Biochemistry

Gas Chromatography (GC) is an analytical technique for a wide variety of volatile and/or semi-volatile organic compounds identification and quantitation.

In the quantitative proteomics research, several MS-based methodologies for relative quantification have been introduced for comparison of different proteomes from collected biological samples.

For many proteins and peptides, disulfide bridges are prerequisite for their proper biological function.

If an exact knowledge of protein/peptide quantities is required for further applications, quantitative amino acid analysis.

Peptide de novo sequencing is the analytical process that derives a peptide’s amino acid sequence from its tandem mass spectrum (MS/MS) without the assistance of a sequence database.

The gallbladder is a hollow organ that sits just beneath the right lobe of the liver. The gallbladder cells from Creative Bioarray are isolated from human gallbladder tissue.

Bone marrow cells are the cells contained within the bone marrow. These include stromal cells, which are not directly involved in haematopoiesis, and haematopoietic stem cells.

Established by irradiation of the adherent cells in long-term bone marrow cultures derived from C3H/HeNSlc strain mice and MS-5.

In the quantitative proteomics investigate, a few MS-based approachs for relative measurement have been presented for examination of various

Peptidomics, characterized as the precise, far reaching, subjective/quantitative multiplex examination of endogenous peptides (up to ~20 kDa).

Protein phosphorylation is the most ordinarily contemplated region of post-translational adjustment.

Creative Proteomics gives Shotgun proteomics benefit in light of ID and measurement of peptides from processed proteins utilizing couple mass spectrometry.

Peptide mass fingerprinting (PMF) is an investigative method for protein distinguishing proof.

Matriptase-2 (TMPRSS6) is a type II transmembrane serine protease mainly produced by the liver.

A thermostable Alpha-L-Rhamnosidase (Naringinase, RhamA) that catalyzes the cleavage of the bond between terminal L.

Phospholipase A2 (PLA2) hydrolyzes the β-ester bond of zwitterionic glycerophospholipids.