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Polyclonal Antibody Immunofluorescence Immunocytochemistry Single-Stranded Dna Binding

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

Application Methods: 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).

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

Application Methods: 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).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: RPA70 (HSSB, REPA1, RF-A, RP-A, p70) is a component of a heterotrimeric complex, composed of 70, 32/30 and 14 kDa subunits, collectively known as RPA. RPA is a single stranded DNA binding protein, whose DNA binding activity is believed to reside entirely in the 70 kDa subunit. The complex is required for almost all aspects of cellular DNA metabolism such as DNA replication (1-3), recombination, cell cycle and DNA damage checkpoints, and all major types of DNA repair including nucleotide excision, base excision, mismatch and double-strand break repairs (4-7). In response to genotoxic stress in eukaryotic cells, RPA has been shown to associate with the Rad9/Rad1/Hus1 (9-1-1) checkpoint complex (8). RPA is hyperphosphorylated upon DNA damage or replication stress by checkpoint kinases including ataxia telangiectasia mutated (ATM), ATM and Rad3-related (ATR), and DNA-dependent protein kinase (DNA-PK) (9-11). Phosphorylation of RPA32 occurs at serines 4, 8 and 33 (11). Hyperphosphorylation may alter RPA-DNA and RPA-protein interactions. In addition to the checkpoint partners, RPA interacts with a wide variety of protein partners, including proteins required for normal replication such as RCF, PCNA and Pol α, and also proteins involved in SV40 replication, such as DNA polymerase I and SV40 large T antigen (10,12).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: High mobility group protein B1 (HMGB1) belongs to a family of highly conserved proteins that contain HMG box domains (1,2). All three family members (HMGB1, HMGB2, and HMGB3) contain two HMG box domains and a C-terminal acidic domain. HMGB1 is a widely expressed and highly abundant protein (2). HMGB2 is widely expressed during embryonic development, but is restricted to lymphoid organs and testis in adult animals (3). HMGB3 is only expressed during embryogenesis (4). While expression varies, the biochemical properties of the different family members may be indistinguishable. The HMG box domains facilitate the binding of HMGB proteins to the minor groove of DNA, which results in local bending of the DNA double helix (1,2). HMGB proteins are recruited by and help facilitate the assembly of site-specific DNA binding proteins to their cognate binding sites in chromatin. For example, HMGB1 facilitates the binding of Hox proteins, Oct-1, p53, Rel proteins, and steroid hormone receptor proteins to their target gene promoters (1,2). In addition to their functions in the nucleus, HMGB proteins play a significant role in extracellular signaling associated with inflammation (5,6). HMGB1 is massively released into the extracellular environment during cell necrosis, but not apoptosis. Extracellular HMGB1 "alarms" the innate immune system by acting as a chemoattractant for inflammatory leukocytes, smooth muscle cells, and stem cells, functioning as an immune adjuvant for soluble and particulate antigens, and triggering activation of T cells and dendritic cells. In addition, activated monocytes, macrophages and, dendritic cells also secrete HMGB1, forming a positive feedback loop that results in the release of additional cytokines and neutrophils. Hypoxia has also been shown to cause the release of HMGB1 in the liver, and some studies suggest a role for extracellular HMGB1 in tumor homeostasis (5,6).

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

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

Background: The Y-box binding protein 1 (YB1) belongs to a family of evolutionarily conserved, multifunctional Y-box proteins that bind single-stranded DNA and RNA and function as regulators of transcription, RNA metabolism, and protein synthesis (1). YB1 binds to Y-box sequences (TAACC) found in multiple gene promoters and can positively or negatively regulate transcription. YB1 activates genes associated with proliferation and cancer, such as cyclin A, cyclin B1, matrix metalloproteinase-2 (MMP-2), and the multi-drug resistance 1 (MDR1) gene (2-4). YB1 represses genes associated with cell death, including the Fas cell death-associated receptor and the p53 tumor suppressor gene (5-7). It also interacts with the RNA-splicing factor SRp30c and stabilizes interleukin-2 (IL-2) mRNA upon induction of T lymphocytes by IL-2 (8,9). The majority of YB1 protein localizes to the cytoplasm, with a minor pool found in the nucleus; however, nuclear localization appears to be critical for its role in promoting proliferation. Nuclear translocation is cell cycle regulated, with YB1 protein accumulating in the nucleus during G1/S phase (2). In addition, nuclear translocation is induced in response to extracellular stimuli such as hyperthermia and UV irradiation, or treatment of cells with thrombin, interferons, or insulin-like growth factor (IGF-I) (2,10). Treatment of the MCF7 breast cancer cell line with IGF-I results in Akt-mediated phosphorylation of YB1 at Ser102, which is required for nuclear translocation of YB1 and its ability to promote anchorage-independent growth (10). Research studies have shown that YB1 is overexpressed in many malignant tissues, including breast cancer, non-small cell lung carcinoma, ovarian adenocarcinomas, human osteosarcomas, colorectal carcinomas, and malignant melanomas. Investigators have shown that nuclear YB1 expression correlates with high levels of proliferation, drug resistance, and poor tumor prognosis (2,7,10).

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

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

Background: Heterogeneous nuclear ribonucleoprotein K (hnRNP K) belongs to a family of RNA binding multiprotein complexes (hnRNP proteins) that facilitate pre-mRNA processing and transport of mRNA from the nucleus to cytoplasm (1-3). hnRNP K contains three unique structural motifs termed KH domains that bind poly(C) DNA and RNA sequences (4,5). Intricate architecture enables hnRNP K to facilitate mRNA biosynthesis (6), transcriptional regulation (7), and signal transduction. Research studies have shown that cytoplasmic hnRNP K expression is increased in oral squamous cell carcinoma and pancreatic cancer, and may be a potential prognostic factor (8,9). hnRNP K coordinates with p53 to regulate its target gene transcription in response to DNA damage. Proteasome degradation of hnRNP K is mediated by E3 ligase MDM2 (10). The interaction between hnRNP K and c-Src leads to hnRNP K phosphorylation, which allows for hnRNP K activation of silenced mRNA translation (11).

$260
100 µl
APPLICATIONS
REACTIVITY
D. melanogaster, Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), 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
D. melanogaster, Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), 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).