381411 Results for: "single-use assemblies"

Supplier: Prosci

CD80 (B7-1) and CD86 (B7-2) together with their receptors CD28 and CTLA-4 constitute one of the dominant costimulatory pathways that regulate T cell and B cell responses. Although both CTLA-4 and CD28 can bind to the same ligands, CTLA-4 binds to B7-1 and B7-2 with a 20-100 fold higher affinity than CD28 and is involved in the down-regulation of the immune response. B7-1 is expressed on activated B cells, activated T cells, and macrophages. B7-2 is constitutively expressed on interdigitating dendritic cells, Langerhans cells, peripheral blood dendritic cells, memory B cells and germinal center B cells. Additionally, B7-2 is expressed at low levels on monocytes and can be up-regulated through interferon-gamma. B7-1 and B7-2 are both members of the immunoglobulin superfamily. It has been observed that both human and mouse B7-1 and B7-2 can bind to either human or mouse CD28 and CTLA-4, suggesting that there are conserved amino acids which form the B7-1/B7-2/CD28/CTLA-4 critical binding sites.

Supplier: Prosci

CD80 (B7-1) and CD86 (B7-2) together with their receptors CD28 and CTLA-4 constitute one of the dominant costimulatory pathways that regulate T cell and B cell responses. Although both CTLA-4 and CD28 can bind to the same ligands, CTLA-4 binds to B7-1 and B7-2 with a 20-100 fold higher affinity than CD28 and is involved in the down-regulation of the immune response. B7-1 is expressed on activated B cells, activated T cells and macrophages. B7-2 is constitutively expressed on interdigitating dendritic cells, Langerhans cells, peripheral blood dendritic cells, memory B cells, and germinal center B cells. Additionally, B7-2 is expressed at low levels on monocytes and can be up-regulated through interferon-gamma. B7-1 and B7-2 are both members of the immunoglobulin superfamily. It has been observed that both human and mouse B7-1 and B7-2 can bind to either human or mouse CD28 and CTLA-4, suggesting that there are conserved amino acids which form the B7-1/B7-2/CD28/CTLA-4 critical binding sites.

Supplier: Prosci

This gene is a target gene of the transcription factor tumor protein p53. The encoded protein is a nuclear phosphoprotein that binds and inhibits transactivation by tumor protein p53, as part of an autoregulatory negative feedback loop. Overexpression of this gene can result in excessive inactivation of tumor protein p53, diminishing its tumor suppressor function. This protein has E3 ubiquitin ligase activity, which targets tumor protein p53 for proteasomal degradation. This protein also affects the cell cycle, apoptosis, and tumorigenesis through interactions with other proteins, including retinoblastoma 1 and ribosomal protein L5. More than 40 different alternatively spliced transcript variants have been isolated from both tumor and normal tissues

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 PK136 antibody is specific for mouse NK1.1, a type II transmembrane lectin-like receptor and member of the killer cell lectin-like receptor (KLR) family. NK1.1 is prominently expressed on natural killer (NK) cells, and is correlated with NK cytotoxic effects toward virus-infected cells and tumor cells. NK1.1 is expressed on subsets of NKT cells in certain mouse strains (C57BL/6, FVB/N, and NZB), yet absent from others (AKR, BALB/c, CBA/J, C3H, DBA/1, DBA/2, NOD, SJL, and 129). Putative subsets of NK cells and their expression of NK1.1 antigen are of continuing interest, including NK1.1+/CD117+ (c-Kit) cells reported to be immunosuppressive for CD8+ T cells in a mechanism involving PD-1 and PD-L1 (Ehlers et al. 2012. Endocrinology. 10: 1247).

Supplier: Tonbo Biosciences

The PK136 antibody is specific for mouse NK1.1, a type II transmembrane lectin-like receptor and member of the killer cell lectin-like receptor (KLR) family. NK1.1 is prominently expressed on natural killer (NK) cells, and is correlated with NK cytotoxic effects toward virus-infected cells and tumor cells. NK1.1 is expressed on subsets of NKT cells in certain mouse strains (C57BL/6, FVB/N, and NZB), yet absent from others (AKR, BALB/c, CBA/J, C3H, DBA/1, DBA/2, NOD, SJL, and 129). Putative subsets of NK cells and their expression of NK1.1 antigen are of continuing interest, including NK1.1+/CD117+ (c-Kit) cells reported to be immunosuppressive for CD8+ T cells in a mechanism involving PD-1 and PD-L1 (Ehlers et al. 2012. Endocrinology. 10: 1247).

