You Searched For: D-Lysine

Catalog Number: (PRSI79-759)

Supplier: ProSci Inc.

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. 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 µG

Catalog Number: (PRSI6219)

Supplier: ProSci Inc.

Description: LRRFIP1 Antibody: LRRFIP1, also known as GC-binding factor 2 (GCF2), is a 738 amino acid transcriptional repressor that mainly plays a cytoskeletal role. It is primarily localized in the cytoplasm and preferentially binds to GC-rich dsDNA, but will also bind directly to dsRNA as well. The RNA binding domain encompasses a lysine-rich motif. LRRFIP1 interacts with the mammalian Flightless I (Fli-I) and is a key component in the cytoskeletal regulation of platelet function. LRRFIP1 and the related protein LRRFIP2 may modulate canonical WNT signaling and mediate the IRF3-induced production of type I interferon via a beta-catenin-dependent pathway.

UOM: 1 * 100 µG

Catalog Number: (PRSI91-976)

Supplier: ProSci Inc.

Description: Ubiquitin-Conjugating Enzyme E2 G2 (UBE2G2) is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation, which belong to the ubiquitin-conjugating enzyme family. It shares 60% and 100% sequence identity with S.cerevisiae Ubc7 and mouse respectively. The UBE2G2 enzyme and the GP78 E3 ligase are active components of endoplasmic reticulum-associated degradation pathway which is essential for the degradation of misfolded ER proteins. The mechanism of K48-linked poly-ubiquitination by UBE2G2/GP78 appears to involve the transfer of preassembled Ub chains from UBE2G2 to lysine residues in a substrate. The E2 and E3 enzymes form a large hetero-oligomer which brings multiple UBE2G2 molecules into close proximity which allows for Ub transfer between neighboring E2s.

UOM: 1 * 50 µG

Catalog Number: (PRSI27-006)

Supplier: ProSci Inc.

Description: TRIB2 is one of three members of the Tribbles family. The Tribbles members share a Trb domain, which is homologous to protein serine-threonine kinases, but lacks the active site lysine and probably lacks a catalytic function. The Tribbles proteins interact and modulate the activity of signal transduction pathways in a number of physiological and pathological processes. This Tribbles member induces apoptosis of cells mainly of the hematopoietic origin. It has been identified as a protein up-regulated by inflammatory stimuli in myeloid (THP-1) cells, and also as an oncogene that inactivates the transcription factor C/EBPalpha (CCAAT/enhancer-binding protein alpha) and causes acute myelogenous leukemia.

UOM: 1 * 50 µG

Catalog Number: (PRSI91-351)

Supplier: ProSci Inc.

Description: Brain-Specific Serine Protease 4 (BSSP-4) is a serine protease that preferentially cleaves the synthetic substrate H-D-Leu-Thr-Arg-pNA compared to tosyl-Gly-Pro-Arg-pNA. BSSP-4 is expressed abundantly in the epithelial cells of the airways, including trachea, esophagus and fetal lung, but scarce in adult lung and expressed at low levels in placenta, pancreas, prostate and thyroid gland. BSSP-4 belongs to the peptidase S1 family and related to trypsin, referentially hydrolyzing substrates after arginine and lysine residues. However, BSSP-4 is less susceptible to inhibition by common trypsin inhibitors such as aprotinin, alpha1-antitrypsin and secretory leukocyte protease inhibitor. BSSP-4 efficiently converts pro-urokinase- type plasminogen activator to its mature, active form.

UOM: 1 * 50 µG

Catalog Number: (PRSI49-312)

Supplier: ProSci Inc.

Description: SIRT7 is a human member of a family of proteins called Sirtuins (Sir2-like proteins) and are present in prokaryotes and eukaryotes. All Sir2-like proteins have a sirtuin core domain, which contains a series of sequence motifs conserved in organisms ranging from bacteria to humans. Bacterial, yeast and mammalian sirtuins are able to metabolize NAD and possibly at as mono-ADP-ribosyltransferases. The enzymatic function of sirtuins is not yet completely understood but recent reports of histone-activated Sir2-mediated NAD metabolism and NAD-activated Sir2-mediated histone deacetylation suggest a possible coupled reciprocal activation mechanism involving interactions of Sir2 with NAD and the N epsilon-acetyl-lysine groups of acetylated histones.

