You searched for: Antibodies

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Peroxidase Conjugated Horse IgG F(c) Fragment

Supplier: Bioss

Involved in transcriptional regulation and chromatin remodeling. Facilitates DNA replication in multiple cellular environments and is required for efficient replication of a subset of genomic loci. Binds to DNA tandem repeat sequences in both telomeres and euchromatin and in vitro binds DNA quadruplex structures. May help stabilizing G-rich regions into regular chromatin structures by remodeling G4 DNA and incorporating H3.3-containing nucleosomes. Catalytic component of the chromatin remodeling complex ATRX:DAXX which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres, and the in vitro remodeling of H3.3-containing nucleosomes. Its heterochromatin targeting is proposed to involve a combinatorial readout of histone H3 modifications (specifically methylation states of H3K9 and H3K4) and association with CBX5. Involved in maintaining telomere structural integrity in embryonic stem cells which probably implies recruitment of CBX5 to telomers. Reports on the involvement in transcriptional regulation of telomeric repeat-containing RNA (TERRA) are conflicting; according to a report, it is not sufficient to decrease chromatin condensation at telomers nor to increase expression of telomeric RNA in fibroblasts (PubMed:24500201). May be involved in telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines. Acts as negative regulator of chromatin incorporation of transcriptionally repressive histone H2AFY, particularily at telomeres and the alpha-globin cluster in erythroleukemic cells. Participates in the allele-specific gene expression at the imprinted IGF2/H19 gene locus. On the maternal allele, required for the chromatin occupancy of SMC1 and CTCTF within the H19 imprinting control region (ICR) and involved in esatblishment of histone tails modifications in the ICR. May be involved in brain development and facial morphogenesis. Binds to zinc-finger coding genes with atypical chromatin signatures and regulates its H3K9me3 levels. Forms a complex with ZNF274, TRIM28 and SETDB1 to facilitate the deposition and maintenance of H3K9me3 at the 3' exons of zinc-finger genes (PubMed:27029610).

Supplier: Thermo Scientific

Von Hippel-Lindau syndrome (VHL) is a dominantly inherited familial cancer syndrome predisposing to a variety of malignant and benign tumors. A germline mutation of VHL gene is the basis of familial inheritance of VHL syndrome. The protein is a component of the protein complex that includes elongin B, elongin C, and cullin-2, and possesses ubiquitin ligase E3 activity. This protein is involved in the ubiquitination and degradation of hypoxia-inducible-factor (HIF), which is a transcription factor that plays a central role in the regulation of gene expression by oxygen. RNA polymerase II subunit POLR2G/RPB7 is also reported to be a target of this protein.

Supplier: Thermo Scientific

PA5-16681 targets Calretinin in IHC (P) applications and shows reactivity with Human, mouse, and Rat samples. The PA5-16681 immunogen is recombinant full-length mouse calretinin protein. Calretinin is an intracellular calcium-binding protein belonging to the troponin C superfamily characterized by a structural motif described as the EF-hand domain. The immunohistochemical detection of calretinin in developing cerebellum is restricted to the later stages indicated by weak staining from week 21 of gestation, in Purkinje and basket cells and in neurons of the dentate nucleus. The intensity of staining increases as the cerebellum matures. In tumors, calretinin has been detected in mesotheliomas and some pulmonary adenocarcinomas.

Supplier: Thermo Scientific

DUSP4 is a member of the dual specificity protein phosphatase subfamily. These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues. They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which are associated with cellular proliferation and differentiation. Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli. DUSP4 inactivates ERK1, ERK2 and JNK, is expressed in a variety of tissues, and is localized in the nucleus.

Supplier: Thermo Scientific

Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and the second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. PKC eta is one of the PKC family members. This protein is most abundant in lung, less in heart and skin.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Thermo Scientific

NANOS1 is a protein that belongs to the nanos family. The C terminus contains a conserved RNA-binding domain that consists of two zinc fingers. Nanos-type zinc finger is composed of two C2HC motifs, each motif binds one molecule of zinc. It is essential for the translation repression activity of the protein. The zinc finger region of NANOS1 shares 62% identity with the zinc finger region of Drosophila Nanos. It is required for the development of germ stem cells in both the sexes. It may regulate translation of specific mRNAs by forming a complex with PUM2. A region of PUM2 that include the RNA-binding domain and 155 upstream amino acids interacted with the zinc finger domain of NANOS1. NANOS1 is expressed during meiosis in spermatocytes but is absent in late post meiotic-stage germ cells. Northern blot analysis shows its almost exclusive expression on testis. It is also expressed in fetal testis and fetal ovary. It is essential for both establishing and maintaining germline stem cells by preventing their precocious entry into oogenesis. Removing NANOS from germline stem cells or their precursors, the primordial germ cells, causes both cell types to differentiate into germline cysts.

