4 Host, 96T, apoptosis, array, Assay, Bacteria Pig Pigeon, Bafilomycin A1, Blocking, Ch 223191, Choline Acetyltransferase Antibody, Deoxycholic Acid Sodium Salt, Glycodeoxycholic Acid, GMO, Goat, Green, Guinea, Mip 1B, Pamabrom 100Mg, Pepstatin A, Phospho 4Ebp1, Tubastatin A

Copper Isotopes and Copper to Zinc Ratio as Possible Biomarkers for Thyroid Cancer

Thyroid cancer is the most common endocrine cancer. There is no systematic screening for such cancer, and the current challenge is to find potential biomarkers to facilitate an early diagnosis. Copper (Cu) and zinc (Zn) are essential micronutrients involved in the proper functioning of the thyroid gland, and changes in their concentrations have been observed in the development of cancer.
Previous studies have highlighted the potential 65Cu/63Cu ratio (δ65Cu) to be a cancer biomarker. This study tests its sensitivity on plasma samples (n = 46) of Algerian patients with papillary thyroid carcinoma and a set of corresponding biopsies (n = 11). The δ65Cu ratio in blood and tumor samples was determined using multi collector inductively coupled plasma-mass spectrometry (MC-ICP-MS), and their corresponding Cu and Zn plasma total concentrations using total reflection X-ray fluorescence (TXRF).
Plasma concentrations of Cu were significantly higher (1346.1 ± 328.3 vs. 1060.5 ± 216.1 μg/L, p < 0.0001), and Zn significantly lower (942.1 ± 205.2 vs. 1027.9 ± 151.4 μg/L, p < 0.05) in thyroid cancer patients as compared to healthy controls (n = 50). Accordingly, the Cu/Zn ratio was significantly different between patients and controls (1.5 ± 0.4 vs. 1.0 ± 0.3, p < 0.0001). Furthermore, the δ65Cu plasma levels of patients were significantly lower than healthy controls (p < 0.0001), whereas thyroid tumor tissues presented high δ65Cu values. These results support the hypothesis that Cu isotopes and plasma trace elements may serve as suitable biomarkers of thyroid cancer diagnosis.

Visualization of DNA replication in single chromosome by stable isotope labeling

Among the inheritance of cellular components during cell division, deoxyribonucleic acid (DNA) and its condensate (chromosome) are conventionally visualized using chemical tag-labeled nucleotide analogs. However, associated mutagenesis with nucleotide analogs in the visualization of chromosomes is cause for concern. This study investigated the efficiency of using stable isotope labels in visualizing the replicating cultured human cell-chromosomes, in the absence of analog labels, at a high spatial resolution of 100 nm.
The distinct carbon isotope ratio between sister chromatids reflected the semi-conservative replication of individual DNA strands through cell cycles and suggested the renewal of histone molecules in daughter chromosomes. Thus, this study provides a new, powerful approach to trace and visualize cellular components with stable-isotope labeling.Key Words: stable isotope, chromosome replication, semi-conservative replication, imaging, mass spectrometry.

A high temperature water vapor equilibration method to determine non-exchangeable hydrogen isotope ratios of sugar, starch, and cellulose

The analysis of the non-exchangeable hydrogen isotope ratio (δ2 Hne ) in carbohydrates is mostly limited to the structural component cellulose, while simple high-throughput methods for δ2 Hne values of non-structural carbohydrates (NSC) such as sugar and starch do not yet exist. Here we tested if the hot vapor equilibration method originally developed for cellulose is applicable for NSC, verified by comparison with the traditional nitration method.
We set up a detailed analytical protocol and applied the method to plant extracts of leaves from species with different photosynthetic pathways (i.e., C3 , C4 , CAM). δ2 Hne of commercial sugars and starch from different classes and sources, ranging from -157.8 to +6.4‰, were reproducibly analysed with a precision between 0.2 and 7.7‰. Mean δ2 Hne values of sugar are lowest in C3 (-92.0‰), intermediate in C4(-32.5‰), and highest in CAM plants (6.0‰), with NSC being 2 H-depleted compared to cellulose and sugar being generally more 2 H-enriched than starch.
Our results suggest that our method can be used in future studies to disentangle 2 H-fractionation processes, for improving mechanistic δ2 Hne models for leaf and tree-ring cellulose, and for further development of δ2 Hne in plant carbohydrates as a potential proxy for climate, hydrology, plant metabolism and physiology. This article is protected by copyright. All rights reserved.
isotope
isotope