UOM: 1 * 50 µG

Catalog Number: (PRSI5765)

Supplier: ProSci Inc.

Description: SIRT1 Antibody: The Silent Information Regulator (SIR2) family of genes are highly conserved from prokaryotes to eukaryotes and have important functions in the regulation of metabolism, growth and differentiation, inflammation, cellular survival, as well as in senescence and lifespan extension. Sirtuins, including SIRT1-7, are human homologs of yeast Sir2p. Sirtuins are NAD+-dependent histone/protein deacetylases (HDAC) which regulate cellular metabolism, e.g. energy metabolism, and thereby are associated with aging and several age-related diseases. SIRT1 has the closest homology to the yeast Sir2p and is widely expressed in fetal and adult tissues. SIRT1 regulates the p53-dependent DNA damage response pathway by binding to and deacetylating p53, specifically via lysine residue.

UOM: 1 * 100 µG

Catalog Number: (PRSI49-311)

Supplier: ProSci Inc.

Description: SIRT5 is a human member of a family of proteins called Sirtuins (Sir2-like proteins) and are present in prokaryotes and eukaryotes. All Sir2-like proteins have a sirtuin core domain, which contains a series of sequence motifs conserved in organisms ranging from bacteria to humans. Bacterial, yeast and mammalian sirtuins are able to metabolize NAD and possibly at as mono-ADP-ribosyltransferases. The enzymatic function of sirtuins is not yet completely understood but recent reports of histone-activated Sir2-mediated NAD metabolism and NAD-activated Sir2-mediated histone deacetylation suggest a possible coupled reciprocal activation mechanism involving interactions of Sir2 with NAD and the N epsilon-acetyl-lysine groups of acetylated histones.

UOM: 1 * 50 µG

Catalog Number: (PRSI3969)

Supplier: ProSci Inc.

Description: Sumo Antibody: The sumo family of proteins is related both structurally and functionally to ubiquitin in that they are post-translationally attached to the e-amino group of a lysine residue of the substrate protein. This sumoylation plays a number of roles in DNA replication and repair, protein targeting to various subnuclear structures, and the regulation of numerous cellular processes including the inflammatory response in mammalian cells. Sumo was initially identified as a covalent modification of RanGAP1 in studies on nuclear import in mammalian cells. More recently, sumo has been shown to be involved in the regulation of transcription factors, possibly by enhancing their interactions with co-repressors. Sumo is also thought to play some role in the modulation of ubiquitin-mediated degradation of proteins by acting as an inhibitor. At least four different isoforms of sumo are known to exist; Sumo antibody will only recognize isoform 1.

UOM: 1 * 100 µG

Catalog Number: (PRSI91-155)

Supplier: ProSci Inc.

Description: 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 * 50 µG

Catalog Number: (PRSI26-032)

Supplier: ProSci Inc.

Description: Cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. COX10 is heme A: farnesyltransferase, which is not a structural subunit but required for the expression of functional COX and functions in the maturation of the heme A prosthetic group of COX. This protein is predicted to contain 7-9 transmembrane domains localized in the mitochondrial inner membrane. A gene mutation, which results in the substitution of a lysine for an asparagine (N204K), is identified to be responsible for cytochrome c oxidase deficiency. In addition, this gene is disrupted in patients with CMT1A (Charcot-Marie-Tooth type 1A) duplication and with HNPP (hereditary neuropathy with liability to pressure palsies) deletion.Cytochrome c oxidase (COX), the terminal component of the mitochondrial respiratory chain, catalyzes the electron transfer from reduced cytochrome c to oxygen. This component is a heteromeric complex consisting of 3 catalytic subunits encoded by mitochondrial genes and multiple structural subunits encoded by nuclear genes. The mitochondrially-encoded subunits function in electron transfer, and the nuclear-encoded subunits may function in the regulation and assembly of the complex. This nuclear gene encodes heme A:farnesyltransferase, which is not a structural subunit but required for the expression of functional COX and functions in the maturation of the heme A prosthetic group of COX. This protein is predicted to contain 7-9 transmembrane domains localized in the mitochondrial inner membrane. A gene mutation, which results in the substitution of a lysine for an asparagine (N204K), is identified to be responsible for cytochrome c oxidase deficiency. In addition, this gene is disrupted in patients with CMT1A (Charcot-Marie-Tooth type 1A) duplication and with HNPP (hereditary neuropathy with liability to pressure palsies) deletion. Publication Note: This RefSeq record includes a subset of the publications that are available for this gene. Please see the Entrez Gene record to access additional publications.

