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Monoclonal Antibody Immunohistochemistry Paraffin Response to Testosterone Stimulus

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

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: p70 S6 kinase is a mitogen activated Ser/Thr protein kinase that is required for cell growth and G1 cell cycle progression (1,2). p70 S6 kinase phosphorylates the S6 protein of the 40S ribosomal subunit and is involved in translational control of 5' oligopyrimidine tract mRNAs (1). A second isoform, p85 S6 kinase, is derived from the same gene and is identical to p70 S6 kinase except for 23 extra residues at the amino terminus, which encode a nuclear localizing signal (1). Both isoforms lie on a mitogen activated signaling pathway downstream of phosphoinositide-3 kinase (PI-3K) and the target of rapamycin, FRAP/mTOR, a pathway distinct from the Ras/MAP kinase cascade (1). The activity of p70 S6 kinase is controlled by multiple phosphorylation events located within the catalytic, linker and pseudosubstrate domains (1). Phosphorylation of Thr229 in the catalytic domain and Thr389 in the linker domain are most critical for kinase function (1). Phosphorylation of Thr389, however, most closely correlates with p70 kinase activity in vivo (3). Prior phosphorylation of Thr389 is required for the action of phosphoinositide 3-dependent protein kinase 1 (PDK1) on Thr229 (4,5). Phosphorylation of this site is stimulated by growth factors such as insulin, EGF and FGF, as well as by serum and some G-protein-coupled receptor ligands, and is blocked by wortmannin, LY294002 (PI-3K inhibitor) and rapamycin (FRAP/mTOR inhibitor) (1,6,7). Ser411, Thr421 and Ser424 lie within a Ser-Pro-rich region located in the pseudosubstrate region (1). Phosphorylation at these sites is thought to activate p70 S6 kinase via relief of pseudosubstrate suppression (1,2). Another LY294002 and rapamycin sensitive phosphorylation site, Ser371, is an in vitro substrate for mTOR and correlates well with the activity of a partially rapamycin resistant mutant p70 S6 kinase (8).

$122
20 µl
$307
100 µl
$719
300 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

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

Background: Bad is a proapoptotic member of the Bcl-2 family that promotes cell death by displacing Bax from binding to Bcl-2 and Bcl-xL (1,2). Survival factors, such as IL-3, inhibit the apoptotic activity of Bad by activating intracellular signaling pathways that result in the phosphorylation of Bad at Ser112 and Ser136 (2). Phosphorylation at these sites promotes binding of Bad to 14-3-3 proteins to prevent an association between Bad with Bcl-2 and Bcl-xL (2). Akt phosphorylates Bad at Ser136 to promote cell survival (3,4). Bad is phosphorylated at Ser112 both in vivo and in vitro by p90RSK (5,6) and mitochondria-anchored PKA (7). Phosphorylation at Ser155 in the BH3 domain by PKA plays a critical role in blocking the dimerization of Bad and Bcl-xL (8-10).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: CAD is essential for the de novo synthesis of pyrimidine nucleotides and possesses the following enzymatic activities: glutamine amidotransferase, carbamoyl-phosphate synthetase, aspartate transcarbamoylase, and dihydroorotase. Thus, the enzyme converts glutamine to uridine monophosphate, a common precursor of all pyrimidine bases, and it is necessary for nucleic acid synthesis (1). In resting cells, CAD is localized mainly in the cytoplasm where it carries out pyrimidine synthesis. As proliferating cells enter S phase, MAP Kinase (Erk1/2) phosphorlyates CAD at Thr456, resulting in CAD translocation to the nucleus. As cells exit S phase, CAD is dephosphorylated at Thr456 and phosphorylated at Ser1406 by PKA, returning the pathway to basal activity (2). Various research studies have shown increased expression of CAD in several types of cancer, prompting the development of pharmacological inhibitors such as PALA. Further studies have identified CAD as a potential predictive early marker of prostate cancer relapse (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

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

Background: HOXB13 is a member of the HOXB cluster which, along with the HOXA, HOXC, and HOXD clusters, governs embryonic patterning along the cranio-caudal axis (1,2). HOXB13 plays a key role in the development of the ventral prostate, where it is expressed highly from the embryonic stage through adulthood (3,4). Research studies have shown that both overexpression and RNA interference can inhibit the growth of prostate cancer cells. HOXB13 can function as a tumor suppressor by negatively regulating growth through repression of TCF4 and androgen receptor (AR) signaling (4,5). However, HOXB13 has also been shown to be overexpressed in more invasive prostate cancers, breast and ovarian cancers, and hepatocellular carcinomas (6-9). A common germline mutation G84E in the HOXB13 protein has recently been found to be associated with significant increased risk of prostate cancer (10). Currently, HOXB13 is being evaluated as a marker for metastatic lesions of prostate origin (11,12).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: NKX3.1 is a homeobox transcription factor that in mammals plays a defining role in embryonic prostate morphogenesis. The expression of mammalian NKX3.1 is androgen-dependent, restricted primarily to developing and mature prostate epithelium, and is frequently reduced or lost in prostate cancer (1-3). The human NKX3.1 gene is located on chromsome 8p21.2, within a region that shows loss of heterozygosity (LOH) in >50% of prostate cancer cases (2). Allelic loss at the NKX3.1 locus is also common in high grade Prostate Intraepithelial Neoplasia (PIN), thought to be a putative precursor lesion to invasive prostate adenocarcinomas, suggesting that LOH at the NKX3.1 locus is a critical early step in prostate cancer development (4). Notably, the remaining NKX3.1 allele is intact in the majority of LOH cases, leading to the suggestion that NKX3.1 functions as a haploinsufficient tumor suppressor (4-6). Due to its highly restricted expression in prostate epithelial cells, NKX3.1 has been suggested as a diagnostic marker of prostate carcinoma (7), and may have additional utility as a biomarker of metastatic lesions originating in the prostate (8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Carbonic anhydrases (CA) are a family of ancient zinc metalloenzymes found in almost all living organisms. All CA can be divided into 3 distinct classes (α, β, and γ) that evolved independently and have no significant homology in sequence and overall folding. All functional CA catalyze the reversible hydration of CO2 into HCO3- and H+ and contain a zinc atom in the active sites essential for catalysis. There are many isoforms of CA in mammals and they all belong to the α class (1,2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

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

Background: Carbonic anhydrases (CA) are a family of ancient zinc metalloenzymes found in almost all living organisms. All CA can be divided into 3 distinct classes (α, β, and γ) that evolved independently and have no significant homology in sequence and overall folding. All functional CA catalyze the reversible hydration of CO2 into HCO3- and H+ and contain a zinc atom in the active sites essential for catalysis. There are many isoforms of CA in mammals and they all belong to the α class (1,2).

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

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

Background: Cyclin-dependent kinase activity is regulated by T-loop phosphorylation (Thr172 in the case of CDK4), by the abundance of their cyclin partners, and by association with CDK inhibitors of the Cip/Kip or INK family of proteins (1). The inactive ternary complex of CDK4/cyclin D and p27 Kip1/Cip1 requires extracellular mitogenic stimuli for the release and degradation of p27, which affects progression through the restriction point and pRb-dependent entry into S-phase (2). The active complex of CDK4/cyclin D targets the retinoblastoma protein for phosphorylation, allowing the release of E2F transcription factors that activate G1/S-phase gene expression (3). In HeLa cells, upon UV irradiation, upregulation of p16 INK4A association with CDK4/cyclin D3 leads to a G2 delay, implicating CDK4/cyclin D3 activity in progression through the G2-phase of the cell cycle (4).