Supplier: Prosci

General protein kinase capable of phosphorylating several known proteins. Phosphorylates TBC1D4. Signals downstream of phosphatidylinositol 3-kinase (PI3K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). Plays a role in glucose transport by mediating insulin-induced translocation of the GLUT4 glucose transporter to the cell surface. Mediates the antiapoptotic effects of IGF-I. Mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. Promotes glycogen synthesis by mediating the insulin-induced activation of glycogen synthase.

Supplier: Prosci

This receptor binds insulin-like growth factor 1 (IGF1) with a high affinity and IGF2 with a lower affinity. It has a tyrosine-protein kinase activity, which is necessary for the activation of the IGF1-stimulated downstream signaling cascade. When present in a hybrid receptor with INSR, binds IGF1. Ref.19 shows that hybrid receptors composed of IGF1R and INSR isoform Long are activated with a high affinity by IGF1, with low affinity by IGF2 and not significantly activated by insulin, and that hybrid receptors composed of IGF1R and INSR isoform Short are activated by IGF1, IGF2 and insulin. In contrast, Ref.21 shows that hybrid receptors composed of IGF1R and INSR isoform Long and hybrid receptors composed of IGF1R and INSR isoform Short have similar binding characteristics, both bind IGF1 and have a low affinity for insulin.

Supplier: Prosci

Interleukin-21 (IL-21) is a key factor in the transition between innate and adaptive immune responses secreted by activated T cells. The IL-21 receptor (IL-21R) is expressed in lymphoid tissue, in particular by NK, B, T and dendritic cells, macrophages and endothelial cells. Recent evidence suggests that IL-21 plays a supportive role in the proliferation of T and B cells and influences the cytolytic activity of natural killer cells. IL-21 has been shown to up-regulate genes associated with innate immunity and to inhibit the differentiation of naive T helper cells. IL-21 specifically inhibits IFN-gamma production from developing TH1 cells and is preferentially expressed by TH2 cells. Furthermore IL-21 has been identified as a growth and survival factor for human myeloma cells. IL-21/IL-21R interactions have a unique role in sequentially activating both innate and adaptive immune responses against poorly immunogenic tumors, leading to tumor rejection that is perforin dependent but IFN-gamma independent.

Supplier: Rockland Immunochemical

NALP1 belongs to a family of cytoplasmic proteins that have been implicated in cell responses to apoptotic and inflammatory stimuli. It contains a caspase recruitment domain (CARD) in addition to a NACHT domain and leucine rich repeat (LRR). This protein interacts strongly with caspase 2 and weakly with caspase 9, as well as with Apaf-1. Transient overexpression of this gene in cultured cells was sufficient to induce apoptosis. NALP1 mRNA and protein expression levels in myeloid leukemia cells are increased following CREB (cAMP-response element binding protein) activation, suggesting that NALP1 may contribute to modulate the response of these cells to pro-inflammatory stimuli. Multiple alternatively spliced transcript variants encoding distinct isoforms have been found for NALP1.

Supplier: Rockland Immunochemical

Matrilin (MATNs) are a family of non-collagenous extracellular matrix proteins consisting of four known members that have been proposed to play key roles in the formation of both collagen-dependent and collagen-independent filamentous networks. Members of the matrilin family all share a structure made up of von Willebrand factor A domains, epidermal growth factor-like domains and a coiled coil alpha-helical module. MATN1 and MATN3 are expressed mainly in cartilage, while MATN2 and MATN4 occur in a wide variety of extracellular matrices such as embryonic kidney, lung, bone, cartilage and nervous system. The matrilin genes are strictly and differently regulated and their expression may serve as markers for cellular differentiation. MATN4 could serve as an odontoblast differentiation marker, e.g. in odontoblast stem cell research.

Supplier: Rockland Immunochemical

Glutamate receptors are the predominant excitatory neurotransmitter receptors in the mammalian brain and are activated in a variety of normal neurophysiologic processes. Grik1, also known as glutamate receptor 5, belongs to the kainate family of glutamate receptors, which are composed of four subunits and function as ligand-activated ion channels. Grik1 is expressed in GABAergic interneurons of the hippocampus and are thought to participate in the formation of various subtypes of kainate receptors with Grik2 and KA2. Stimulation of Grik1 leads to intracellular calcium release and activation of protein kinase C. Excessive activation has been associated with psychiatric, neurological and neurodegenerative diseases. Numerous isoforms of Grik1 are known to exist and may be subject to RNA editing within the second transmembrane domain, which is thought to alter the properties of ion flow.