UOM: 1 * 50 µG

Catalog Number: (PRSI3967)

Supplier: ProSci Inc.

Description: Cbl Antibody: The mammalian cbl family of ubiquitin ligases consists of three homologs known as cbl (also known as c-Cbl), Cbl-B, and Cbl-3 which share highly conserved a tyrosine-kinase-binding domain, linker and RING finger domain in their amino-terminal halves. Similar to other E3 ubiquitin ligases, Cbl catalyzes the transfer of ubiquitin from an E2 or Ubc (ubiquitin-conjugating) enzyme to the e-amino group of a lysine residue of the substrate protein. Cbl acts to negatively regulate many types of cell-surface receptors, including the Syk protein tyrosine kinase family. Cbl is thought to be involved in T- and B-cell signaling, in addition to thymus development. Of the three known homologs in the cbl family, cbl antibody reacts specifically with cbl. Multiple isoforms of cbl have been reported.

UOM: 1 * 100 µG

Catalog Number: (ROCK600-401-J22)

Supplier: Rockland Immunochemicals

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. Anti-HDAC7 antibodies are ideal for researches interested in Breast Cancer, Cancer, Cell Cycle and Replication, Chromatin Research, Epigenetics, and Histone Deacetylases research.

UOM: 1 * 100 µG

Catalog Number: (PRSI79-244)

Supplier: ProSci Inc.

Description: Histone Deacetylases (HDACs) are a group of enzymes closely related to sirtuins. They catalyze the removal of acetyl groups from lysine residues in histones and non-histone proteins, resulting in transcriptional repression. In general, they do not act autonomously but as components of large multiprotein complexes, such as pRb-E2F and mSin3A, that mediate important transcription regulatory pathways. There are three classes of HDACs; classes 1, 2 and 4, which are closely related Zn2+-dependent enzymes. HDACs are ubiquitously expressed and they can exist in the nucleus or cytosol. Their subcellular localization is effected by protein-protein interactions (for example HDAC-14.3.3 complexes are retained in the cytosol) and by the class to which they belong (class 1 HDACs are predominantly nuclear whilst class 2 HDACs shuttle between the nucleus and cytosol). HDACs have a role in cell growth arrest, differentiation and death and this has led to substantial interest in HDAC inhibitors as possible antineoplastic agents.

UOM: 1 * 100 µG

Catalog Number: (PRSI33-516)

Supplier: ProSci Inc.

Description: Reacts with a protein of ~66 kDa, identified as bovine serum albumin (BSA). It is a high affinity antibody and can be used for detection of traces of BSA. Bovine serum albumin (BSA) is an abundant plasma protein in cows that is important for maintaining osmotic pressure in blood plasma for proper distribution of body fluids between intravascular compartments and body tissues. BSA is a common buffer component for immunoglobulin type assays due to good solubility characteristics for water, Ca2+, Na+, K+, fatty acids, hormones and bilirubin. BSA makes up about half of the protein in plasma and represents the most stable and soluble protein in the plasma. It is a suitable reagent for laboratories developing immunoassays, mostly due to its availability, solubility and the numerous functional groups present for coupling. The BSA component contains several lysines that are capable of reacting with conjugation sites of linkers, making it applicable as a carrier protein for antigenic compounds.

UOM: 1 * 100 µG

New Product

Catalog Number: (PRSI5215)

Supplier: ProSci Inc.

Description: 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 * 100 µG