"Virginiamycin+complex&amp"

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.

Supplier: Bioss

Eukaryotic translation initiation factor 2C (eIF2C) proteins (argonaute family) influence RNA interference (RNAi) as components of the RNA-inducible silencing complex (RISC) or microRNA (miRNA)-containing ribonucleoprotein particle (miRNP). Small RNAs, including small interfering RNAs (siRNAs) and miRNAs, can silence target genes through mechanisms that utilize RISC or miRNP particles. eIF2C1 (argonaute 1, AGO1, eIF2C, GERP95, Q99) and Dicer1 play a coordinated role in siRNA-mediated gene silencing. eIF2C2 (Slicer, argonaute 2, AGO2, Q10) is a RISC component that can concentrate in cytoplasmic processing bodies (P-bodies) and catalyze mRNA cleavage. Mammalian P-bodies contain mRNAs and have an association with miRNA-induced translational silencing and siRNA-induced mRNA degradation. Additional eIF2C proteins include eIF2C3 (argonaute 3, AGO3), eIF2C4 (argonaute 4, AGO4) and meIF2c5 (mouse argonaute 5).

Supplier: Bioss

Eukaryotic translation initiation factor 2C (eIF2C) proteins (argonaute family) influence RNA interference (RNAi) as components of the RNA-inducible silencing complex (RISC) or microRNA (miRNA)-containing ribonucleoprotein particle (miRNP). Small RNAs, including small interfering RNAs (siRNAs) and miRNAs, can silence target genes through mechanisms that utilize RISC or miRNP particles. eIF2C1 (argonaute 1, AGO1, eIF2C, GERP95, Q99) and Dicer1 play a coordinated role in siRNA-mediated gene silencing. eIF2C2 (Slicer, argonaute 2, AGO2, Q10) is a RISC component that can concentrate in cytoplasmic processing bodies (P-bodies) and catalyze mRNA cleavage. Mammalian P-bodies contain mRNAs and have an association with miRNA-induced translational silencing and siRNA-induced mRNA degradation. Additional eIF2C proteins include eIF2C3 (argonaute 3, AGO3), eIF2C4 (argonaute 4, AGO4) and meIF2c5 (mouse argonaute 5).

Supplier: ProSci Inc.

FBXW8 is a member of the F-box protein family, members of which are characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into three classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. FBXW8 contains a WD-40 domain, in addition to an F-box motif, so it belongs to the Fbw class.This gene encodes a member of the F-box protein family, members of which are characterized by an approximately 40 amino acid motif, the F-box. The F-box proteins constitute one of the four subunits of ubiquitin protein ligase complex called SCFs (SKP1-cullin-F-box), which function in phosphorylation-dependent ubiquitination. The F-box proteins are divided into three classes: Fbws containing WD-40 domains, Fbls containing leucine-rich repeats, and Fbxs containing either different protein-protein interaction modules or no recognizable motifs. The protein encoded by this gene contains a WD-40 domain, in addition to an F-box motif, so it belongs to the Fbw class. Alternatively spliced transcript variants encoding distinct isoforms have been identified for this gene.

Supplier: Biorbyt

Anti-p19INK4d Mouse Monoclonal Antibody

Supplier: Biorbyt

Anti-GOLM1 Rabbit Polyclonal Antibody

Supplier: Bioss

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.

Supplier: Bioss

This gene encodes a G-protein beta-subunit-like polypeptide which is a member of the WD repeat protein family. WD repeats are minimally conserved regions of approximately 40 amino acids typically bracketed by gly-his and trp-asp (GH-WD), which may facilitate formation of heterotrimeric or multiprotein complexes. Members of this family are involved in a variety of cellular processes, including cell cycle progression, signal transduction, apoptosis, and gene regulation. This protein contains 6 WD repeats and is highly expressed in the heart. The gene maps to the region on chromosome 22q11, which is deleted in DiGeorge syndrome, trisomic in derivative 22 syndrome and tetrasomic in cat-eye syndrome. Therefore, this gene may contribute to the etiology of those disorders. Transcripts from this gene share exons with some transcripts from the C22orf29 gene. [provided by RefSeq, Jul 2008].

Supplier: Bioss

This protein belongs to a family of Zn-containing metallocarboxypeptidases specific to C-terminal lysine and arginine residues. It circulates in plasma as a zymogen with molecular weight of 55 kDa (401 amino acid residues; pI 5.0). Being activated by thrombin-thrombomodulin complex during blood coagulation, it exerts carboxypeptidase activity. Activated carboxypeptidase B2 removes C-terminal lysine residues from fibrin, which is necessary for plasminogen binding to fibrin. This prevents plasminogen from activation into plasmin and retards the lysis of a fibrin clot. The concentration in plasma of healthy people is 5-10 ug/ml. High plasma levels were found in patients with stable angina pectoris and angiographically verified coronary artery disease. Elevated concentration in blood is considered as a risk factor for venous thrombosis. A deficiency might contribute to the severity of bleeding disorders in hemophilias A and B, and decreased levels are found in chronic liver disease.