Rapid analysis of S-adenosylmethionine (SAM) and S-adenosylhomocysteine (SAH) isotopologues in stable isotope-resolved metabolomics (SIRM) using direct infusion nanoelectrospray ultra-high-resolution Fourier transform mass spectrometry (DI-nESI-UHR-FTMS)

S-Adenosylmethionine (SAM) and S-adenosylhomocysteine (SAH) are important metabolites in the one-carbon cycle that modulates cellular methylation required for proliferation and epigenetic regulation. Their concentrations, synthesis, and turnover are difficult to determine conveniently and reliably. We have developed such a method by coupling a simple and rapid purification scheme that efficiently captures both compounds, with high sensitivity, sample throughput direct infusion nanoelectrospray ultra-high-resolution Fourier transform mass spectrometry (DI-nESI-UHR-FTMS). This method is compatible with Stable Isotope-Resolved Metabolomic (SIRM) analysis of numerous other metabolites.
The limits of detection for both SAM and SAH were <1 nM, and the linearity range was up to 1000 nM. The method was first illustrated for SAM/SAH analysis of mouse livers, and lung adenocarcinoma A549 cells. We then applied the method to track 13C1-CH3-Met incorporation into SAM and 13C6-glucose transformation into SAM and SAH via de novo synthesis. We further used the method to show the distinct effects on A549 and H1299 cells with treatment of anti-cancer methylseleninic acid (MSA), selenite, and selenomethionine, notably SAM depletion and increased SAM to SAH ratio by MSA, which implicates altered epigenetic regulation.

Novel nickel isolation procedure for a wide range of sample matrices without using dimethylglyoxime for isotope measurements using MC-ICP-MS

Nickel isotope ratios have traditionally been used as an important tracer in cosmochemistry, and recently, it has gained attention in geochemistry, biochemistry, and environmental sciences with the development of MC-ICP-MS. Purification of Ni before isotope measurement is mandatory for obtaining precise data, which has been commonly achieved with ion-exchange chromatography, employing dimethylglyoxime (DMG) as a chelating agent for Ni.
  1. However, it has been pointed out that the use of DMG can adversely affect the isotope measurement due to insufficient Ni recovery and mass bias during measurement caused by the remaining DMG. Ni isolation procedures without the usage of DMG were innovated, but they have disadvantages such as the necessity of complex separation methods, high Ni blank, and matrix-dependent Ni recovery.
  2. Here, we present a simple Ni isolation procedure without using DMG but with the aid of oxalic acid along with common inorganic acids, achieving near-complete recovery of Ni with low blanks [0.7 ± 0.3 ng (2SD, n = 4)] only using three ion exchange column steps.
  3. To validate our method and strengthen the Ni isotope database of reference materials, 60Ni/58Ni of 20 geological reference materials, covering wide matrix compositions, were measured by MC-ICP-MS using the double-spike method.
  4. The results have shown that high recovery of Ni, independent of the sample matrix elements was achieved (98 ± 4%) and the 60Ni/58Ni was measured with a 2SD of 0.006-0.084‰ from samples containing 100-200 ng Ni.

Recombinant Human Parathyroid hormone protein (PTH)

MBS9423157-01mg 0.1mg
EUR 610

Recombinant Human Parathyroid hormone protein (PTH)

MBS9423157-025mg 0.25mg
EUR 1035

Recombinant Human Parathyroid hormone protein (PTH)

MBS9423157-05mg 0.5mg
EUR 1320

Recombinant Human Parathyroid hormone protein (PTH)

MBS9423158-002mg 0.02mg
EUR 210

Recombinant Human Parathyroid hormone protein (PTH)

MBS9423158-01mg 0.1mg
EUR 365

Recombinant Human Parathyroid hormone protein (PTH)

MBS9423158-025mg 0.25mg
EUR 1035

Recombinant Human Parathyroid hormone protein (PTH)

MBS9423158-05mg 0.5mg
EUR 1320

Recombinant Human Parathyroid hormone protein (PTH)

MBS9423158-1mg 1mg
EUR 1775

Recombinant Human Parathyroid hormone protein (PTH)

MBS9423159-002mg 0.02mg
EUR 210

Recombinant Human Parathyroid hormone protein (PTH)

MBS9423159-01mg 0.1mg
EUR 365

Recombinant Human Parathyroid hormone protein (PTH)

MBS9423159-025mg 0.25mg
EUR 1035

Recombinant Human Parathyroid hormone protein (PTH)

MBS9423159-05mg 0.5mg
EUR 1460

Recombinant Human Parathyroid hormone protein (PTH)

MBS9423159-1mg 1mg
EUR 1775

Recombinant Human Parathyroid hormone protein (PTH)

