AKT 1/2/3 Total ELISA Kit

Name: AKT 1/2/3 Total ELISA Kit
SKU: DEIA1880
Rating: 5 (1 reviews)

Regulatory status: For research use only, not for use in diagnostic procedures.

COA

SDS

Datasheet

Summary

Sample

Cell lysates

Species Reactivity

Human; Mouse

Detection Method

sELISA

Intended Use

For the semi-quantitative measurement of AKT 1/2/3 Total in Human and mouse cell lysates.

Contents of Kit

1. AKT 1/2/3 Total Capture Antibody, 3mL, +4°C
2. AKT 1/2/3 Total Detector Antibody, 3mL, +4°C
3. Control Lysate, 1 Vial, +4°C
4. 10X Wash Buffer PT, 15 mL, +4°C
5. 5X Cell Extraction Buffer PTR, 12 mL, +4°C
6. 50X Cell Extraction Enhancer Solution, 1 mL, +4°C
7. TMB Substrate, 12 mL, +4°C
8. Stop Solution, 12 mL, +4°C
9. Pre-Coated 96 Well Microplate, (12 x 8 well strips) 96 Wells, +4°C
10. Plate Seal, 1, +4°C
Control Lysate:
Prepared from HEK293 cells, cultured to confluence in T175 flasks in 10% FBS containing medium, then treated with 20% FBS for 15min

Storage

Store kit at +4°C immediately upon receipt.
Refer to list of materials supplied for storage conditions of individual components. Observe the storage conditions for individual prepared components in the Materials Supplied section.

General Description

AKT isoforms belong to a conserved family of serine/threonine protein kinases. AKT plays a central role in cell survival and inhibiting apoptosis, by phosphorylating and inactivating several targets. AKT is activated by insulin and various other agonists, which promote transport to the plasma membrane, where the activation loop of AKT is phosphorylated at Thr308 by PDK1. The carboxy terminus is phosphorylated at Ser473 by mammalian target of rapamycin complex 2 (TORC2).
AKT substrates include Bad, forkhead transcription factors, and caspase-9. Another vital AKT function is the regulation of glycogen synthesis through phosphorylation of GSK-3. AKT phosphorylation also prevents GSK-3β mediated phosphorylation and degradation of cyclin D1, and negatively regulates the cyclin dependent kinase inhibitors p27 Kip and p21 Waf1/CIP1. AKT also plays a critical role in the regulation of TORC1 and tuberin (TSC2).

Citations

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Documents

pdf COA

pdf SDS

pdf Datasheet

QA & Reviews

Customer Reviews

References

Histopathological evaluation of minor salivary gland papillary-cystic tumours: focus on genetic alterations in sialadenoma papilliferum and intraductal papillary mucinous neoplasm

HISTOPATHOLOGY

Authors: Nakaguro, Masato; Urano, Makoto; Ogawa, Ikuko; Hirai, Hideaki; Yamamoto, Yoshinari; Yamaguchi, Hiroshi; Tanigawa, Maki; Matsubayashi, Jun; Hirano, Hiroshi; Shibahara, Junji; Tada, Yuichiro; Tsuzuki, Toyonori; Okada, Yasuo; Sato, Yuichiro; Ikeda, Kenichiro; Sukeda, Aoi; Honda, Yumi; Mikami, Yoshiki; Nagao, Toshitaka

Abstract

Aims Minor salivary gland tumours showing a predominant papillary-cystic structure are rare, and constitute a mixture of various types of neoplasm; thus, the histopathological assessment of these tumours poses a significant diagnostic challenge. We aimed to delineate the histological characteristics of these tumours and further mutational aspects with a particular focus on sialadenoma papilliferum (SP) and intraductal papillary mucinous neoplasm (IPMN). Methods and results We retrieved 28 papillary-cystic tumours of the minor salivary glands, and performed histological re-evaluation and mutation analyses of several key oncogenes. The histological classifications were as follows: SP (n = 10), SP-like intraductal papillary tumour (SP-IPT) (n = 2), IPMN (n = 9), intraductal papilloma, cystadenoma, and cystadenocarcinoma (two, three and two respectively). Whereas SP typically consisted of a combination of exophytic squamous epithelium and endophytic intraductal papillary infoldings, SP-IPT lacked the exophytic component. SP and SP-IPT frequently harboured BRAF V600E mutations (75.0%), which were identified in both squamous and ductal components. IPMN was characterised by a well-demarcated cystic lesion filled exclusively with a papillary proliferation of mucinous cells and a high rate of AKT1 E17K mutations (88.9%). Intraductal papillomas were unilocular cystic lesions with intraluminal papillary growth of bland columnar cells. In contrast, both cystadenomas and cystadenocarcinomas showed a multicystic appearance with a papillary configuration. Cystadenocarcinomas invaded the surrounding tissue and were composed of markedly atypical tumour cells. Conclusion The appropriate interpretation of histological findings and specific genetic alterations (e.g. BRAF V600E and AKT1 E17K in SP and IPMN) would be useful for the correct diagnosis of minor salivary gland papillary-cystic tumours.

Carrageenan-Free Diet Shows Improved Glucose Tolerance and Insulin Signaling in Prediabetes: A Randomized, Pilot Clinical Trial

JOURNAL OF DIABETES RESEARCH

Authors: Feferman, Leo; Bhattacharyya, Sumit; Oates, Erin; Haggerty, Nicole; Wang, Tianxiu; Varady, Krista; Tobacman, Joanne K.

Abstract

Objectives. Carrageenan is well known to cause inflammation and is used in laboratory experiments to study mediators and treatments of inflammation. However, carrageenan is added to hundreds of processed foods to improve texture. Previous work indicated that low concentrations of carrageenan in drinking water caused marked glucose intolerance and insulin resistance in a mouse model. This exploratory, clinical study tested the impact of the no-carrageenan diet in prediabetes. Research Design and Methods. Participants with prediabetes (n=13), defined as HbA1c of 5.7%-6.4%, enrolled in a 12-week, randomized, parallel-arm, feeding trial. One group (n=8) was provided all meals and snacks with no carrageenan. A second group (n=5) received a similar diet with equivalent content of protein, fat, and carbohydrate, but with carrageenan. Blood samples were collected at baseline and during oral glucose tolerance tests at 6 and 12 weeks. The primary outcome measure was changed in %HbA1c between baseline and 12 weeks. Statistical analysis included paired and unpaired t-tests, correlations, and 2x2 ANOVAs. Results. Subjects on no carrageenan had declines in HbA1c and HOMA-IR (p=0.006, p=0.026; paired t-test, two tailed). They had increases in C-peptide (p=0.029) and Matsuda Index (2.1 +/- 0.7 to 4.8 +/- 2.3; p=0.052) and declines in serum IL-8, serum galectin-3, and neutrophil phospho-(Ser307/312)-IRS1 (p=0.049, p=0.003, and p=0.006; paired t-tests, two tailed). Subjects on the diet with carrageenan had no significant changes in these parameters. Significant differences between no-carrageenan and carrageenan-containing diet groups for changes from baseline to 12 weeks occurred in C-peptide, phospho-Ser-IRS1, phospho-AKT1, and mononuclear cell arylsulfatase B (p=0.007, p=0.038, p=0.0012, and p=0.0008; 2x2 ANOVA). Significant correlations were evident between several of the variables. Conclusions. Findings indicate improvement in HbA1c and HOMA-IR in participants on no-carrageenan diets, but not in participants on carrageenan-containing diets. Significant differences between groups suggest that removing carrageenan may improve insulin signaling and glucose tolerance. Larger studies are needed to further consider the impact of carrageenan on development of diabetes.