31756 Results for: "Benzoyl+isothiocyanate"

Supplier: Tonbo Biosciences

The 3G3 antibody reacts with mouse Foxp3, a 50-55 kDa transcription factor which is a central regulator of T cell activity and is critical for the development and function of regulatory T cells (Tregs). Foxp3 is expressed at constitutively high levels in Treg cells, which are further identified as being CD4+ CD25+. In resting conventional T cells (CD4+ CD25-) Foxp3 expression is restricted, and upon TCR activation is expressed only transiently and in a small proportion of cells. However, the growth factor TGF-beta has been shown to induce expression of Foxp3 in naïve T cells, driving their development into Foxp3+ Tregs, which are called “induced” or “adaptive” Tregs. These cells are phenotypically similar to so-called “natural” Tregs (CD4+ CD25high Foxp3+) which originate in the thymus and comprise the majority of Treg cells. Tregs are critical for maintaining peripheral tolerance and are implicated in the development of autoimmunity.

Supplier: Tonbo Biosciences

The RA3-6B2 antibody reacts with the human and mouse CD45 isoform known as CD45R, or B220, a protein tyrosine phosphatase of 220 kDa. CD45 is one of the most abundant hematopoietic markers, and is expressed on all leukocytes (the Leukocyte Common Antigen, LCA). Various isoforms are generated and expressed in cell-specific patterns, all critical for leukocyte function. In mouse, the CD45R/B220 isoform is predominantly found on B cells, at varying levels on all stages from pro-B cells to activated B cells, and may also be detected on certain T cell and NK cell subsets. It is of note that B220 is not similarly expressed on human B cells, where it appears to be differentiation-specific and therefore expressed on only some B cell subsets. Other forms of CD45 with restricted cellular expression include CD45RA, CD45RB and CD45RO.

Supplier: Bioss

C9orf96, also known as Protein kinase-like protein SgK071, is a 680 amino acid protein that belongs to the Ser/Thr protein kinase family of the protein kinase superfamily. There are three isoforms of C9orf96 that are produced as a result of alternative splicing events. The gene encoding C9orf96 maps to human chromosome 9, which consists of about 145 million bases and 4% of the human genome and encodes nearly 900 genes. Considered to play a role in gender determination, deletion of the distal portion of 9p can lead to development of male to female sex reversal, the phenotype of a female with a male X,Y genotype. Hereditary hemorrhagic telangiectasia, which is characterised by harmful vascular defects, is associated with the chromosome 9 gene encoding endoglin protein, ENG. Familial dysautonomia is also associated with chromosome 9 though through the gene IKBKAP. Notably, chromosome 9 encompasses the largest interferon family gene cluster. Chromosome 9 is partnered with chromosome 22 in the translocation leading to the aberrant production of BCR-ABL fusion protein often found in leukemias.

Supplier: Tonbo Biosciences

The M1/70 antibody reacts with human and mouse CD11b, also known as integrin alpha M. This 165-170 kDa cell surface glycoprotein is part of a family of integrin receptors that mediate adhesion between cells (cell-cell) and components of the extracellular matrix, e.g. fibrinogen (cell-matrix). In addition, integrins are active signaling receptors which recruit leukocytes to inflammatory sites and promote cell activation. Complete, functional integrin receptors consist of distinct combinations of integrin chains which are differentially expressed. Integrin alpha M (CD11b) assembles with Integrin beta-2 (CD18) into a receptor known as Macrophage Antigen-1 (Mac-1) or complement receptor type 3 (CR3). This receptor binds and induces intracellular signaling through ICAM-1 on endothelial cells and can also facilitate removal of iC3b bearing foreign cells.

Supplier: Bioss

ARRDC1, ARRDC2 (which exists as multiple alternatively spliced isoforms), ARRDC4 and ARRDC5 are arrestin domain-containing proteins that are encoded by genes which map to human chromosomes 9, 15 and 19. Chromosome 9, on which the ARRDC1 gene is localised, contains 145 million base pairs and comprises 4% of the human genome, encoding nearly 900 genes. Hereditary hemorrhagic telangiectasia, which is characterised by harmful vascular defects, and Familial dysautonomia, are both associated with chromosome 9. Notably, chromosome 9 encompasses the largest interferon family gene cluster. The ARRDC2 and ARRDC5 genes map to chromosome 19, which consists of over 63 million bases, houses approximately 1,400 genes and is recognised for having the greatest gene density of the human chromosomes. Unlike other ARRDC genes, the ARRDC4 gene maps to human chromosome 15, which houses over 700 genes and comprises nearly 3% of the human genome. Angelman syndrome, Prader-Willi syndrome, Tay-Sachs disease and Marfan syndrome are all associated with defects in chromosome 15-localised genes.