Supplier: Thermo Scientific

The human AF9 gene is one of the most common fusion partner genes with the ALL1 gene at 11q23 (also called MLL), resulting in the t(9;11)(p22;q23). The AF9 gene is more than 100 kb, and 2 patient breakpoint cluster regions (BCRs) have been identified; BCR1 is within intron 4, previously called site A, whereas BCR2 or site B spans introns 7 and 8. Several different structural elements have been identified in AF9, including a colocalizing in vivo DNA topo II cleavage site and an in vitro DNase I hypersensitive (DNase 1 HS) site in intron 7 in BCR2. Reversibility experiments demonstrated a religation of the topo II cleavage sites. In addition, 2 scaffold associated regions (SARs) are located centromeric to the topo II and DNase I HS cleavage sites and border breakpoint regions in 2 leukemic cells lines: SAR1 is located in intron 4, whereas SAR2 encompasses parts of exons 5-7. The patient breakpoint regions of AF9 share the same structural elements as the MLL BCR. A DNA breakage and repair model for nonhomologous recombination between MLL and its partner genes, particularly AF9, has been proposed.

Supplier: Thermo Scientific

Peroxisome proliferators are non-genotoxic carcinogens which are purported to exert their effect on cells through their interaction with members of the nuclear hormone receptor family termed peroxisome proliferator activated receptors (PPAR’s). Nuclear hormone receptors are ligand-dependent intracellular proteins that stimulate transcription of specific genes by binding to specific DNA sequences following activation by the appropriate ligand. Studies indicate that PPAR’s are activated by peroxisome proliferators such as clofibric acid, nafenopin, and WY- 14,643, as well as by some fatty acids. It has also been shown that PPAR’s can induce transcription of acyl coenzyme A oxidase & cytochrome P450 (CYP450) A6 through interaction with specific response elements. The PPAR gamma 2 isoform appears to be induced very early in the differentiation of several cultured adipocyte cell lines, and has been suggested to be a dominant regulator of the murine P2 (aP2) gene which encodes an intracellular lipid binding protein which is expressed only in adipose cells. PPAR gamma 2, like several other nuclear hormone receptors, heterodimerizes with RXR alpha.

Supplier: Bioss

Plays a key role in the control of the eukaryotic cell cycle by modulating the centrosome cycle as well as mitotic onset; promotes G2-M transition, and regulates G1 progress and G1-S transition via association with multiple interphase cyclins. Required in higher cells for entry into S-phase and mitosis. Phosphorylates PARVA/actopaxin, APC, AMPH, APC, BARD1, Bcl-xL/BCL2L1, BRCA2, CALD1, CASP8, CDC7, CDC20, CDC25A, CDC25C, CC2D1A, CSNK2 proteins/CKII, FZR1/CDH1, CDK7, CEBPB, CHAMP1, DMD/dystrophin, EEF1 proteins/EF-1, EZH2, KIF11/EG5, EGFR, FANCG, FOS, GFAP, GOLGA2/GM130, GRASP1, UBE2A/hHR6A, HIST1H1 proteins/histone H1, HMGA1, HIVEP3/KRC, LMNA, LMNB, LMNC, LBR, LATS1, MAP1B, MAP4, MARCKS, MCM2, MCM4, MKLP1, MYB, NEFH, NFIC, NPC/nuclear pore complex, PITPNM1/NIR2, NPM1, NCL, NUCKS1, NPM1/numatrin, ORC1, PRKAR2A, EEF1E1/p18, EIF3F/p47, p53/TP53, NONO/p54NRB, PAPOLA, PLEC/plectin, RB1, UL40/R2, RAB4A, RAP1GAP, RCC1, RPS6KB1/S6K1, KHDRBS1/SAM68, ESPL1, SKI, BIRC5/survivin, STIP1, TEX14, beta-tubulins, MAPT/TAU, NEDD1, VIM/vimentin, TK1, FOXO1, RUNX1/AML1, SIRT2 and RUNX2. CDK1/CDC2-cyclin-B controls pronuclear union in interphase fertilized eggs. Essential for early stages of embryonic development. During G2 and early mitosis, CDC25A/B/C-mediated dephosphorylation activates CDK1/cyclin complexes which phosphorylate several substrates that trigger at least centrosome separation, Golgi dynamics, nuclear envelope breakdown and chromosome condensation. Once chromosomes are condensed and aligned at the metaphase plate, CDK1 activity is switched off by WEE1- and PKMYT1-mediated phosphorylation to allow sister chromatid separation, chromosome decondensation, reformation of the nuclear envelope and cytokinesis. Inactivated by PKR/EIF2AK2- and WEE1-mediated phosphorylation upon DNA damage to stop cell cycle and genome replication at the G2 checkpoint thus facilitating DNA repair.

