"Virginiamycin+complex&amp"

Supplier: Biorbyt

Anti-RSF1 Rabbit Polyclonal Antibody

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 homodimerisation 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

Collapsin response mediator proteins (CRMPs) are cytosolic phosphoproteins involved in neuronal differentiation and axonal guidance. CRMP2 was previously shown to mediate the repulsive effect of Sema3A on axons and to participate in axonal specification. The CRMPs appear to play a complex role in axon growth as well as microtubule dynamics and axon induction. CRMPs localise to the lamellipodia and filopodia of axonal growth cones, suggesting a role in axon guidance. Moreover, CRMP2 is upregulated after axotomy, and appears to increase the formation of axon-type processes from hippocampal neurons. CRMP2 has been reported to bind tubulin dimers directly and modulate microtubule assembly. CRMPs have also been implicated in the pathogenesis of a paraneoplastic neurologic syndrome. Interaction studies have implicated phospholipase D2 (PLD2), the cytosolic tyrosine kinase Fes, and intersectin in CRMP function. Hyperphosphorylation of CRMP2 is an early event in the progression of Alzheimer's disease.

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

SH3MD2 acts as a scaffold protein, contributes to Rac-induced signal transduction such as JNKs (MAPK8 and MAPK9) activation and induces apoptosis. Within a signaling complex, it probably recruits protein kinases such as MAP3K10 or MAP3K11 which are in turn activated leading to the sequential activation of MAP2K4, MAP2K7 and JNKs (MAPK8 and MAPK9). SH3MD2 may be involved in targeting of HIV-1 GAG and GAG-POL polyproteins to the plasma membrane. This gene encodes a protein containing an N-terminus RING-finger, four SH3 domains, and a region implicated in binding of the Rho GTPase Rac. Via the RING-finger, the encoded protein has been shown to function as an ubiquitin-protein ligase involved in protein sorting at the trans-Golgi network. The encoded protein may also act as a scaffold for the c-Jun N-terminal kinase signaling pathway, facilitating the formation of a functional signaling module. There are two named isoforms.

Supplier: Bioss

SH3MD2 acts as a scaffold protein, contributes to Rac-induced signal transduction such as JNKs (MAPK8 and MAPK9) activation and induces apoptosis. Within a signaling complex, it probably recruits protein kinases such as MAP3K10 or MAP3K11 which are in turn activated leading to the sequential activation of MAP2K4, MAP2K7 and JNKs (MAPK8 and MAPK9). SH3MD2 may be involved in targeting of HIV-1 GAG and GAG-POL polyproteins to the plasma membrane. This gene encodes a protein containing an N-terminus RING-finger, four SH3 domains, and a region implicated in binding of the Rho GTPase Rac. Via the RING-finger, the encoded protein has been shown to function as an ubiquitin-protein ligase involved in protein sorting at the trans-Golgi network. The encoded protein may also act as a scaffold for the c-Jun N-terminal kinase signaling pathway, facilitating the formation of a functional signaling module. There are two named isoforms.

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: 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 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

Collapsin response mediator proteins (CRMPs) are cytosolic phosphoproteins involved in neuronal differentiation and axonal guidance. CRMP2 was previously shown to mediate the repulsive effect of Sema3A on axons and to participate in axonal specification. The CRMPs appear to play a complex role in axon growth as well as microtubule dynamics and axon induction. CRMPs localize to the lamellipodia and filopodia of axonal growth cones, suggesting a role in axon guidance. Moreover, CRMP2 is upregulated after axotomy, and appears to increase the formation of axon-type processes from hippocampal neurons. CRMP2 has been reported to bind tubulin dimers directly and modulate microtubule assembly. CRMPs have also been implicated in the pathogenesis of a paraneoplastic neurologic syndrome. Interaction studies have implicated phospholipase D2 (PLD2), the cytosolic tyrosine kinase Fes, and intersectin in CRMP function. Hyperphosphorylation of CRMP2 is an early event in the progression of Alzheimer's disease.

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

The regulated oscillation of protein expression is an essential mechanism of cell cycle control. The SCF class of E3 ubiquitin ligases is involved in this process by targeting cell cycle regulatory proteins for degradation by the proteasome, with the F-box subunit of the SCF specifically recruiting a given substrate to the SCF core. NIPA (nuclear interaction partner of ALK) is a human F-box-containing protein that defines an SCF-type E3 ligase (SCFNIPA) controlling mitotic entry. Assembly of this SCF complex is regulated by cell-cycle-dependent phosphorylation of NIPA, which restricts substrate ubiquitination activity to interphase. Nuclear cyclin B1 is a substrate of SCFNIPA. Inactivation of NIPA by RNAi results in nuclear accumulation of cyclin B1 in interphase, activation of cyclin B1-Cdk1 kinase activity, and premature mitotic entry. Thus, SCFNIPA-based ubiquitination may regulate S-phase completion and mitotic entry in the mammalian cell cycle.

Supplier: Bioss

Collapsin response mediator proteins (CRMPs) are cytosolic phosphoproteins involved in neuronal differentiation and axonal guidance. CRMP2 was previously shown to mediate the repulsive effect of Sema3A on axons and to participate in axonal specification. The CRMPs appear to play a complex role in axon growth as well as microtubule dynamics and axon induction. CRMPs localize to the lamellipodia and filopodia of axonal growth cones, suggesting a role in axon guidance. Moreover, CRMP2 is upregulated after axotomy, and appears to increase the formation of axon-type processes from hippocampal neurons. CRMP2 has been reported to bind tubulin dimers directly and modulate microtubule assembly. CRMPs have also been implicated in the pathogenesis of a paraneoplastic neurologic syndrome. Interaction studies have implicated phospholipase D2 (PLD2), the cytosolic tyrosine kinase Fes, and intersectin in CRMP function. Hyperphosphorylation of CRMP2 is an early event in the progression of Alzheimer's disease.

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

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.