Free Shipping on orders over 50$

British Pound Sterling - GBP Euro - EUR US Dollar - USD (EUR)

Welcom to Gentaur Biotech Products!

MOUSE ANTI RAT C_PEPTIDE

Be the first to review this product

Availability: In stock

€288.64
OR

Quick Overview

[#ABS11792] MOUSE ANTI RAT C_PEPTIDE

Details

Product Tags

Use spaces to separate tags. Use single quotes (') for phrases.

(1) Gallic acid ameliorates hyperglycemia and improves hepatic carbohydrate metabolism in rats fed a high-fructose diet.[TOP]

Pubmed ID :26547672
Publication Date : //
Herein, we investigated the hypoglycemic effect of plant gallic acid (GA) on glucose uptake in an insulin-resistant cell culture model and on hepatic carbohydrate metabolism in rats with a high-fructose diet (HFD)-induced diabetes. Our hypothesis is that GA ameliorates hyperglycemia via alleviating hepatic insulin resistance by suppressing hepatic inflammation and improves abnormal hepatic carbohydrate metabolism by suppressing hepatic gluconeogenesis and enhancing the hepatic glycogenesis and glycolysis pathways in HFD-induced diabetic rats. Gallic acid increased glucose uptake activity by 19.2% at a concentration of 6.25 μg/mL in insulin-resistant FL83B mouse hepatocytes. In HFD-induced diabetic rats, GA significantly alleviated hyperglycemia, reduced the values of the area under the curve for glucose in an oral glucose tolerance test, and reduced the scores of the homeostasis model assessment of insulin resistance index. The levels of serum C-peptide and fructosamine and cardiovascular risk index scores were also significantly decreased in HFD rats treated with GA. Moreover, GA up-regulated the expression of hepatic insulin signal transduction-related proteins, including insulin receptor, insulin receptor substrate 1, phosphatidylinositol-3 kinase, Akt/protein kinase B, and glucose transporter 2, in HFD rats. Gallic acid also down-regulated the expression of hepatic gluconeogenesis-related proteins, such as fructose-1,6-bisphosphatase, and up-regulated expression of hepatic glycogen synthase and glycolysis-related proteins, including hexokinase, phosphofructokinase, and aldolase, in HFD rats. Our findings indicate that GA has potential as a health food ingredient to prevent diabetes mellitus.

Authors : Huang Da-Wei, Chang Wen-Chang, Wu James Swi-Bea, Shih Rui-Wen, Shen Szu-Chuan,



(2) Hypotriglyceridemic and hypoglycemic effects of vescalagin from Pink wax apple [Syzygium samarangense (Blume) Merrill and Perry cv. Pink] in high-fructose diet-induced diabetic rats.[TOP]

Pubmed ID :23122137
Publication Date : //
Vescalagin, an active component from Pink wax apple [Syzygium samarangense (Blume) Merrill and Perry cv. Pink] fruit, with glucose uptake enhancing ability in insulin-resistant FL83B mouse hepatocytes, as shown in our previous study, was further evaluated for its hypotriglyceridemic and hypoglycemic effects in high-fructose diet (HFD)-induced diabetic rats. Wistar rats were fed HFD for 16 weeks and orally administered with vescalagin from Pink wax apple daily during the last 4 weeks. The results of biochemical parameters showed that fasting blood glucose, C-peptide, fructosamine, triglyceride and free fatty acid contents decreased by 44.7%, 46.2%, 4.0%, 42.5%, and 10.8%, respectively, in the HFD-induced diabetic rats administered with vescalagin at 30 mg/kg body weight in comparison with those of control HFD-induced diabetic rats. However, high-density-lipoprotein-cholesterol content increased by 14.4% in the HFD rats treated with vescalagin. The present study reveals that vescalagin could have therapeutic value against diabetic progression via its anti-hypertriglyceridemic and anti-hyperglycemic effects.

Authors : Shen Szu-Chuan, Chang Wen-Chang,



(3) Influence of insulin in the ventromedial hypothalamus on pancreatic glucagon secretion in vivo.[TOP]

Pubmed ID :20299468
Publication Date : //
Insulin released by the beta-cell is thought to act locally to regulate glucagon secretion. The possibility that insulin might also act centrally to modulate islet glucagon secretion has received little attention.

