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Rat Regulation of Virion Penetration into Host Cell

Also showing Mouse Regulation of Virion Penetration into Host Cell

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

Application Methods: Western Blotting

Background: TRIM25, also termed Estrogen-responsive Finger Protein (EFP), is a member of the tripartite motif-containing (TRIM) family of proteins, characterized by the presence of a RING domain, one or two B-box motifs, and a coiled-coil region (1). TRIM25 was first identified in a search for estrogen-responsive genes (2), and studies have subsequently shown TRIM25 to be overexpressed in many breast cancer tumors (3). A potentially oncogenic role for TRIM25 was suggested by studies showing that suppression of TRIM25 expression inhibited growth of MCF7 cells in vitro and in mouse xenograft models (4). Functional studies largely suggest that TRIM25 functions as a ubiquitin E3 or ISG15 E3 ligase. For example, TRIM25 was shown to induce K63-linked ubiquitination of Rig-I, resulting in Rig-I-mediated activation of downstream signaling cascades that drive the host antiviral innate immune response (5). Notably, it was reported that the influenza A virus non-structural protein 1 inhibits TRIM25-mediated ubiquitination of Rig-I, which may have evolved as a mechanism to evade the host innate immune response (6).

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Gelsolin (actin-depolymerizing factor, ADF, AGEL, Brevin) is an 83 kDa protein that shares structural and functional homology to villin and adseverin/scinderin (1,2). Gelsolin plays an important role in actin filament assembly by capping and severing actin proteins in a Ca2+-dependent manner (3,4). Gelsolin is important for cellular events (e.g., membrane ruffling, chemotaxis, ciliogenesis) that require cytoskeletal remodeling (3). Accordingly, cells from gelsolin knockout mice exhibit motility defects, including a failure to ruffle in response to growth factor stimulation (5,6). In humans, defects in gelsolin have been linked to amyloidosis type 5 (AMYL5), a hereditary disease characterized by cranial neuropathy, which appears to result from gelsolin amyloid deposition (7).

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

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

Background: During their synthesis, secretory proteins translocate into the endoplasmic reticulum (ER) where they are post-translationally modified and properly folded. To reach their native conformation, many secretory proteins require the formation of intra- or inter-molecular disulfide bonds (1). This process is called oxidative protein folding. Protein disulfide isomerase (PDI) catalyzes the formation and isomerization of these disulfide bonds (2). Studies on mechanisms of oxidative folding suggest that molecular oxygen oxidizes the ER-protein Ero1, which in turn oxidizes PDI through disulfide exchange (3). This event is then followed by PDI-catalyzed disulfide bond formation in folding proteins (3).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: During their synthesis, secretory proteins translocate into the endoplasmic reticulum (ER) where they are post-translationally modified and properly folded. To reach their native conformation, many secretory proteins require the formation of intra- or inter-molecular disulfide bonds (1). This process is called oxidative protein folding. Protein disulfide isomerase (PDI) catalyzes the formation and isomerization of these disulfide bonds (2). Studies on mechanisms of oxidative folding suggest that molecular oxygen oxidizes the ER-protein Ero1, which in turn oxidizes PDI through disulfide exchange (3). This event is then followed by PDI-catalyzed disulfide bond formation in folding proteins (3).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct immunofluorescent analysis in human cells. The antibody is expected to exhibit the same species cross-reactivity as the unconjugated PDI (C81H6) Rabbit mAb #3501.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry)

Background: During their synthesis, secretory proteins translocate into the endoplasmic reticulum (ER) where they are post-translationally modified and properly folded. To reach their native conformation, many secretory proteins require the formation of intra- or inter-molecular disulfide bonds (1). This process is called oxidative protein folding. Protein disulfide isomerase (PDI) catalyzes the formation and isomerization of these disulfide bonds (2). Studies on mechanisms of oxidative folding suggest that molecular oxygen oxidizes the ER-protein Ero1, which in turn oxidizes PDI through disulfide exchange (3). This event is then followed by PDI-catalyzed disulfide bond formation in folding proteins (3).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 594 fluorescent dye and tested in-house for direct immunofluorescent analysis in mouse cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated PDI (C81H6) Rabbit mAb #3501.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry)