MBS9423160-002mg 0.02mg
EUR 210

Recombinant Human Parathyroid hormone protein (PTH)

MBS9423160-01mg 0.1mg
EUR 365

Recombinant Human Parathyroid hormone protein (PTH)

MBS9423160-025mg 0.25mg
EUR 1035

Recombinant Human Parathyroid hormone protein (PTH)

MBS9423160-05mg 0.5mg
EUR 1320

Recombinant Human Parathyroid hormone protein (PTH)

MBS9423160-1mg 1mg
EUR 1775

Recombinant Human Parathyroid hormone protein(PTH) (Active)

AP73570 1mg
EUR 1968

Recombinant Human Parathyroid hormone protein(PTH) (Active)

AP73571 1mg
EUR 1968

Recombinant Human Parathyroid hormone protein(PTH) (Active)

AP73572 1mg
EUR 1968

Recombinant Human Parathyroid hormone protein (PTH) (Active)

CSB-AP000051HU 8497 mg Ask for price

Recombinant Human Parathyroid hormone protein (PTH) (Active)

MBS969120-01mg 0.1mg
EUR 530

Recombinant Human Parathyroid hormone protein (PTH) (Active)

MBS969120-05mg 0.5mg
EUR 1080

Recombinant Human Parathyroid hormone protein (PTH) (Active)

MBS969120-5x05mg 5x0.5mg
EUR 4595

Recombinant Human Parathyroid hormone protein (PTH) (Active)

MBS969121-01mg 0.1mg
EUR 530

Recombinant Human Parathyroid hormone protein (PTH) (Active)

MBS969121-05mg 0.5mg
EUR 1080

Recombinant Human Parathyroid hormone protein (PTH) (Active)

MBS969121-5x05mg 5x0.5mg
EUR 4595

Recombinant Human Parathyroid hormone protein (PTH) (Active)

MBS969123-01mg 0.1mg
EUR 530

Recombinant Human Parathyroid hormone protein (PTH) (Active)

MBS969123-05mg 0.5mg
EUR 1080

Recombinant Human Parathyroid hormone protein (PTH) (Active)

MBS969123-5x05mg 5x0.5mg
EUR 4595

Recombinant Human Parathyroid Hormone/PTH Protein (1-84)

PKSH032854-10ug 10ug
EUR 129
Description: Human

Recombinant Human Parathyroid Hormone/PTH Protein (1-84)

PKSH032854-50ug 50ug
EUR 375
Description: Human

PTH Parathyroid Hormone (7-84) Human Recombinant Protein

PROTP01270-1 Regular: 0.5mg
EUR 818.4
Description: PTH (7-84) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 76 amino acids, having an MW of 8.8kDa. ;The PTH (7-84) is purified by proprietary chromatographic techniques.

PTH Parathyroid Hormone (1-34) Human Recombinant Protein

PROTP01270-3 Regular: 0.5mg
EUR 818.4
Description: Parathyroid Hormone Human Recombinant (C181H290N55O51S2) produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 34 amino acids and having a molecular mass of 4117.8 Dalton. ;The PTH is purified by proprietary chromatographic techniques.

PTH Parathyroid Hormone (1-84) Human Recombinant Protein

PROTP01270-4 Regular: 0.5mg
EUR 818.4
Description: Parathyroid Hormone 1-84 (full length) Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 84 amino acids, having an MW of ~10kDa.;The PTH is purified by proprietary chromatographic techniques.

PTH Parathyroid Hormone (7-34) Human Recombinant Protein

PROTQ03431 Regular: 0.5mg
EUR 818.4
Description: Parathyroid Hormone Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 28 amino acids and having a molecular mass of 3380 Dalton. ;The PTH is purified by proprietary chromatographic techniques.

Recombinant Human Parathyroid hormone protein (PTH), partial (Active)

CSB-AP000021HU 8495 mg Ask for price

Recombinant Human Parathyroid hormone protein (PTH), partial (Active)

CSB-AP000031HU 8496 mg Ask for price

Recombinant Human Parathyroid Hormone (PTH)

MBS7115159-001mg 0.01mg
EUR 260

Recombinant Human Parathyroid Hormone (PTH)

MBS7115159-005mg 0.05mg
EUR 545

Recombinant Human Parathyroid Hormone (PTH)

MBS7115159-5x005mg 5x0.05mg
EUR 2250

Recombinant Human Parathyroid hormone (PTH)

MBS9018515-02mg 0.2mg
EUR 330

Recombinant Human Parathyroid hormone (PTH)

MBS9018515-05mg 0.5mg
EUR 630

Recombinant Human Parathyroid hormone (PTH)