Authors : Paranjape Sachin A, Chan Owen, Zhu Wanling, Horblitt Adam M, McNay Ewan C, Cresswell James A, Bogan Jonathan S, McCrimmon Rory J, Sherwin Robert S,



(4) Islet xenograft destruction in the hu-PBL-severe combined immunodeficient (SCID) mouse necessitates anti-CD3 preactivation of human immune cells.[TOP]

Pubmed ID :10971525
Publication Date : //
Introduction of the hu-PBL-SCID mouse model has yielded a potentially useful tool for research in transplantation. The aim of this study was to define the conditions necessary for a reconstituted human immune system to destroy in a consistent manner rat islet xenografts in the alloxan-diabetic hu-PBL-SCID mouse. We examined different time points of hu-PBL reconstitution, different transplantation sites of the islets and several hu-PBL reconstitution protocols. Major differences in graft destruction were observed between the different hu-PBL reconstitution protocols, irrespective of timing of hu-PBL reconstitution or site of transplantation. Although preactivation of hu-PBL did not improve the level of hu-PBL chimerism, histological and immunohistochemical analysis of the grafts revealed a severe human lymphocytic infiltration and beta cell destruction only in the grafts of mice receiving preactivated hu-PBL. This beta cell injury resulted in impaired glucose tolerance, with in some animals recurrence of hyperglycaemia, and decreased insulin and C-peptide levels after glucose stimulation. Therefore, we conclude that activation of hu-PBL prior to transfer is essential in achieving xenograft infiltration and destruction in hu-PBL-SCID mice. The need for immune manipulation suggests that interactions between hu-PBL and xenografts in this model may be hampered by incompatibilities in cross-species adhesion and/or activation signals.

Authors : Gysemans C, Waer M, Laureys J, Depovere J, Pipeleers D, Bouillon R, Mathieu C,



(5) Characterization of a high-affinity Ins-P4 (inositol 1,3,4,5-tetrakisphosphate) receptor from brain by an anti-peptide antiserum.[TOP]

Pubmed ID :7656984
Publication Date : //
From a high-affinity Ins-P4 (inositol 1,3,4,5-P4) receptor purified from pig cerebellum, digested with the protease Lys C peptide sequences were obtained. Synthetic peptide-3 (19 amino acid residues) was used to generate an antiserum. Reaction of the affinity-purified antibodies with the purified pig receptor protein in ELISA or Western blot was completely inhibited by peptide-3. In cerebellar membranes, the antibodies clearly recognized the 42 kDa Ins-P4 receptor protein and two additional proteins (25 kDa, 37 kDa) which still have to be identified. The anti-peptide antibodies could selectively immunoprecipitate the Ins-P4 receptor protein. The antiserum was used (i) to demonstrate that in brain from different species (human, pig, beef, rat, mouse and sheep) a similar 42 kDa Ins-P4 receptor protein is contained, and (ii) to obtain indications for the existence of a related soluble form of the 42 kDa Ins-P4 receptor besides the membrane-associated receptor.

Authors : Stricker R, Kalbacher H, Lottspeich F, Reiser G,



(6) An improved method for the determination of islet amyloid polypeptide levels in plasma.[TOP]

Pubmed ID :8060096
Publication Date : //
We describe an improved method for the determination of islet amyloid polypeptide (IAPP) levels in plasma. Plasma is first extracted with acid-acetone, followed by a specific and sensitive radioimmunoassay (RIA) for IAPP using rabbit-anti-human-IAPP serum. Recovery of synthetic IAPP from plasma was 82 +/- 6% (n = 16). Standard samples, prepared in 'hormone-free' serum, were also extracted with acid-acetone. Displacement curves of serially diluted acid-acetone extracted plasma samples were parallel to the standard curve. The lower detection limit of the RIA was 2.3 +/- 0.1 fmol/sample (n = 5). Intra-assay variations for IAPP concentrations of 4, 17 and 32 pM were 16.3% (n = 10), 9.2% (n = 10) and 6.2% (n = 10); interassay variations were 35.9% (n = 14), 19.9% (n = 15) and 15.4% (n = 15), respectively. Non-stimulated IAPP levels ranged from 2.4 to 12 pM (mean 6 +/- 4 pM, n = 10) in healthy control subjects. IAPP was not detectable in type 1 (insulin-dependent) diabetic patients before and after glucagon administration. In type 2 (non-insulin-dependent) diabetic patients basal levels ranged from 2.2 to 14.5 pM and glucagon-stimulated levels ranged from 2.2 to 38.9 pM. The increase in IAPP varied from 0 to 24.4 pM. The anti-human-IAPP serum had full cross-reactivity with rat IAPP (= mouse IAPP). Transgenic mice overexpressing the human IAPP gene showed elevated plasma IAPP levels as compared to (non-transgenic) control mice. It is concluded that the method presented for the determination of IAPP in plasma is reliable and easy to perform, yielding reproducible results.(ABSTRACT TRUNCATED AT 250 WORDS)