Background: During their synthesis, secretory proteins translocate into the endoplasmic reticulum (ER) where they are post-translationally modified and properly folded. To reach their native conformation, many secretory proteins require the formation of intra- or inter-molecular disulfide bonds (1). This process is called oxidative protein folding. Protein disulfide isomerase (PDI) catalyzes the formation and isomerization of these disulfide bonds (2). Studies on mechanisms of oxidative folding suggest that molecular oxygen oxidizes the ER-protein Ero1, which in turn oxidizes PDI through disulfide exchange (3). This event is then followed by PDI-catalyzed disulfide bond formation in folding proteins (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Galectins are a family of β-galactose binding proteins that are characterized by their affinity for poly-N-acetyllactosamine-enriched glycoconjugates and their carbohydrate-binding site (1,2). Members of the galectin family have been implicated in a variety of biological functions including cell adhesion (3), growth regulation (4), cytokine production (5), T cell apoptosis (6), and immune responses (7). Galectin-1/LGALS1 has been shown to be expressed in a wide range of tissues and cell types. The level and pattern of expression of galectin-1 have been shown to change during development (8). In addition to a role in developmental processes, galectin-1 has been shown to be involved in central immune tolerance and may function in tumorigenesis by modulating the immune response to the tumor (9,10). Research studies have shown that galectin-1 expression is increased in several human cancers, suggesting a correlation with metastatic potential (10).

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

Application Methods: Immunofluorescence (Immunocytochemistry), Western Blotting

Background: Galectins are a family of β-galactose binding proteins that are characterized by their affinity for poly-N-acetyllactosamine-enriched glycoconjugates and their carbohydrate-binding site (1,2). Members of the galectin family have been implicated in a variety of biological functions including cell adhesion (3), growth regulation (4), cytokine production (5), T cell apoptosis (6), and immune responses (7). Galectin-1/LGALS1 has been shown to be expressed in a wide range of tissues and cell types. The level and pattern of expression of galectin-1 have been shown to change during development (8). In addition to a role in developmental processes, galectin-1 has been shown to be involved in central immune tolerance and may function in tumorigenesis by modulating the immune response to the tumor (9,10). Research studies have shown that galectin-1 expression is increased in several human cancers, suggesting a correlation with metastatic potential (10).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin)

Background: Galectins are a family of β-galactose binding proteins that are characterized by their affinity for poly-N-acetyllactosamine-enriched glycoconjugates and their carbohydrate-binding site (1,2). Members of the galectin family have been implicated in a variety of biological functions including cell adhesion (3), growth regulation (4), cytokine production (5), T cell apoptosis (6), and immune responses (7). Galectin-1/LGALS1 has been shown to be expressed in a wide range of tissues and cell types. The level and pattern of expression of galectin-1 have been shown to change during development (8). In addition to a role in developmental processes, galectin-1 has been shown to be involved in central immune tolerance and may function in tumorigenesis by modulating the immune response to the tumor (9,10). Research studies have shown that galectin-1 expression is increased in several human cancers, suggesting a correlation with metastatic potential (10).

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

Application Methods: Immunohistochemistry (Frozen), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Mre11, originally described in genetic screens from the yeast Saccharomyces cerevisiae in which mutants were defective in meiotic recombination (1), is a central part of a multisubunit nuclease composed of Mre11, Rad50 and Nbs1 (MRN) (2,3). The MRN complex plays a critical role in sensing, processing and repairing DNA double strand breaks. Defects lead to genomic instability, telomere shortening, aberrant meiosis and hypersensitivity to DNA damage (4). Hypomorphic mutations of Mre11 are found in ataxia-telangiectasia-like disease (ATLD), with phenotypes similar to mutations in ATM that cause ataxia-telangiectasia (A-T), including a predisposition to malignancy in humans (5). Cellular consequences of ATLD include chromosomal instability and defects in the intra-S phase and G2/M checkpoints in response to DNA damage. The MRN complex may directly activate the ATM checkpoint kinase at DNA breaks (6).