"Virginiamycin+complex&amp"

Supplier: Cayman Chemical

CYCLIC AMP EIA ANTISERUM 1 * 100 Tests

Supplier: ProSci Inc.

Beta Catenin is a dual function protein, regulating the coordination of cell–cell adhesion and gene transcription. In humans, the CTNNB1 protein is encoded by the CTNNB1 gene. In Drosophila, the homologous protein is called armadillo. b-Catenin is a subunit of the cadherin protein complex and acts as an intracellular signal transducer in the Wnt signaling pathway. It is a member of the catenin protein family and homologous to gamma-Catenin, also known as plakoglobin. b-Catenin is widely expressed in many tissues. In cardiac muscle, it localizes to adherens junctions in intercalated disc structures, which are critical for electrical and mechanical coupling between adjacent cardiomyocyte. [Wiki].

Supplier: Cayman Chemical

Cyclic AMP TR-FRET Kit 1 * 1 items

Supplier: Biorbyt

Anti-NNF1R Rabbit Polyclonal Antibody (FITC (Fluorescein))

Supplier: Cayman Chemical

AMP+ Mass Spectrometry Kit 1 * 50 Tests

Supplier: Cayman Chemical

CYCLIC AMP ELISA KIT 1 * 480 Tests

Supplier: ProSci Inc.

The Fas is also known as FAS receptor (FasR), apoptosis antigen 1 (APO-1 or APT), cluster of differentiation 95 (CD95) or tumor necrosis factor receptor superfamily member 6 (TNFRSF6). is a death receptor on the surface of cells that leads to programmed cell death (apoptosis). It is one of two apoptosis pathways, the other being the mitochondrial pathway. FasR is located on chromosome 10 in humans and 19 in mice. Similar sequences related by evolution (orthologs) are found in most mammals. Fas forms the death-inducing signaling complex (DISC) upon ligand binding. Membrane-anchored Fas ligand trimer on the surface of an adjacent cell causes trimerization of Fas receptor. This event is also mimicked by binding of an agonistic Fas antibody, though some evidence suggests that the apoptotic signal induced by the antibody is unreliable in the study of Fas signaling. To this end, several clever ways of trimerizing the antibody for in vitro research have been employed.Upon ensuing death domain (DD) aggregation, the receptor complex is internalized via the cellular endosomal machinery. This allows the adaptor molecule FADD to bind the death domain of Fas through its own death domain. Recently, Fas has also been shown to promote tumor growth, since during tumor progression, it is frequently downregulated or cells are rendered apoptosis resistant. Cancer cells in general, regardless of their Fas apoptosis sensitivity, depend on constitutive activity of Fas. This is stimulated by cancer-produced Fas ligand for optimal growth.

Supplier: ProSci Inc.

Toll-Interacting Protein (TOLLIP) is a member of the tollip family. TOLLIP localizes to the cytoplasm. It contains one C2 domain and one CUE domain. TOLLIP is an inhibitory adaptor protein for Toll-like receptors (TLR). The Toll-like receptors pathway is a part of the immune system that recognize structurally conserved molecular patterns of microbial pathogens, resulting in an inflammatory immune response. TOLLIP constitutes a complex with Tom1 to regulate endosomal transferring of ubiquitinated proteins. TOLLIP can negative regulate Toll-like receptors signaling, which may limit the production of proinflammatory mediators during the process of inflammation and infection.

Supplier: ProSci Inc.

Serpin Peptidase Inhibitor, Clade A ( alpha-1 Antiproteinase, Antitrypsin), Member 4 (Serpin A4) is a member of the Serpin family. Serpin A4 exists as a monomer and some homodimers. Serpin A4 is expressed by the liver and secreted in plasma. Serpin A4 is a regulator of vascular homeostasis capable of controlling a wide spectrum of biological actions in the cardiovascular and renal systems. It can inhibit intracellular reactive oxygen species formation in cultured cardiac and renal cells. In addition, Serpin A4 has anti-inflammatory effect. Heparin blocks kallistatin's complex formation with tissue kallikrein and abolishes its inhibitory effect on tissue kallikrein's activity.

Supplier: LIOFILCHEM

AMPICILLIN AMP 10 µG 1 * 250 items

Supplier: Bioss

The human protooncogene JUN is the putative transforming gene of avian sarcoma virus 17, and it encodes a protein which is highly homologous to the viral protein. cJun (previously known as the Fos binding protein p39) and c Fos form a complex in the nucleus. AP 1 (activating protein 1) is a collective term referring to these dimeric transcription factors composed of Jun, Fos or ATF subunits that bind to a common DNA site, the AP1 binding site. AP 1 proteins, mostly the Jun group, regulate the expression and function of cell cycle regulators such as Cyclin D1, p53, p21 (cip1/waf1), p19 (ARF) and p16. Fos and Jun proto oncogene expression is induced transiently by a variety of extracellular stimuli associated with mitogenesis, differentiation processes or depolarization of neurons. JUN has been mapped to 1p32 to p31, a chromosomal region involved in both translocations and deletions in human malignancies.

