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Human Androgen Catabolic Process

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The type 6 17-β-hydroxysteroid dehydrogenase (HSD17B6, 17-β-HSD 6) regulates cellular hydroxysteroids by catalyzing the conversion of androsterone to epiandrosterone (1). This enzyme displays both oxidoreductase and epimerase activities, and is also known as 3(α->β)-hydroxysteroid epimerase. The interaction between HSD17B6 and hydroxysteroid compounds has an important effect on steroid activity as these compounds typically act in a stereo-specificity manner (1). Research studies show that the transcriptional activity of androgen receptor in prostate cell lines treated by androstanediol correlates with HSD17B6 protein level, which suggests an important role for enzyme in prostate cancer growth (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Bovine, Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Hic-5 is a LIM domain family member orginally identified as a TGFbeta1 and hydrogen peroxide inducible gene, and is nearly identical to the androgen receptor co-activator ARA55 (1-3). Hic-5 is structurally related to paxillin, and both proteins are localized to focal adhesions and thought to serve as adaptor molecules, linking signals from the extracellular matrix to cytoskeletal regulation and intracelluar signaling (4,5). Like paxillin, Hic-5 contains four LD motifs and four LIM domains. Expression of Hic-5 can affect cell growth and differentiation (6-8). Increased expression of Hic-5 is observed during cellular senescence in fibroblasts, and ectopic expression in immortalized fibroblasts suppressed cell growth (8). Unlike paxillin, Hic-5 may translocate to the nucleus in response to oxidants like hydrogen peroxide (9). It has been proposed that Hic-5 serves to shuttle redox signaling from focal adhesions to the nucleus where it acts as a transcriptional co-activator for some transciption factors including, Sp1 and PPARgamma (7,9,10). Phosphorylation of Hic-5 at Tyr60 by CAKbeta and Fyn may activiate Hic-5 signaling by allowing binding to downstream SH2 domain containing proteins (11).

$122
20 µl
$293
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: The protein inhibitor of activated Stat (PIAS) proteins, which include PIAS1, PIAS3, PIASx, and PIASy, were originally characterized based on their interaction with the Stat family of transcription factors (1,2). PIAS1, PIAS3, and PIASx interact with and repress Stat1, Stat3, and Stat4, respectively (1-3). Deletion of PIAS1 leads to inhibition of interferon-inducible genes and increased protection against infection (4). The PIAS family contains a conserved RING domain that has been linked to a function as a small ubiquitin-related modifier (SUMO) ligase, coupling the SUMO conjugating enzyme Ubc9 with its substrate proteins (5,6). Numerous studies have now shown that PIAS family members can regulate the activity of transcription factors through distinct mechanisms, including NF-κB (7,8), c-Jun, p53 (5,9), Oct-4 (10), and Smads (11,12). The activity of PIAS1 is regulated by both phosphorylation and arginine methylation. Inflammatory stimuli can induce IKK-mediated phosphorylation of PIAS1 at Ser90, which is required for its activity (13). In addition, PRMT1 induces arginine methylation of PIAS1 at Arg303 following interferon treatment and is associated with its repressive activity on Stat1 (14).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Tip60 is a member of the MYST (MOZ, YBF2, SAS2 and Tip60) family of histone acetyltransferases and plays a role in a variety of cellular processes such as transcriptional regulation, DNA repair, and apoptosis (1,2). Tip60 exists as part of a multi-subunit complex that includes proteins such as TRRAP, p400, Reptin, and Pontin (3,4). Tip60 plays important roles in double-stranded DNA break (DSB) repair. Tip60 is required for the activation of the ATM kinase in response to DSBs, as well as acetylation of histones H4 and H2A.X at DSBs to facilitate DNA repair (1,2,5-7). In addition, Tip60 dependent acetylation at Lys120 of p53 within the DNA binding domain is required for the induction of apoptosis upon DNA damage (8,9). Tip60 is involved in a number of transcriptional regulation pathways driven by factors such as nuclear receptors and β-catenin (10-13). The Tip60 complex has been shown to be important for mouse embryonic stem cell self-renewal by regulating transcription of developmental regulators that are controlled by Nanog (14). GSK3 (glycogen synthase kinase-3) mediated phosphorylation at Ser86 of Tip60 promotes Tip60 acetylation and subsequent stimulation of the required autophagy protein ULK1 (15).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Western Blotting

Background: Cytochrome P450, subfamily 3A, polypeptide 4 (CYP3A4) is a mono-oxygenase enzyme (1) found in the endoplasmic reticulum membrane of liver and prostate microsomes. It is an important enzyme in drug metabolism; it catalyzes phase I oxidation reactions in approximately 50% of drugs in the modern market, as well as steroids, fatty acids, and some carcinogens (2). It is also involved in steroid and cholesterol synthesis (3,4). Expression of CYP3A4 can be induced by glucocorticoids, carcinogens, pesticides, and drugs, which can lead to drug interactions and toxicity (5).

$348
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated PIAS1 (D33A7) XP® Rabbit mAb #3550.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry

Background: The protein inhibitor of activated Stat (PIAS) proteins, which include PIAS1, PIAS3, PIASx, and PIASy, were originally characterized based on their interaction with the Stat family of transcription factors (1,2). PIAS1, PIAS3, and PIASx interact with and repress Stat1, Stat3, and Stat4, respectively (1-3). Deletion of PIAS1 leads to inhibition of interferon-inducible genes and increased protection against infection (4). The PIAS family contains a conserved RING domain that has been linked to a function as a small ubiquitin-related modifier (SUMO) ligase, coupling the SUMO conjugating enzyme Ubc9 with its substrate proteins (5,6). Numerous studies have now shown that PIAS family members can regulate the activity of transcription factors through distinct mechanisms, including NF-κB (7,8), c-Jun, p53 (5,9), Oct-4 (10), and Smads (11,12). The activity of PIAS1 is regulated by both phosphorylation and arginine methylation. Inflammatory stimuli can induce IKK-mediated phosphorylation of PIAS1 at Ser90, which is required for its activity (13). In addition, PRMT1 induces arginine methylation of PIAS1 at Arg303 following interferon treatment and is associated with its repressive activity on Stat1 (14).

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

Application Methods: Western Blotting

Background: Hedgehog proteins (Hh) are secreted signaling proteins that play many roles during animal development. Aberrant Hh signaling activity can be associated with numerous birth defects and uncontrolled Hh pathway activation is linked to the development of several types of cancers (1-2). The three identified vertebrate Hh genes are Sonic (Shh), Indian (Ihh) and Desert (Dhh), all of which have distinct as well as overlapping roles (3-5). Hh proteins are synthesized as 45 kDa precursors that undergo auto-cleavage to generate a 19 kDa amino-terminal peptide (Hh-N) and a carboxy-terminal peptide (Hh-C). The amino-terminal peptide becomes covalently attached to a cholesterol molecule at its carboxy terminus and acetylated at its amino terminus. This doubly modified Hh-N peptide is released from cells and responsible for all known Hedgehog signaling activity (6).