888 Results for: "2,6-diamine-4-enoic acid"

Supplier: Bioss

SAS-6 (spindle assembly abnormal protein 6 homolog, HsSAS-6) is a 657 amino acid protein encoded by the human gene SAS6. SAS-6 is a component of the centrosome that contains one PISA (present in SAS-6) domain. LK4, SAS-6, CPAP and other centriole related proteins are required at different stages of procentriole formation and were associated with different centriolar structures. SAS-6 associates only transiently with nascent procentrioles, whereas CEP135 and CPAP form a core structure within the proximal lumen of both parental and nascent centrioles. SAS-6 is necessary for procentriole formation in human cell lines and is localized asymmetrically next to the centriole at the onset of procentriole formation. SAS-6 levels oscillate during the cell cycle; it is degraded in mitosis starting at anaphase, and it accumulates again at the end of the following G1 phase. The anaphase-promoting complex targets SAS-6 for degradation by the 26S Proteasome, and a KEN box in the C-terminus of SAS-6 is necessary for its degradation. Increased SAS-6 levels promoted the formation of multiple procentrioles forming next to a single centriole.

Supplier: Proteintech

PRSS8(protease, serine, 8) displays trypsin-like enzymatic activities by hydrolyzing peptidyl fluorogenic substrates such as D-Pro-Phe-Arg-AMC. This trypsinlike enzymatic activity can be inhibited by aprotinin, antipain, leupeptin, and benzamidine. It is a heterodimer of two chains, light and heavy, which are held by a disulfide bond. PRSS8 is also named as CAP1 and belongs to the peptidase S1 family.

Supplier: Thermo Scientific Chemicals

4-(Cyanomethyl)phenylboronic acid 98%

Supplier: Peprotech

IL-6 is a pleiotropic cytokine that plays an important role in host defense by regulating immune and inflammatory responses. Produced by T cells, monocytes, fibroblasts, endothelial cells and keratinocytes, IL-6 has diverse biological functions. It stimulates B cell differentiation and antibody production, synergizes with IL-3 in megakaryocyte development and platelet production, induces expression of hepatic acute-phase proteins, and regulates bone metabolism. IL-6 signals through the IL-6 receptor system that consists of two chains, IL-6Rα and gp130. Murine IL-6 is inactive on human cells, while both human and murine are equally active on murine cells. Recombinant Rat IL-6 is a 21.7 kDa protein containing 188 amino acid residues.

Supplier: Thermo Scientific Chemicals

3-Bromo-p-toluic acid 98+%

Supplier: Bioss

FAM50A, also known as DXS9928E, HXC26, XAP5 or 9F, is a 339 amino acid nuclear protein that belongs to the FAM50 family. Expressed ubiquitously with highest expression in fetal kidney, liver and brain, as well as adult heart, spleen, skeletal muscle, prostate and small intestine, FAM50A is thought to function as a transcription factor that may bind to DNA. FAM50A contains an SV40 large T antigen nuclear localization signal and a polymorphic CCG repeat region in its 5’-UTR. Defects in the gene encoding FAM50A may be associated with acute lymphoblastic leukemia, suggesting a possible role for FAM50A in carcinogenesis.

Supplier: Proteintech

Matrix metalloproteinases (MMPs) play a critically important role in extracellular matrix remodeling and have been implicated in a number of key normal and pathologic processes.These proteases have come to represent important therapeutic and diagnostic targets for the treatment and detection of human cancers. MMP-3 activate procollagenase via two pathways: slow direct activation and rapid activation in conjunction with tissue or plasma proteinases.

Supplier: Proteintech

Ubiquitin is most famous for its function in targeting proteins for degradation by the 26S proteasome, ubiquitin needs to be attached to a substrate in chains (polyubiquitylation) before being recognized by proteasome. Similarly, SUMO (small ubiquitin-related modifier) can be linked to substrates in chains (polysumoylation), SUMO modification has been implicated in many important cellular processes including the control of genome stability, signal transduction, targeting to and formation of nuclear compartments, cell cycle and meiosis. There are 4 confirmed SUMO isoforms in human, SUMO-1, SUMO-2, SUMO-3 and SUMO-4. SUMO-2 and SUMO-3 are nearly identical but are distinct from SUMO-1. SUMO2/3 conjugation was recently widely involved in neuroprotective activities. A substitution (M55V) of SUMO4 was strongly associated with the pathogenesis of type 1 diabetes (T1D) involving NF kappa B related mechanisms.

