientific Pierce DSP (Lomant's Reagent) is a water-insoluble, homo-bifunctional N-hydroxysuccimide ester (NHS ester) crosslinker that is thiol-cleavable, primary amine-reactive, and useful for many applications. DSP contains an amine-reactive NHS ester at each end of an 8-carbon spacer arm. NHS esters react with primary amines at pH 7–9 to form stable amide bonds and releasing N-hydroxy-succinimide. Proteins, including antibodies, generally have several primary amines in the side chain of lysine (K) residues and the N-terminus of each polypeptide that are available as targets for NHS ester crosslinking reagents. DSP is non-sulfonated and insoluble in water, so it must first be dissolved in an organic solvent and then added to the aqueous reaction mixture. Because DSP does not possess a charged group, it is lipophilic and membrane-permeable and so useful for intracellular and intramembrane conjugation. A sulfonated analog of DSP (DTTSP) is water soluble. DSS, the non-cleavable analog of the DSP crosslinker is also available for applications that require a stable spacer arm that cannot be cleaved in the presence of reducing agents.

UOM: 1 * 10 mg

Tilbud

Leverandør: Thermo Fisher Scientific

Beskrivelse: Thermo Scientific Pierce DSP (Lomant's Reagent) is a water-insoluble, homo-bifunctional N-hydroxysuccimide ester (NHS ester) crosslinker that is thiol-cleavable, primary amine-reactive, and useful for many applications. DSP contains an amine-reactive NHS ester at each end of an 8-carbon spacer arm. NHS esters react with primary amines at pH 7–9 to form stable amide bonds and releasing N-hydroxy-succinimide. Proteins, including antibodies, generally have several primary amines in the side chain of lysine (K) residues and the N-terminus of each polypeptide that are available as targets for NHS ester crosslinking reagents. DSP is non-sulfonated and insoluble in water, so it must first be dissolved in an organic solvent and then added to the aqueous reaction mixture. Because DSP does not possess a charged group, it is lipophilic and membrane-permeable and so useful for intracellular and intramembrane conjugation. A sulfonated analog of DSP (DTTSP) is water soluble. DSS, the non-cleavable analog of the DSP crosslinker is also available for applications that require a stable spacer arm that cannot be cleaved in the presence of reducing agents.

MSDS

Varenummer: (PRSI56-109)

Leverandør: ProSci Inc.

Beskrivelse: Similar to acetylation and phosphorylation, histone methylation at the N-terminal tail has emerged as an important role in regulating chromatin dynamics and gene activity. Histone methylation occurs on arginine and lysine residues and is catalyzed by two families of proteins, the protein arginine methyltransferase family and the SET-domain-containing methyltransferase family. Five members have been identified in the arginine methyltransferase family. About 27 are grouped into the SET-domain family, and another 17 make up the PR domain family that is related to the SET domain family. The retinoblastoma protein-interacting zinc finger geneRIZ1 is a tumor suppressor gene and a FOUNDING member of the PR domain family. RIZ1 inactivation is commonly found in many types of human cancers and occurs through loss of mRNA expression, frame shift mutation, chromosomal deletion, and missense mutation. RIZ1 is also a tumor susceptibility gene in mice. The loss of RIZ1 mRNA in human cancers was shown to associate with DNA methylation of its promoter CpG island. Methylation of the RIZ1 promoter strongly correlated with lost or decreased RIZ1 mRNA expression in breast, liver, colon, and lung cancer cell lines as well as in liver cancer tissues.

UOM: 1 * 400 µl

Tilbud

Varenummer: (PRSI32-194)

Leverandør: ProSci Inc.

Beskrivelse: Myeloid/lymphoid or mixed-lineage leukemia (trithorax homolog, Drosophila).Eukaryotic RNA polymerase II mediates the synthesis of mature and functional messenger RNA. This is a multistep process, called the transcription cycle,that includes five stages: preinitiation, promoter, clearance, elongation and termination. Elongation is thought to be a critical stage for the regulation of gene expression. ELL (11-19 lysine-rich leukemia protein, also designated MEN)
functions as an RNA polymerase II elongation factor that increases the rateof transcription by suppressing transient pausing by RNA polymerase II. Also, ELL is thought to regulate cellular proliferation. ELL is abundantly expressed in peripheral blood leukocytes, skeletal muscle, placenta and testis, and has lower expression in spleen, thymus, heart, brain, lung, kidney, liver and ovary.The gene encoding human ELL, which maps to chromosome 19p13.1, is one of several genes which undergo translocation with the MLL gene on chromo-some 11q23 in acute myeloid leukemia. MLL (myeloid/lymphoid leukemia,also designated ALL-1 and HRX) is a 430 kDa protein that regulates embryonal and hematopoietic development.