Supplier: Rockland Immunochemical

Inhibitor of apoptosis proteins (IAPs) were initially identified in baculoviruses as proteins that inhibit apoptosis of the host cells to allow time for viral replication. Cellular homologues containing at least one baculoviral IAP repeat (BIR) motif essential for their anti-apoptosis activity have been identified in yeasts and higher organisms and often act by binding and inhibiting processed caspases. The activity of these proteins can be modulated by the expression of proteins such as Smac/DIABLO and XAF-1 which displace or prevent the binding of caspases by IAPs. Recently, a mitochondrial serine protease termed Omi/HtrA2 has been found to bind IAPs. Similar to Smac, Omi possesses a conserved IAP-binding motif, but acts to cleave IAPs to irreversibly inactivate IAPs and promote apoptosis.

Supplier: Rockland Immunochemical

Interleukin 15 (IL-15) is a cytokine that regulates T and natural killer cell activation and proliferation. This cytokine and IL-2 share many biological activities as both have been found to bind common hematopoietin receptor subunits, and may compete for the same receptor, and thus negatively regulate each other's activity. The number of CD8+ memory cells is shown to be controlled by a balance between IL-15 and IL-2. This cytokine induces the activation of JAK kinases, as well as the phosphorylation and activation of transcription activators STAT3, STAT5, and STAT6. In mouse, studies suggest that IL-15 may increase the expression of apoptosis inhibitor Bcl-xL, possibly through the transcription activation activity of STAT6, and thus prevent apoptosis.

Supplier: Rockland Immunochemical

Apoptosis is related to many diseases and development. The p53 tumor-suppressor protein induces apoptosis through transcriptional activation of several genes. A novel p53 inducible pro-apoptotic gene was identified recently and designated PUMA (for p53 upregulated modulator of apoptosis) and bbc3 (for Bcl-2 binding component 3) in human and mouse. PUMA/bbc3 is one of the pro-apoptotic Bcl-2 family members including Bax and Noxa, which are also transcriptional targets of p53. The PUMA gene encodes two BH3 domain-containing proteins termed PUMA-alpha and PUMA-beta. PUMA proteins bind Bcl-2, localize to the mitochondria, and induce cytochrome c release and apoptosis in response to p53. PUMA may be a direct mediator of p53-induced apoptosis.

Supplier: Prosci

This cytokeratin 18 antibody reacts with a wide variety of simple epithelia. It does not react with stratified squamous epithelia. It reacts with epithelial tumors of the gastrointestinal tract, lung, breast, pancreas, ovary, and thyroid. Cytokeratin 18, which belongs to the type A (acidic) subfamily of low molecular weight keratins, exists in combination with cytokeratin 8. It is reported that tissues from gastrointestinal tract are positive for both cytokeratin 18 and 8 but do not contain cytokeratin 14. Tissues from gastrointestinal tract, respiratory tract and urogenital tract, as well as endocrine and exocrine tissues and mesothelial cells are positive for cytokeratin 18.

Supplier: Rockland Immunochemical

HAAO (3-Hydroxyanthranilate 3, 4-dioxygenase) is a monomeric cytosolic protein of the family of intramolecular dioxygenases containing non-heme ferrous iron. It is widely distributed in peripheral organs, such as liver and kidney, and is present in low amounts in the central nervous system. This enzyme participates in tryptophan metabolism. It employs one cofactor, iron. HAAO catalyzes the synthesis of quinolinic acid (QUIN) from 3-hydroxyanthranilic acid. QUIN is an excitotoxin whose toxicity is mediated by its ability to activate glutamate N-methyl-D-aspartate receptors. Increased cerebral levels of QUIN may participate in the pathogenesis of neurological and inflammatory disorders. HAAO has been suggested to play a role in disorders associated with altered tissue levels of QUIN. Furthermore, recent study shows that HAAO are excellent candidate biomarkers for detecting ovarian cancer.

Supplier: CHI Scientific

The PrimaCell™ system has been developed for the acquisition and growth of primary cells from a variety of different tissue types. Each PrimaCell™ kit has been optimized for each cell type to produce 4-7 times the number of primary cells obtained from published literature protocols. Each kit comes with 100 ml of tissue washing medium, our optimized tissue dissociation system OptiTDS™, 500 ml of growth medium, and enough growth supplements and serum to add to the supplied medium. Kits that require a Fibroblast control system also come with our FibrOut™ kit (added to the growth medium) which reduces or eliminates Fibroblast growth after 2-3 cell growth cycles.