MBS9018515-1mg 1mg
EUR 920

Recombinant Human Parathyroid hormone (PTH)

MBS9018515-5x1mg 5x1mg
EUR 4090

Recombinant Human Parathyroid Hormone/PTH Protein (His Tag)

PKSH033570-10ug 10ug
EUR 92
Description: Human

Recombinant Human Parathyroid Hormone/PTH Protein (His Tag)

PKSH033570-50ug 50ug
EUR 178
Description: Human

Recombinant Human Parathyroid Hormone/PTH Protein (N-His)

MBS2557179-001mg 0.01mg
EUR 155

Recombinant Human Parathyroid Hormone/PTH Protein (N-His)

MBS2557179-005mg 0.05mg
EUR 220

Recombinant Human Parathyroid Hormone/PTH Protein (N-His)

MBS2557179-5x005mg 5x0.05mg
EUR 980

Parathyroid Hormone/PTH Protein, Human, Recombinant (hFc Tag)

MBS8121322-01mg 0.1mg
EUR 395

Parathyroid Hormone/PTH Protein, Human, Recombinant (hFc Tag)

MBS8121322-1mg 1mg
EUR 1960

Parathyroid Hormone/PTH Protein, Human, Recombinant (hFc Tag)

MBS8121322-5x1mg 5x1mg
EUR 8665

Recombinant Human Parathyroid Hormone/Parathormone/PTH (1-84) Protein

MBS2553052-001mg 0.01mg
EUR 180

Recombinant Human Parathyroid Hormone/Parathormone/PTH (1-84) Protein

MBS2553052-005mg 0.05mg
EUR 380

Recombinant Human Parathyroid Hormone/Parathormone/PTH (1-84) Protein

MBS2553052-5x005mg 5x0.05mg
EUR 1690

Recombinant Human PTH 1-84/Parathyroid hormone/Parathormone Protein

E40KMP1621 20ug
EUR 495

Recombinant Human PTH 1-84/Parathyroid hormone/Parathormone Protein

RP00477 10 μg
EUR 219.6

Recombinant Human PTH / parathyroid hormone Protein (aa 32-65, GST tag)

MBS2545381-01mg 0.1mg
EUR 685

Recombinant Human PTH / parathyroid hormone Protein (aa 32-65, GST tag)

MBS2545381-5x01mg 5x0.1mg
EUR 3080

Recombinant Human Parathyroid hormone (PTH) (Active)

CSB-AP005621HU 8718 mg Ask for price

Parathyroid Hormone, Recombinant, Human (PTH) (1-84)

MBS637586-05mg 0.5mg
EUR 775

Parathyroid Hormone, Recombinant, Human (PTH) (1-84)

MBS637586-5x05mg 5x0.5mg
EUR 3330

Parathyroid Hormone, Recombinant, Human (PTH) (1-34)

MBS637836-01mg 0.1mg
EUR 525

Parathyroid Hormone, Recombinant, Human (PTH) (1-34)

MBS637836-05mg 0.5mg
EUR 895

Parathyroid Hormone, Recombinant, Human (PTH) (1-34)

MBS637836-5x05mg 5x0.5mg
EUR 3885

Parathyroid Hormone, Recombinant, Human (PTH) (1-84)

MBS636511-01mg 0.1mg
EUR 640

Parathyroid Hormone, Recombinant, Human (PTH) (1-84)

MBS636511-05mg 0.5mg
EUR 1060

Parathyroid Hormone, Recombinant, Human (PTH) (1-84)

MBS636511-1mg 1mg
EUR 1515

Parathyroid Hormone, Recombinant, Human (PTH) (1-84)

MBS636511-5x1mg 5x1mg
EUR 6670

Recombinant Human Parathyroid Hormone/PTH Protein (aa 32-65, GST Tag)

PKSH030707-100ug 100ug
EUR 732
Description: Human

PTH Parathyroid Hormone (1-84) N15 Labeled Human Recombinant Protein

PROTP01270 Regular: 20ug
EUR 380.4
Description: PTH (1-84) N15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 84 amino acids and having a molecular mass of 9550 Dalton labeled by the stable isotope N15.;The PTH (1-84) N15 is purified by proprietary chromatographic techniques.

PTH Parathyroid Hormone (7-84) N15 Labeled Human Recombinant Protein

PROTP01270-2 Regular: 20ug
EUR 380.4
Description: PTH (7-84) N15 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 78 amino acids and having a molecular mass of 8900 Dalton labeled by the stable isotope N15.

Recombinant Parathyroid Hormone (PTH)

RPA866Bo01 10ug
EUR 164
Andrew Green