Supplier: Proteintech

The hemoglobin molecule is a tetramer consisting of two alpha- and two beta-globin-like chains. HBA1 (hemoglobin alpha chain) protein is a alpha-type chain of hemoglobin encoded by two independent genes (HBA1 and HBA2) whose coding sequences are identical. Two alpha chains coupled with two beta chains constitute the adult hemoglobin (HbA or α2β2). HBA1 is also the component of fetal hemoglobin (HbF or α2γ2). This antibody detects a major band around 14-16 kDa in the western blot analysis of heart tissue and K-562 cells. A higher band around 26-27 kDa can also be observed occasionally, which may represents the dimer form of HBA1 (20836851). This antibody may cross-react with other hemoglobin chains.

Supplier: Peprotech

Visfatin is a 55 kDa protein produced and secreted primarily by white adipose tissue.  Recently, visfatin was isolated from visceral fat deposits and shown to possess insulin-mimetic activity.  Like insulin, visfatin exerts hypoglycemic effects by interacting with the insulin receptor.  The binding affinity of visfatin for the insulin receptor is similar to that of insulin, but it does not compete with insulin, suggesting that the two proteins interact with different receptor sites.  The circulating levels of visfatin are much lower than those of insulin and are not affected by feeding, implying that the hypoglycemic effect of visfatin may not be of physiological importance.  The plasma visfatin levels, like those of leptin, correlate positively with the percent of body fat, and increase during the development of obesity. Receptors for both leptin (Ob-R) and visfatin (i.e. the insulin receptor) are expressed by neurons within the arcuate nucleus of the hypothalamus, a brain area that plays a pivotal role in the regulation of energy metabolism.  Although the metabolic function of visfatin is still unknown, it appears that this newly identified adipocytokine might play an important role, similar to that of leptin, in the regulation of body weight, i.e. as an afferent signal reflecting excess body fat.  The PBEF gene encodes a polypeptide of 491 amino acid residues. The secreted form of this polypeptide, i.e. visfatin, contains 465 residues and lacks the first 26 N-terminal residues of the PBEF gene product. The 491-residue form has been shown to be a nicotinamide phosphoribosyltransferase, a cytosolic enzyme involved in NAD biosynthesis. The amino acid sequence of visfatin is highly conserved across different species and shows no homology to any known protein. It contains 5 cysteine residues, of which only two of them appear to be involved in disulfide bridge formation. Recombinant human Visfatin is a 52.6 kDa protein containing 466 amino acid residues (isoform 1).

Supplier: Prosci

CSN8 Antibody: The COP9 signalosome (CSN) is an evolutionarily conserved protein complex of the eight subunits that interacts with deubiquitinating enzymes and protein kinases and is highly homologous to the lid sub-complex of 26S proteasome. The CSN complex is an essential regulator of the ubiquitin conjugation pathway by mediating the deneddylation of the SCF-type E3 ligase complexes, which leads to a decrease in ubiquitin ligase activity of SCF-comlpexes such as SCF, CSA or DDB2. It is also involved in phosphorylation of p53, c-jun/JUN, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN8 encodes the smallest and the least conserved but first identified subunit of CSN. Recent studies show CSN8 is essential for Drosophila development and is essential for peripheral T cell homeostasis and antigen receptor-induced entry into the cell cycle from quiescence.

Supplier: Thermo Scientific Chemicals

(R)-(-)-Hydratropic acid 97%

Supplier: Thermo Scientific Chemicals

2-Indanylacetic acid 99%

Supplier: Peprotech

IL-6 is a pleiotropic cytokine that plays an important role in host defense by regulating immune and inflammatory responses. Produced by T cells, monocytes, fibroblasts, endothelial cells and keratinocytes, IL-6 has diverse biological functions. It stimulates B cell differentiation and antibody production, synergizes with IL-3 in megakaryocyte development and platelet production, induces expression of hepatic acute-phase proteins, and regulates bone metabolism. IL-6 signals through the IL-6 receptor system that consists of two chains, IL-6Rα and gp130. Murine IL-6 is inactive on human cells, while both human and murine are equally active on murine cells. Recombinant Murine IL-6 is a 21.7 kDa protein containing 188 amino acid residues.

Supplier: Thermo Scientific Chemicals

Supplier: Diagnostic Biosystems

This MAb recognizes human 17-26kDa protein, which is identified as cytokine TNF-α (Tumor Necrosis Factor-alpha). Monomeric human TNF-α is a 157 amino acid protein (non-glycosylated) with a reported molecular weight of 17 kDa and can be expressed as a free molecule, also TNF-α is generated as a precursor form called transmembrane TNF-α can be expressed as a cell surface type II polypeptide consisting of 233 amino acid residues molecular weight 26 kDa. TNF-α is an important cell-signaling component of the immune system. It is a protein secreted by LPS stimulated macrophages, and causes tumor necrosis when injected into tumor bearing mice. TNF-α is currently being evaluated in treatment of certain cancers and AIDS Related Complex.