Supplier: Genetex

Tau proteins are microtubule-associated proteins that are abundant in neurons in the central nervous system and are less common elsewhere. They were discovered in 1975 in Marc Kirschner's laboratory at Princeton University. Tau proteins interact with tubulin to stabilize microtubules and promote tubulin assembly into microtubules. Tau has two ways of controlling microtubule stability: isoforms and phosphorylation. Six tau isoforms exist in brain tissue, and they are distinguished by their number of binding domains. Three isoforms have three binding domains and the other three have four binding domains. The binding domains are located in the carboxy-terminus of the protein and are positively-charged (allowing it to bind to the negatively-charged microtubule). The isoforms with four binding domains are better at stabilizing microtubules than those with three binding domains. The isoforms are a result of alternative splicing in exons 2,3, and 10 of the tau gene. Phosphorylation of tau is regulated by a host of kinases. For example, PKN, a serine/threonine kinase. When PKN is activated, it phosphorylates tau, resulting in disruption of microtubule organization. Hyperphosphorylation of the tau protein (tau inclusions), however, can result in the self-assembly of tangles of paired helical filaments and straight filaments, which are involved in the pathogenesis of Alzheimer's disease and other tauopathies. Tau protein is a highly soluble microtubule-associated protein (MAP). In humans, these proteins are mostly found in neurons compared to non-neuronal cells. One of tau's main functions is to modulate the stability of axonal microtubules. Tau is not present in dendrites and is active primarily in the distal portions of axons where it provides microtubule stabilization but also flexibility as needed. This contrasts with STOP proteins in the proximal portions of axons which essentially lock down the microtubules and MAP2 that stabilizes microtubules in dendrites. The tau gene locates on chromosome 17q21, containing 16 exons. The major tau protein in the human brain is encoded by 11 exons. Exon 2, 3 and 10 are alternative spliced, allowing six combinations (2-3-10-; 2+3-10-; 2+3+10-; 2-3-10+; 2+3-10+; 2+3+10+). Thus, in the human brain, the tau proteins constitute a family of six isoforms with the range from 352-441 amino acids. They differ in either no, one or two inserts of 29 amino acids at the N-terminal part (exon 2 and 3), and three or four repeat-regions at the C-terminal part exon 10 missing. So, the longest isoform in the CNS has four repeats (R1, R2, R3 and R4) and two inserts (441 amino acids total), while the shortest isoform has three repeats (R1, R3 and R4) and no insert (352 amino acids total). All of the six tau isoforms are present in an often hyperphosphorylated state in paired helical filaments from Alzheimer's Disease brain. In other neurodegenerative diseases, the deposition of aggregates enriched in certain tau isoforms has been reported. When misfolded this otherwise very soluble protein can form extremely insoluble aggregates that contribute to a number of neurodegenerative diseases.

Supplier: Thermo Scientific

ABL1 is a cytoplasmic and nuclear protein tyrosine kinase that has been implicated in processes of cell differentiation, cell division, cell adhesion, and stress response. Activity of c-Abl protein is negatively regulated by its SH3 domain, and deletion of the SH3 domain turns ABL1 into an oncogene. The t(9;22) translocation results in the head-to-tail fusion of the BCR and ABL1 genes present in many cases of chronic myelogeneous leukemia. The DNA-binding activity of the ubiquitously expressed ABL1 tyrosine kinase is regulated by CDC2-mediated phosphorylation, suggesting a cell cycle function for ABL1.

Supplier: Rockland Immunochemical

Fluorescein Conjugated Rat IgG F(ab')2 Fragment

Supplier: Rockland Immunochemical

Peroxidase Conjugated Sheep IgG F(ab')2 Fragment

Supplier: Rockland Immunochemical

Polyclonal AntibodyHost: Goat, Species: Lactococcus lacti, Immunogen: Beta Phosphoglucomutase [Lactococcus lacti], Concentration: by UV absorbance at 280 nm, Application: ELISA, Western Blot

Supplier: Thermo Scientific

Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role in cells. PKC beta is one of the PKC family members. This protein kinase has been reported to be involved in many different cellular functions, such as B cell activation, apoptosis induction, endothelial cell proliferation, and intestinal sugar absorption. Studies in mice also suggest that this kinase may also regulate neuronal functions and correlate fear-induced conflict behavior after stress. Alternatively spliced transcript variants encoding distinct isoforms have been reported. Isoform 1 uses an alternate exon at the 3' end compared to isoform 2, which includes a part of the coding region. The resulting isoform 1 has a distinct and shorter C-terminus, as compared to isoform 2.

Supplier: Bioss

Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1 and histone H3 at 'Ser-10', which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the preinitiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4).

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.

Supplier: Rockland Immunochemical

Produced through a multi-stage process that includes delipidation, salt fractionation, ion-exchange chromatography, gel filtration, and affinity chromatography. No contaminating proteins are observed when assayed at a protein concentration of 20mg/mL against anti-whole serum or anti-fragment specific antisera. All immunoglobulin fragments are prepared from highly purified, whole molecules subject to enzymatic digestion.