Supplier: Bioss

Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome. Binds to the phospholipid lysobisphosphatidic acid (LBPA) which is abundant in MVBs internal membranes. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and enveloped virus budding (HIV-1 and other lentiviruses). Appears to be an adapter for a subset of ESCRT-III proteins, such as CHMP4, to function at distinct membranes. Required for completion of cytokinesis. Involved in HIV-1 virus budding. Can replace TSG101 it its role of supporting HIV-1 release; this function implies the interaction with CHMP4B. May play a role in the regulation of both apoptosis and cell proliferation.

Supplier: Bioss

Potential tumor suppressor. Required for death receptor-dependent apoptosis. Mediates activation of STK3/MST2 and STK4/MST1 during Fas-induced apoptosis by preventing their dephosphorylation. When associated with MOAP1, promotes BAX conformational change and translocation to mitochondrial membranes in response to TNF and TNFSF1 stimulation. Isoform A interacts with CDC2, an activator of the anaphase-promoting complex, APC, resulting in the inhibition of APC activity and mitotic progression. Inhibits proliferation by negatively regulating cell cycle progression at the level of G1/S-phase transition by regulating accumulation of cyclin D1 protein. Isoform C has been shown not to perform these roles, no function has been identified for this isoform. Isoform A disrupts interactions among MDM2, DAXX and USP7, thus contributing to the efficient activation of TP53 by promoting MDM2 self-ubiquitination in cell-cycle checkpoint control in response to DNA damage.

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: Bioss

The ubiquitin (Ub) pathway involves three sequential enzymatic steps that facilitate the conjugation of Ub and Ub-like molecules to specific protein substrates. The first step requires the ATP-dependent activation of the Ub C-terminus and the assembly of multi-Ub chains by the Ub-activating enzyme known as the E1 component. The Ub chain is then conjugated to the Ub-conjugating enzyme (E2) to generate an intermediate Ub-E2 complex. The Ub-ligase (E3) then catalyzes the transfer of Ub from E2 to the appropriate protein substrate. UBE2E1 and UBE2L3, also designated UBCH6 and UBCH7 respectively in human, are E2 conjugating enzymes that interact with various proteins. Specifically, UBE2E1 interacts with the tumor suppressor protein TSSC5. UBE2L3 has been shown to mediate c-fos degradation, NF-kB maturation, human papilloma virus-mediated p53 and Myc protein degradation.

Supplier: Bioss

The ubiquitin (Ub) pathway involves three sequential enzymatic steps that facilitate the conjugation of Ub and Ub-like molecules to specific protein substrates. The first step requires the ATP-dependent activation of the Ub C-terminus and the assembly of multi-Ub chains by the Ub-activating enzyme known as the E1 component. The Ub chain is then conjugated to the Ub-conjugating enzyme (E2) to generate an intermediate Ub-E2 complex. The Ub-ligase (E3) then catalyzes the transfer of Ub from E2 to the appropriate protein substrate. UBE2E1 and UBE2L3, also designated UBCH6 and UBCH7 respectively in human, are E2 conjugating enzymes that interact with various proteins. Specifically, UBE2E1 interacts with the tumor suppressor protein TSSC5. UBE2L3 has been shown to mediate c-fos degradation, NF-kB maturation, human papilloma virus-mediated p53 and Myc protein degradation.

Supplier: Bioss

CYTIP is a cytoplasmic protein that is involved in lymphocytic cell adhesion. Expressed primarily in hematopoetic cells, CYTIP regulates the activity of cytohesin-1 (an integrin-activating protein involved in cell adhesion) by mediating its recruitment to the leukocyte membrane. Through its ability to bind cytohesin-1, CYTIP is able to sequester it to the cytoplasm, thereby preventing cytohesin-1 translocation to lymphocytes and interrupting the flow of information in the cell adhesion pathway. CYTIP can be recruited from the cytoplasm to the membrane by leukocyte integrins which interact with CYTIP through its PDZ domain. After membrane translocation, CYTIP can be re-located to the cytoplasm via exposure to a phorbol ester. Additionally, CYTIP associates with SNX27 (sorting nexin 27) and helps to coordinate trafficking and signaling complexes. Up-regulation of CYTIP is observed in maturing dendritic cells, suggesting a possible role in developmentally-controlled cell adhesion.

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.