Supplier: Rockland Immunochemical

TRIM5 is a member of a broad family of otherwise unrelated proteins defined by the presence of a tripartite motif containing a RING domain, a B-box type 1, and a B-box type 2, followed by a coiled-coil region. TRIM5 has six alternately spliced isoforms, the longest of which is the alpha variant which also contains a carboxy-terminal B30.2 (SPRY) domain. Expression of TRIM5a variants from humans, rhesus monkeys, and African green monkeys enabled resistance to infection by various retroviruses including HIV-1, albeit at differing efficiencies. All TRIM5a variants could inhibit at least two different retroviruses, but not from those viruses isolated from the same species, suggesting that TRIM5a acts as a natural barrier to cross-species retrovirus transmission.

Supplier: Biosensis

Glutathione peroxidase 1 has a role in detoxification of hydrogen peroxide and is one of the most important antioxidant enzymes in humans. It exists as a homotetramer which localises to the cytoplasm. It belongs to the glutathione peroxidase family. Glutathione peroxidase 1 is one of few proteins in higher vertebrates to contain selenocysteine, which occurs at the active site of glutathione peroxidase and is coded by UGA, that normally functions as a translation termination codon. This protein has a polyalanine sequence polymorphism in the N-terminal region, which includes three alleles with five, six or seven alanine repeats. The allele with five alanine repeats is significantly associated with breast cancer risk. Two alternatively spliced isoforms have been identified.

Supplier: Tonbo Biosciences

The 53-6.7 antibody reacts with the 32-34 kDa alpha subunit of mouse 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 in 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 53-6.7 antibody reacts with the 32-34 kDa alpha subunit of mouse 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 in 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 53-6.7 antibody reacts with the 32-34 kDa alpha subunit of mouse 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 in 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: Prosci

NXF1 is one member of a family of nuclear RNA export factor. Common domain features of this family are a noncanonical RNP-type RNA-binding domain (RBD), 4 leucine-rich repeats (LRRs), a nuclear transport factor 2 (NTF2)-like domain that allows heterodimerization with NTF2-related export protein-1 (NXT1), and a ubiquitin-associated domain that mediates interactions with nucleoporins. The LRRs and NTF2-like domains are required for export activity. NXF1 shuttles between the nucleus and the cytoplasm and binds in vivo to poly (A)+ RNA. NXF1 overcomes the mRNA export block caused by the presence of saturating amounts of CTE (constitutive transport element) RNA of type D retroviruses.This gene is one member of a family of nuclear RNA export factor genes. Common domain features of this family are a noncanonical RNP-type RNA-binding domain (RBD), 4 leucine-rich repeats (LRRs), a nuclear transport factor 2 (NTF2)-like domain that allows heterodimerization with NTF2-related export protein-1 (NXT1), and a ubiquitin-associated domain that mediates interactions with nucleoporins. The LRRs and NTF2-like domains are required for export activity. Alternative splicing seems to be a common mechanism in this gene family. The encoded protein of this gene shuttles between the nucleus and the cytoplasm and binds in vivo to poly (A)+ RNA. It is the vertebrate homologue of the yeast protein Mex67p. The encoded protein overcomes the mRNA export block caused by the presence of saturating amounts of CTE (constitutive transport element) RNA of type D retroviruses.This gene is one member of a family of nuclear RNA export factor genes. Common domain features of this family are a noncanonical RNP-type RNA-binding domain (RBD), 4 leucine-rich repeats (LRRs), a nuclear transport factor 2 (NTF2)-like domain that allows heterodimerization with NTF2-related export protein-1 (NXT1), and a ubiquitin-associated domain that mediates interactions with nucleoporins. The LRRs and NTF2-like domains are required for export activity. Alternative splicing seems to be a common mechanism in this gene family. The encoded protein of this gene shuttles between the nucleus and the cytoplasm and binds in vivo to poly (A)+ RNA. It is the vertebrate homologue of the yeast protein Mex67p. The encoded protein overcomes the mRNA export block caused by the presence of saturating amounts of CTE (constitutive transport element) RNA of type D retroviruses.