UOM: 1 * 100 µl

Tilbud

Varenummer: (PRSI56-133)

Leverandør: ProSci Inc.

Beskrivelse: Similar to acetylation and phosphorylation, histone methylation at the N-terminal tail has emerged as an important role in regulating chromatin dynamics and gene activity. Histone methylation occurs on arginine and lysine residues and is catalyzed by two families of proteins, the protein arginine methyltransferase family and the SET-domain-containing methyltransferase family. Five members have been identified in the arginine methyltransferase family. About 27 are grouped into the SET-domain family, and another 17 make up the PR domain family that is related to the SET domain family. The retinoblastoma protein-interacting zinc finger geneRIZ1 is a tumor suppressor gene and a FOUNDING member of the PR domain family. RIZ1 inactivation is commonly found in many types of human cancers and occurs through loss of mRNA expression, frame shift mutation, chromosomal deletion, and missense mutation. RIZ1 is also a tumor susceptibility gene in mice. The loss of RIZ1 mRNA in human cancers was shown to associate with DNA methylation of its promoter CpG island. Methylation of the RIZ1 promoter strongly correlated with lost or decreased RIZ1 mRNA expression in breast, liver, colon, and lung cancer cell lines as well as in liver cancer tissues.

UOM: 1 * 400 µl

Tilbud

Varenummer: (BOSSBS-1306R-A680)

Leverandør: Bioss

Beskrivelse: Protein deglycase that repairs methylglyoxal- and glyoxal-glycated amino acids and proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteines, arginines and lysines residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) (PubMed:25416785). Plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor and redox-sensitive chaperone and protease; functions probably related to its primary function (PubMed:17015834, PubMed:20304780, PubMed:18711745, PubMed:12796482, PubMed:19229105, PubMed:25416785). It is involved in neuroprotective mechanisms like the stabilisation of NFE2L2 and PINK1 proteins, male fertility as a positive regulator of androgen signaling pathway as well as cell growth and transformation through, for instance, the modulation of NF-kappa-B signaling pathway (PubMed:12612053, PubMed:15502874, PubMed:14749723, PubMed:17015834, PubMed:21097510, PubMed:18711745). Its involvement in protein repair could also explain other unrelated functions. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death (PubMed:16390825). Required for correct mitochondrial morphology and function as well as for autophagy of dysfunctional mitochondria (PubMed:19229105, PubMed:16632486). Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking (PubMed:18711745). Regulates astrocyte inflammatory responses, may modulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells (PubMed:23847046).

UOM: 1 * 100 µl

Tilbud

Varenummer: (BOSSBS-3097R-A555)

Leverandør: Bioss

Beskrivelse: Protein kinase involved in the regulation of transcription. Member of the cyclin-dependent kinase pair (CDK9/cyclin-T) complex, also called positive transcription elongation factor b (P-TEFb), which facilitates the transition from abortive to productive elongation by phosphorylating the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAP II) POLR2A, SUPT5H and RDBP. This complex is inactive when in the 7SK snRNP complex form. Phosphorylates EP300, MYOD1, RPB1/POLR2A and AR, and the negative elongation factors DSIF and NELF. Regulates cytokine inducible transcription networks by facilitating promoter recognition of target transcription factors (e.g. TNF-inducible RELA/p65 activation and IL-6-inducible STAT3 signaling). Promotes RNA synthesis in genetic programs for cell growth, differentiation and viral pathogenesis. P-TEFb is also involved in cotranscriptional histone modification, mRNA processing and mRNA export. Modulates a complex network of chromatin modifications including histone H2B monoubiquitination (H2Bub1), H3 lysine 4 trimethylation (H3K4me3) and H3K36me3; integrates phosphorylation during transcription with chromatin modifications to control co-transcriptional histone mRNA processing. The CDK9/cyclin-K complex has also a kinase activity towards CTD of RNAP II and can substitute for CDK9/cyclin-T P-TEFb in vitro. Replication stress response protein; the CDK9/cyclin-K complex is required for genome integrity maintenance, by promoting cell cycle recovery from replication arrest and limiting single-stranded DNA amount in response to replication stress, thus reducing the breakdown of stalled replication forks and avoiding DNA damage. In addition, probable function in DNA repair of isoform 2 via interaction with KU70/XRCC6. Promotes cardiac myocyte enlargement.

UOM: 1 * 100 µl

Tilbud