Supplier: Bioss

Guanine nucleotide-exchange proteins (GEPs) accelerate replacement of bound GDP with GTP and thereby activate ADP-ribosylation factors (ARFs), a family of guanine nucleotide-binding proteins that play an important role in intracellular vesicular trafficking. GEPs comprise two major families, large GEPs that are inhibited by brefeldin A (BFA), a protein that effects Golgi structure and a group of smaller GEPs that are insenstive to BFA. Two genes for GEPs found on human chromosomes 8 and 20 encode BFA sensitive GEPs designated BIG1 and BIG2. Both GEPS contain a sec7 domain that is responsible for their brefeldin inhibition and also their catalytic activity. In vivo, BIG1 and BIG2 exist in macromolecular complexes that move between the Golgi membranes and cytosol. BIG2 associates with PKA regulatory subunits, implying that BIG2 may act as an A kinase-anchoring protein (AKAP) that could coordinate the cAMP and ARF regulatory pathways.

Supplier: Bioss

TAP is an integral transmembrane protein involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum for association with MHC class I molecules. It is a heterodimer of TAP1 and TAP2, and the peptide-binding site is shared between the cytoplasmic loops of TAP1 and TAP2. TAP is inducible by interferon gamma and belongs to the ABC transporter family, MDR subfamily. TAP also acts as a molecular scaffold for the final stage of MHC class I folding, namely the binding of peptide. Nascent MHC class I molecules associate with TAP via tapasin. TAP is inhibited by the covalent attachment of herpes simplex virus ICP47 protein, which blocks the peptide-binding site of TAP. It is inhibited by human cytomegalovirus US6 glycoprotein, which binds to the lumenal side of the TAP complex and inhibits peptide translocation by specifically blocking ATP-binding to TAP and prevents the conformational rearrangement of TAP induced by peptide binding.

Supplier: Biotium

This MAb reacts with the beta-chain of HLA-DRB1 antigen, a member of MHC class II molecules. It does not cross react with HLA-DP and HLA-DQ. HLA-DR is a heterodimeric cell surface glycoprotein comprised of a 36 kDa alpha (heavy) chain and a 28 kDa beta (light) chain. It is expressed on B-cells, activated T-cells, monocytes/macrophages, dendritic cells and other non-professional APCs. In conjunction with the CD3/TCR complex and CD4 molecules, HLA-DR is critical for efficient peptide presentation to CD4 T cells. It is an excellent histiocytic marker in paraffin sections producing intense cytoplasmic staining. True histiocytic neoplasms are similarly positive. HLA-DR antigens also occur on a variety of epithelial cells and their corresponding neoplastic counterparts. Loss of HLA-DR expression is related to tumor microenvironment and predicts adverse outcome in diffuse large B-cell lymphoma.

Supplier: Bioss

The BTB (Broad-Complex, Tramtrack and Bric a brac) domain, also known as the POZ (Poxvirus and Zinc finger) domain, is an N-terminal homodimerization domain that contains multiple copies of kelch repeats and/or C2H2-type zinc fingers. Proteins that contain BTB domains are thought to be involved in transcriptional regulation via control of chromatin structure and function. ZBTB1 (zinc finger and BTB domain containing 1), also known as KIAA0997, is a 713 amino acid nuclear protein that contains one BTB (POZ) domain and 8 C2H2-type zinc fingers. ZBTB2 is a 514 amino acid nuclear protein that contains one BTB (POZ) domain and 4 C2H2-type zinc fingers. ZBTB25, also known as ZNF46 or KUP, is a 435 amino acid nuclear protein that is expressed mainly in hematopoietic cells and testis and contains one BTB (POZ) domain and 2 C2H2-type zinc fingers.

Supplier: Bioss

The human complement subcomponent C1q associates with C1r and C1s in order to yield the first component of the serum complement system (SCS). The SCS contains over 30 glycoproteins that influence physiological mechanisms of the body in response to immune complex (the classical pathway), carbohydrate (the lectin pathway) or bacterial (alternative pathway) initiation. C1q binding protein (C1QBP), also designated gC1q-R, p32 (p33) or HABP1 (hyaluronan-binding protein 1), is known to bind the globular heads of C1q molecules and inhibit C1 activation. C1QBP has been described as a complement receptor for C1q on B cells, neutrophils and mast cells. The C1QBP protein may form homodimers. C1QBP is expressed in vascular endothelial cells and has been found to be a multifunctional protein interacting with elements of complement, coagulation and kinin systems. In addition, C1QBP is a subunit of pre-mRNA splicing factor SF2/ASF.