Supplier: Bioss

E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyses polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation. Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner.

Supplier: Bioss

Hypermethylated in cancer (HIC-1) was originally identified as a target of p53-induced gene expression. HIC-1 is deleted in the genetic disorder Miller-Dieker syndrome (MDS), and the expression of HIC-1 is also frequently suppressed in leukemia and various cancers due to the hypermethylation of specific DNA regions and the resulting transcriptional silencing. These and other studies indicate that HIC-1 acts as a putative tumor suppressor protein that mediates transcriptional repression. HIC-1 is ubiquitously expressed in adult tissues and its structure is defined by five Zinc fingers and an N-terminal broad complex POZ (or BTB) domain. In several BTB/POZ containing proteins, including BCL-6 and the promyelocytic leukemia Zinc-finger (PLZF) oncoprotein, this domain interacts with the SMRT/N-CoR-mSin3A HDAC complex and is directly involved in repressing and silencing gene transcription. When this domain is deleted, as with the oncogenic PLZF-RAR chimera of promyelocytic leukemias, this transcriptional repression is attenuated. Conversely, HIC-1 does not interact with components of the HDAC complex, suggesting that HIC-1-induced transcriptional repression is unassociated with the POZ/BTB domain.

Supplier: Tonbo Biosciences

The RPA-T8 antibody is specific for the 32-34 kDa alpha chain of human CD8, known as CD8a or CD8 alpha. CD8a can form a homodimer (CD8 alpha-alpha), but is more commonly expressed as a heterodimer with a second chain known as CD8b or CD8 beta. CD8 acts as a co-receptor for antigen recognition and subsequent T cell activation that is initiated upon binding of the T cell receptor (TCR) to antigen-bearing MHC Class I molecules. The cytoplasmic domains of CD8 provide binding sites for the tyrosine kinase lck, facilitating intracellular signaling events that lead to T cell activation, development, and cytotoxic effector functions. CD8+ cytotoxic T cells (CTLs) play an important role in inducing cell death of tumor cells, as well as cells infected by virus, bacteria or parasites.

Supplier: Tonbo Biosciences

The OKT3 antibody is specific for human CD3e, also known as CD3 epsilon, a 20 kDa subunit of the T cell receptor complex along with CD3 gamma and CD3 delta. These integral membrane protein chains assemble with additional chains of the T cell receptor (TCR), as well as CD3 zeta chain, to form the T cell receptor – CD3 complex. Together with co-receptors CD4 or CD8, the complex serves to recognize antigens bound to MHC molecules on antigen-presenting cells. These interactions promote T cell receptor signaling (T cell activation), inducing a number of cellular responses including proliferation, differentiation, production of cytokines or activation-induced cell death. CD3 is differentially expressed during thymocyte-to-T cell development and on all mature T cells.

Supplier: Bioss

DNA deaminase (cytidine deaminase) which acts as an inhibitor of retrovirus replication and retrotransposon mobility via deaminase-dependent and -independent mechanisms. Exhibits potent antiviral activity against vif-deficient HIV-1. After the penetration of retroviral nucleocapsids into target cells of infection and the initiation of reverse transcription, it can induce the conversion of cytosine to uracil in the minus-sense single-strand viral DNA, leading to G-to-A hypermutations in the subsequent plus-strand viral DNA. The resultant detrimental levels of mutations in the proviral genome, along with a deamination-independent mechanism that works prior to the proviral integration, together exert efficient antiretroviral effects in infected target cells. Selectively targets single-stranded DNA and does not deaminate double-stranded DNA or single-or double-stranded RNA. Exhibits antiviral activity also against simian immunodeficiency viruses (SIVs), hepatitis B virus (HBV), equine infectious anemia virus (EIAV), xenotropic MuLV-related virus (XMRV) and simian foamy virus (SFV). May inhibit the mobility of LTR and non-LTR retrotransposons.