Supplier: Prosci

The tetraspanins are integral membrane proteins expressed on cell surface and granular membranes of hematopoietic cells and are components of multi-molecular complexes with specific integrins. The tetraspanin CD63 is a lysosomal membrane glycoprotein that translocates to the plasma membrane after platelet activation. CD63 is expressed on activated platelets, monocytes and macrophages, and is weakly expressed on granulocytes, T cell and B cells. It is located on the basophilic granule membranes and on the plasma membranes of lymphocytes and granulocytes. CD63 is a member of the TM4 superfamily of leukocyte glycoproteins that includes CD9, CD37 and CD53, which contain four transmembrane regions. CD63 may play a role in phagocytic and intracellular lysosome-phagosome fusion events. CD63 deficiency is associated with Hermansky-Pudlak syndrome and is strongly expressed during the early stages of melanoma progression.

Supplier: GILSON, INC.

PIPETMAX is an automated pipetting solution for the efficient processing of high-throughput biological assays. It will help you to improve on the accuracy, reproducibility, and consistency among all samples processed. Unlike traditional automation platforms, PIPETMAX comes in a benchtop size that easily fits into any laboratory.

Supplier: Rockland Immunochemical

PTPRF or leukocyte common antigen-related protein (LAR) is a widely expressed protein tyrosine phosphatase with an extracellular receptor region that resembles a cell adhesion molecule. PTPRF removes phosphate group from β-catenin, an event that may subsequently facilitate cell-cell adhesion and ensure the stability of the cadherin complex. This phosphatase has also been implicated in various cellular processes such as neurite growth, nerve regeneration, actin remodeling and regulation of insulin function (1,2,3,4). Anti-PTPRF (C-terminal) antibody is specific for the extracellular and cytoplasmic subunits of human PTPRF (approx. 210, 150 and 85 kDa). Detection of the PTPRF bands by immunoblotting is specifically inhibited by the immunizing peptide. Anti-PTPRF is ideal for researchers interested in Cell adhesion Cadherin-mediated cell adhesion pathways, PAK pathways, insulin resistance and ureterocele.

Supplier: Prosci

CD63 functions as cell surface receptor for TIMP1 and plays a role in the activation of cellular signaling cascades. Plays a role in the activation of ITGB1 and integrin signaling, leading to the activation of AKT, FAK/PTK2 and MAP kinases. Promotes cell survival, reorganization of the actin cytoskeleton, cell adhesion, spreading and migration, via its role in the activation of AKT and FAK/PTK2. Plays a role in VEGFA signaling via its role in regulating the internalization of KDR/VEGFR2. Plays a role in intracellular vesicular transport processes, and is required for normal trafficking of the PMEL luminal domain that is essential for the development and maturation of melanocytes. Plays a role in the adhesion of leukocytes onto endothelial cells via its role in the regulation of SELP trafficking. May play a role in mast cell degranulation in response to Ms4a2/FceRI stimulation, but not in mast cell degranulation in response to other stimuli. [UniProt]

Supplier: Rockland Immunochemical

Ubiquitin-conjugating enzyme E2 (UEV1) was initially discovered as a protein similar in sequence and structure to the E2 ubiquitin-conjugating enzymes but lacking their enzymatic activity. There are at least two variants and multiple isoforms of UEV1. In particular, UEV1A (Ubiquitin-conjugating enzyme E2 variant 1 isoform A) has recently been shown to be an important component of the Toll-like receptor and IL-1R signaling pathway. Signals from these pathways are relayed by a number of downstream molecules such as MyD88 and tumor necrosis factor receptor associated factor (TRAF6), ultimately activating various kinases and transcription factors. UEV1A is part of a dimeric ubiquitin-conjugating enzyme complex also containing Ubc13 (ubiquitin-conjugating enzyme 13) that together with TRAF6 activates TAK1, a member of the mitogen-activated protein kinase kinase kinase family. The Ubc13-UEV1A complex also mediates the Lys-63 ubiquitination of TRAF-6, and this ubiquitination is essential for TAK1 activation.

Supplier: Rockland Immunochemical

Histone H3 is one of the five main histone proteins involved in the structure of chromatin in eukaryotic cells. Histone proteins are highly post-translationally modified with Histone H3 being the most extensively modified of the five histones. The N-terminal tail of histone H3 protrudes from the globular nucleosome core and can undergo several different types of post-translational modification that influence cellular processes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Histone H3 Antibody is ideal for investigators involved in Cell Signaling, Epigenetics, Nuclear Signaling research and Signal Transduction research.