Authors : van Hulst K L, Hackeng W H, Höppener J W, van Jaarsveld B C, Nieuwenhuis M G, Blankenstein M A, Lips C J,



(7) The characterization of radioimmunoassay for rat pancreatic polypeptide in serum.[TOP]

Pubmed ID :1585018
Publication Date : //
A radioimmunoassay for the measurement of rat pancreatic polypeptide (RPP) in serum or plasma has been developed and characterized using a new guinea-pig anti-rat-PP antibody. The assay provides a high degree of sensitivity and lacks cross-reactivity (CR less than 0.01%) to neuropeptide Y and peptide YY. It also does not interact with PPs of other species or peptide hormones namely, amylin, glucagon, human insulin, human-PP, human-proinsulin, rat C-peptide and rat insulin. The assay employs synthetic rat PP as standards from concentrations of 21-2100 pg/ml (i.e., 5-500 pM) and produces a sensitivity limit of 19 pg/ml (4.5 pM) PP at +/- 3 S.D. The intra- and interassay % coefficient of variations are 6.4% and 5.9%, respectively. The % recovery of RPP added to rat serum samples ranges from 98% to 103%. Assay of serum volumes ranging from 25 microliters to 100 microliters does not significantly alter the expected RPP level. The migration patterns of rat serum PP and that of a synthetic RPP are identical by Sephadex G-50 chromatographic analysis. The mean values of fasting and a 2 h post-feeding plasma RPP levels in normal rats are 40 +/- 2 and 80 +/- 10 pg/ml (9.5 pM and 19.0 pM), respectively. Rat-PP release during insulin induced hypoglycemia in conscious rats rises from 38 +/- 5 pg/ml to 261 +/- 34 pg/ml (9.0 to 62.1 pM, P less than 0.005) by 30 min. Additionally, the antibody used in this study cross-reacts well with mouse-PP as determined by linear serum dilution curves, thus making it useful in the measurement of murine-PP. In conclusion, we have developed and validated a sensitive and specific rat-PP assay. This assay provides a new tool for the reliable measurement of PP in physiologic studies using rat and mouse animal models.

Authors : Akpan J O, Havel P J, Parry S J, Shalwitz R A, Gingerich R L,



(8) Diffusion of C-peptide but not proinsulin from islets in frozen sections of human pancreas identified by monoclonal antibodies.[TOP]

Pubmed ID :3888205
Publication Date : //
Human proinsulin (HPI) and C-peptide (HCP) were visualized by specific monoclonal antibodies (Mab's) in the conventional indirect immunofluorescent assay for ICA (islet cell cytoplasmic antibodies) on frozen sections of human pancreas. Two different Mab's GS-9A8 (anti-HPI, mouse IgG1) and GN-ID4 (anti-HPI/HCP, rat IgG2a) showed both intense islet cell cytoplasmic staining. In contrast to the anti-HPI staining which was confined to cell bodies only the GN-ID4 Mab produced an additional extensive staining of treadlike structures radiating from the islets. Both types of staining were blocked by excess HPI. Staining of fixed islet cell tissue were identical for the two different antibodies. Double-staining experiments clearly demonstrated that HCP but not HPI may diffuse from islets in sections of frozen human pancreas. It is concluded that antibodies cross-reacting with HCP do not define (pro) insulin containing cells.

Authors : Madsen O D, Larsson L I, Lernmark A,



(9) On the nature of crossreactions observed with antibodies directed to defined epitopes.[TOP]

Pubmed ID :6193510
Publication Date : //
Antibodies directed against a synthetic peptide (src-c) containing the six carboxyl-terminal amino acids of p60src, the transforming protein of Rous sarcoma virus, recognize p60src. However, when used at sufficiently high concentrations they also react with a number of constituents of untransformed cells. These reactions can be completely inhibited by src-c peptide. Crossreactivities are to different components in cells from different species and cannot be attributed to p60c-src, the ubiquitous cellular homologue of p60src. By indirect immunofluorescence microscopy and immunochemical techniques we have identified three cytoskeletal proteins, myosin, tubulin, and vimentin, as well as an unknown intranuclear antigen, as major targets of anti-src-c antibodies in different untransformed cells. These crossreactivities probably reflect identities or similarities in the amino acid sequence of the immunogenic peptide and segments of the otherwise unrelated crossreactive proteins. These findings are discussed with respect to the interpretation of crossreactivities that are occasionally observed with anti-peptide sera and with monoclonal antibodies.

Authors : Nigg E A, Walter G, Singer S J,