Supplier: Bioss

Transmembrane adapter protein which associates with KLRK1 to form an activation receptor KLRK1-HCST in lymphoid and myeloid cells; this receptor plays a major role in triggering cytotoxicity against target cells expressing cell surface ligands such as MHC class I chain-related MICA and MICB, and UL16-binding proteins (ULBPs); these ligands are up-regulated by stress conditions and pathological state such as viral infection and tumor transformation. Functions as docking site for PI3-kinase PIK3R1 and GRB2. Interaction of ULBPs with KLRK1-HCST triggers calcium mobilisation and activation of the PIK3R1, MAP2K/ERK, and JAK2/STAT5 signaling pathways. Both PIK3R1 and GRB2 are required for full KLRK1-HCST-mediated activation and ultimate killing of target cells. In NK cells, KLRK1-HCST signaling directly induces cytotoxicity and enhances cytokine production initiated via DAP12/TYROBP-associated receptors. In T-cells, it provides primarily costimulation for TCR-induced signals. KLRK1-HCST receptor plays a role in immune surveillance against tumors and is required for cytolysis of tumors cells; indeed, melanoma cells that do not express KLRK1 ligands escape from immune surveillance mediated by NK cells.

Supplier: Bioss

Atypical chemokine receptor that controls chemokine levels and localisation via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalising receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalisation and activation of MAPK signaling pathway. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. Acts as coreceptor with CXCR4 for a restricted number of HIV isolates.

Supplier: Bioss

Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. The majority of Zinc-finger proteins contain a Kr_ppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. HIC-2 (hypermethylated in cancer 2) possesses Zinc finger motifs that are thought to be important for DNA-binding and also has a BTB/POZ domain at the N-terminus, which is thought to be important for protein-protein binding, as well as for the binding of transcription factors. HIC-2 is also known as Hic-3, HIC1-related gene on chromosome 22 or Zinc finger and BTB domain-containing protein 30, and is a 615 amino acid protein that is expressed as two isoforms produced by alternative splicing. HIC-2 is highly expressed in cerebellum and is localised to the nucleus in cells. HIC-2 contains a short amino acid sequence that is thought to interact with CtBP, a transcriptional repressor. The gene sequence associated with HIC-2 is thought to be a target for miRNAs (microRNAs) which are expressed in many cancers, suggesting that HIC-2 could possess tumor suppressor capabilities.

Supplier: VWR Chemicals

TriFast™ is a complete ready to use reagent for simultaneous isolation of RNA, DNA and proteins from liquid samples, tissue and cells.

Supplier: Bioss

Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Zince lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Alpha crystallins are composed of two gene products: alpha-A and alpha-B, for acidic and basic, respectively. Alpha crystallins can be induced by heat shock and are members of the small heat shock protein (sHSP also known as the HSP20) family. They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead they hold them in large soluble aggregates. Post-translational modifications decrease the ability to chaperone. These heterogeneous aggregates consist of 30 to 40 subunits; the alpha-A and alpha-B subunits have a 3:1 ratio, respectively. Two additional functions of alpha crystallins are an autokinase activity and participation in the intracellular architecture. Alpha-A and alpha-B gene products are differentially expressed; alpha-A is preferentially restricted to the lens and alpha-B is expressed widely in many tissues and organs. Elevated expression of alpha-B crystallin occurs in many neurological diseases; a missense mutation cosegregated in a family with a desmin-related myopathy.

Supplier: Bioss

Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Binds to polyubiquitin chains. Proposed to be capable to bind simultaneously to the 26S proteasome and to polyubiquitinated substrates and to deliver ubiquitinated proteins to the proteasome. May play a role in endoplasmic reticulum-associated degradation (ERAD) of misfolded glycoproteins by association with PNGase and delivering deglycosylated proteins to the proteasome. Involved in global genome nucleotide excision repair (GG-NER) by acting as component of the XPC complex. Cooperatively with CETN2 appears to stabilise XPC. May protect XPC from proteasomal degradation. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognises a wide spectrum of damaged DNA characterised by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognise and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts.