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Monoclonal Antibody Immunofluorescence Immunocytochemistry Single-Stranded Rna Binding

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: Heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) is a member of the hnRNP A/B family of related RNA binding proteins that bind pre-mRNA and are involved in the processing, metabolism, and transport of nuclear pre-mRNA transcripts (1). hnRNP A1 regulates the alternative splicing of c-Src and c-H-Ras (2,3) and modifies initiation of translation of the fibroblast growth factor 2 mRNA (4). hnRNP A1 expression level is elevated in many cancers; knockdown of hnRNP A1 leads to apoptosis in various cancer cells (5). Although predominantly nuclear, hnRNP A1 is continually transported from the nucleus to the cytoplasm where it disassociates from mRNA and is rapidly re-imported into the nucleus (6,7). hnRNP A1 binds to cis-acting repressive sequences (CRS) of HIV-1 to influence HIV-1 production (8,9). HIV-1 enhances hnRNP A1 expression and promotes the relocalization of hnRNP A1 to the cytoplasm (10).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: The annexin superfamily consists of 13 calcium or calcium and phospholipid binding proteins with high biological and structural homology (1). Annexin-1 (ANXA1) is the first characterized member of the annexin family of proteins and is able to bind to cellular membranes in a calcium-dependent manner, promoting membrane fusion and endocytosis (2-4). Annexin A1 has anti-inflammatory properties and inhibits phospholipase A2 activity (5,6). Annexin A1 can accumulate on internalized vesicles after EGF-stimulated endocytosis and may be required for a late stage in inward vesiculation (7). Phosphorylation by PKC, EGFR, and Chak1 results in inhibition of annexin A1 function (8-10). Annexin A1 has also been identified as one of the 'eat-me' signals on apoptotic cells that are to be recognized and ingested by phagocytes (11). Annexin A1, as an endogenous anti-inflammatory mediator, has roles in many diverse cellular functions, such as membrane aggregation, inflammation, phagocytosis, proliferation, apoptosis, and tumorigenesis and cancer development (12-14).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Chromatin IP, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: The polycomb group (PcG) proteins contribute to the maintenance of cell identity, stem cell self-renewal, cell cycle regulation, and oncogenesis by maintaining the silenced state of genes that promote cell lineage specification, cell death, and cell-cycle arrest (1-4). PcG proteins exist in two complexes that cooperate to maintain long-term gene silencing through epigenetic chromatin modifications. The first complex, EED-EZH2, is recruited to genes by DNA-binding transcription factors and methylates histone H3 on Lys27. This histone methyl-transferase activity requires the Ezh2, Eed, and Suz12 subunits of the complex (5). Histone H3 methylation at Lys27 facilitates the recruitment of the second complex, PRC1, which ubiquitinylates histone H2A on Lys119 (6). CBX4 is a component of the PRC1 complex, which together with Ring1 strongly enhances the E3 ubiquitin ligase activity of the Ring2 catalytic subunit (7,8). CBX4 itself is a SUMO E3 ligase, and its function influences EMT, DNA damage response, tumor angiogenesis, and self-renewal (9-13).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Bovine, Hamster, Human, Monkey, Mouse, Pig, Rat, Xenopus, Zebrafish

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Western Blotting

Background: In both prokaryotic and eukaryotic cells the misfolding and aggregation of proteins during biogenesis and under conditions of cellular stress are prevented by molecular chaperones (1-3). HSP60 has primarily been known as a mitochondrial protein that is important for folding key proteins after import into the mitochondria (4). Research studies have shown that a significant amount of HSP60 is also present in the cytosol of many cells, and that it is induced by stress, inflammatory and immune responses, and autoantibodies correlated with Alzheimer's, coronary artery diseases, MS, and diabetes (5-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Nucleolin is a multi-functional protein that is one of the major components of the nucleoli (1). Nucleolin plays an essential role in various steps of ribosome biogenesis including rRNA synthesis, processing of pre-rRNA, pre-ribosomal RNA assembly, and transport of ribosomal proteins out of the nucleus (1-3). While the main function of nucleolin is ribosome biogenesis, it plays an important role in various other nuclear activities. Down regulation of nucleolin leads to increased expression of p53, defects in genome duplication, and a delay at prometaphase during mitosis leading to cell cycle arrest (4-6). In addition, nucleolin has been found in a complex with Rad51 and may participate in DNA repair by homologous recombination (7). Nucleolin binds to the catalytic subunit of the human telomerase reverse transcriptase, hTERT, and is thought to be involved in telomere maintenance (8). Nucleolin also possesses histone chaperone activity and is able to enhance the chromatin remodeling efficiency of SWItch/Sucrose Non Fermentable (SWI/SNF) and ATP-dependent chromatin-assembly factor (ACF), remove histone H2A-H2B dimers from nucleosomes, and facilitate the passage of RNA polymerase through chromatin (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Nucleolin is a multi-functional protein that is one of the major components of the nucleoli (1). Nucleolin plays an essential role in various steps of ribosome biogenesis including rRNA synthesis, processing of pre-rRNA, pre-ribosomal RNA assembly, and transport of ribosomal proteins out of the nucleus (1-3). While the main function of nucleolin is ribosome biogenesis, it plays an important role in various other nuclear activities. Down regulation of nucleolin leads to increased expression of p53, defects in genome duplication, and a delay at prometaphase during mitosis leading to cell cycle arrest (4-6). In addition, nucleolin has been found in a complex with Rad51 and may participate in DNA repair by homologous recombination (7). Nucleolin binds to the catalytic subunit of the human telomerase reverse transcriptase, hTERT, and is thought to be involved in telomere maintenance (8). Nucleolin also possesses histone chaperone activity and is able to enhance the chromatin remodeling efficiency of SWItch/Sucrose Non Fermentable (SWI/SNF) and ATP-dependent chromatin-assembly factor (ACF), remove histone H2A-H2B dimers from nucleosomes, and facilitate the passage of RNA polymerase through chromatin (9).