Supplier: Prosci

IL-6 is a pleiotropic cytokine that plays an important role in host defense by regulating immune and inflammatory responses. Produced by T cells, monocytes, fibroblasts, endothelial cells and keratinocytes, IL-6 has diverse biological functions. It stimulates B-cell differentiation and antibody production, synergizes with IL-3 in megakaryocyte development and platelet production, induces expression of hepatic acute-phase proteins, and regulates bone metabolism. IL-6 signals through the IL-6 receptor system that consists of two chains, IL-6R α and gp130. Murine IL-6 is inactive on human cells, while both human and murine are equally active on murine cells. Recombinant human IL-6 is a 20.9 kDa protein containing 184 amino acid residues. Recombinant rat IL-6 is a 21.7 kDa protein containing 187 amino acid residues. Recombinant murine IL-6 is a 21.7 kDa protein containing 187 amino acid residues.

Supplier: Thermo Scientific Chemicals

3-Amino-p-anisic acid 98+%

Supplier: Thermo Scientific Chemicals

3-Fluoro-4-methoxyphenylboronic acid 98+%

Supplier: Proteintech

MAP1S (also known as C19ORF5 or VCY2IP1) is a novel member of the microtubule-associated protein 1 family and a homologue of the exclusively neuronal distributed microtubule-associated protein 1A and 1B (MAP1A/B). In contrast to MAP1A and MAP1B, MAP1S is expressed in a wide range of tissues in addition to neurons. MAP1S is synthesized as a precursor protein that is partially cleaved into heavy and light chains in a tissue-specific manner. In addition, a short chain isoform may be induced under prolonged mitotic arrest or inhibiton of the 26S proteasome. Recently it has been reported that the short chain isoform associates with mitochondria in addition to microtubules and causes irreversible aggregation of dysfunctional mitochondria resulting in cell death. Western blot analysis in human brain using this antibody detected two main bands between 100-130 kDa corresponding to heavy and light chains of MAP1S.

Supplier: Prosci

CIP75 Antibody: The ubiquitin-proteosome pathway of protein degradation is one of the mechanisms that ensure the proper level of cellular proteins. The ubiquitin-like (UbL) and ubiquitin-associated (UBA) domain containing protein family is thought to be involved in proteosomal degradation. One such protein is CIP75, also known as ubiquilin-4, interacts with a number of proteins such as Ataxin-1 and Connexin-43, resulting in an increased rate of turnover of these proteins. Overexpression CIP75 led to a significant reduction of Connexin-43 half-life, with the opposite being observed in siRNA knockdown experiments. CIP75 contains an N-terminal UbL domain which is thought to interact with proteins of the 26S proteosome complex and a C-terminal UBA domain which appears to mediate its interaction with Connexin-75. At least three isoforms of CIP75 are known to exist.

Supplier: Proteintech

Ubiquitin is most famous for its function in targeting proteins for degradation by the 26S proteasome, ubiquitin needs to be attached to a substrate in chains (polyubiquitylation) before being recognized by proteasome. Similarly, SUMO (small ubiquitin-related modifier) can be linked to substrates in chains (polysumoylation), SUMO modification has been implicated in many important cellular processes including the control of genome stability, signal transduction, targeting to and formation of nuclear compartments, cell cycle and meiosis. There are 4 confirmed SUMO isoforms in human, SUMO-1, SUMO-2, SUMO-3 and SUMO-4. SUMO-2 and SUMO-3 are nearly identical but are distinct from SUMO-1. SUMO2/3 conjugation was recently widely involved in neuroprotective activities. A substitution (M55V) of SUMO4 was strongly associated with the pathogenesis of type 1 diabetes (T1D) involving NF kappa B related mechanisms.This antibody can detect endogenous levels of SUMOylated proteins (e.g. SUMO-1-RanGAP at 80-90 kD).

Supplier: Proteintech

Ubiquitin is most famous for its function in targeting proteins for degradation by the 26S proteasome, ubiquitin needs to be attached to a substrate in chains (polyubiquitylation) before being recognized by proteasome. Similarly, SUMO (small ubiquitin-related modifier) can be linked to substrates in chains (polysumoylation), SUMO modification has been implicated in many important cellular processes including the control of genome stability, signal transduction, targeting to and formation of nuclear compartments, cell cycle and meiosis. There are 4 confirmed SUMO isoforms in human, SUMO-1, SUMO-2, SUMO-3 and SUMO-4. SUMO-2 and SUMO-3 are nearly identical but are distinct from SUMO-1. SUMO2/3 conjugation was recently widely involved in neuroprotective activities. A substitution (M55V) of SUMO4 was strongly associated with the pathogenesis of type 1 diabetes (T1D) involving NF kappa B related mechanisms.

Supplier: Proteintech

RAD23A, also named as HHR23A, belongs to the RAD23 family. It is a multiubiquitin chain receptor involved in modulation of proteasomal degradation. RAD23A binds to 'Lys-48'-linked polyubiquitin chains in a length-dependent manner and with a lower affinity to 'Lys-63'-linked polyubiquitin chains. It is proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. It is involved in nucleotide excision repair and is thought to be functional equivalent for RAD23B in global genome nucleotide excision repair (GG-NER) by association with XPC. In vitro, the XPC:RAD23A dimer has NER activity. Can stabilize XPC. It is also involved in vpr-dependent replication of HIV-1 in non-proliferating cells and primary macrophages and is required for the association of HIV-1 vpr with the host proteasome. This antibody is a rabbit polyclonal antibody raised against full length RAD23A of human origin.

Supplier: Prosci

Interleukin-20 (IL-20) is a member of the IL-10 family of regulatory cytokines that includes IL-10, IL-19, IL-20, IL-22, IL-24 and IL-26. Members of this family share partial homology in their amino acid sequences but they are dissimilar in their biological functions. IL-20 exhibits approximately 28% amino acid identity with IL-10 and 76% amino acid identity with mouse IL-20. There are two heterodimeric receptor complexes for IL-20. The first is composed of IL-20 R alpha and IL-20 R beta . The second is composed of IL-22 R and IL-20 R beta . Whereas the IL-22 R/IL-20 R beta complex is shared with IL-24, the IL-20 R alpha/IL-20 R beta complex is shared with both IL-19 and IL-24. IL-20 has been shown to initiate transduction cascades involving STAT3 and stimulates the induction of pro-inflammatory genes including TNF- alpha and MCP-1. Initial functional studies using transgenic mice suggest that IL-20 has the ability to regulate skin development. The over-expression of both human and mouse forms of IL-20 results in keratinocyte hyper-proliferation, abnormal epidermal differentiation, and neonatal lethality. In humans, IL-20 and its receptors are up-regulated in psoriatic skin, and polymorphisms in the IL-20 gene have been associated with plaque-type psoriasis. IL-20 may also have a role in hematopoiesis. It enhances the proliferation of multi-potential progenitors in vitro and increases their numbers and cell cycling status in IL-20 transgenic mice. IL-20 is also shown to suppress COX-2 and PGE2 and acts as an inhibitor of angiogenesis in model systems.

Supplier: Prosci

CIP75 Antibody: The ubiquitin-proteosome pathway of protein degradation is one of the mechanisms that ensure the proper level of cellular proteins. The ubiquitin-like (UbL) and ubiquitin-associated (UBA) domain containing protein family is thought to be involved in proteosomal degradation. One such protein is CIP75, also known as ubiquilin-4, interacts with a number of proteins such as Ataxin-1 and Connexin-43, resulting in an increased rate of turnover of these proteins. Overexpression CIP75 led to a significant reduction of Connexin-43 half-life, with the opposite being observed in siRNA knockdown experiments. CIP75 contains an N-terminal UbL domain which is thought to interact with proteins of the 26S proteosome complex and a C-terminal UBA domain which appears to mediate its interaction with Connexin-75. At least three isoforms of CIP75 are known to exist.

Supplier: Thermo Scientific Chemicals

3,5-Di-tert-butylbenzoic acid 99%

Supplier: Thermo Scientific Chemicals

1,4-Phenyldiboronic acid 96%

Supplier: Proteintech

VEGFA, also named as VEGF or VPF, belongs to the PDGF/VEGF growth factor family. It is a growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. VEGFA induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. It binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. Defects in VEGFA are a cause of susceptibility to microvascular complications of diabetes type 1 (MVCD1). VEGFA has 13 isoforms with MW 16kd to 45kd. Some isoforms has homodimer form, such as VEGFA189(38kd), VEFGA110(34kd). VEGFA is a 34kd to 42kd, dimeric, disulfide-bound glycoprotein. VEGF-A exists in at least seven homodimeric isoforms. The monomers consist of 121, 145, 148, 165, 183, 189, or 206 amino acids. This antibody can recognize all the isoforms of VEFGA.

Supplier: Thermo Scientific Chemicals

Soluble in acetic acid, dilute mineral acids, ammonia. Insoluble in water