Proteins are one of the most important macromolecules in the cell, carrying out a variety of functions including catalyzing biochemical reactions, serving as structural components of cells and tissues and regulating gene expression. Because of their complex properties and broad range of responsibilities, proteins need to be isolated from other cells and tissue components for accurate characterization and application. Our protein expression and purification services help you obtain pure samples for use in downstream experiments that require the highest quality materials (e.g. structural studies, enzyme assays or protein-protein interaction studies).

In order to obtain the highest quality recombinant proteins, our protein expression laboratories employ stringent screening and optimization processes. Parallel small-scale screening in bacterial, yeast, insect and mammalian cell cultures along with an innovative purify first platform enable us to find the best constructions for each target protein. This is followed by the recombinant expression of your target in large quantities using an automated instrument from Nuclera.

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Viral vector-mediated transfection provides a solution to the challenge of delivering genes into hard-to-transfect cells for recombinant protein overexpression or knockdown applications. This technique utilizes adenoviruses, oncoviruses, or lentiviruses as delivery vehicles.

Affinity purification tags (e.g. GST, MBP) can be added during recombinant protein production to trap the resulting proteins for downstream analysis and remove impurities. Fluorescent labels can also be covalently coupled to the proteins during expression to facilitate imaging and interaction studies using biophysical techniques like optical tweezers. Molecular weight, purity and functionality of your recombinant protein can be further assessed with SDS-PAGE, Western blotting, mass spectrometry or isoelectric focusing.

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The runner in your life will thank you for this ultra-soft and stretchy pair of joggers. Designed with a built-in sweatshirt liner, they’ll keep him warm and comfortable on the trail and when he’s lounging on the couch. And they come in a wide range of colors and two inseams to suit any man’s body type.

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Anti-Annexin A4 antibody is directed against annexin IV. It is a member of the annexin family of calcium/phospholipid-binding proteins and promotes membrane fusion during exocytotic processes. It also has in vitro anticoagulant activity and inhibits phospholipase A2 activity. Its function has been implicated in the progression, invasion, migration, adhesion and drug resistance of a variety of cancer cells.

The 2F11 molecule was used to immuno-precipitate possible antigens from the lysate of zebrafish embryos at 72 hpf, at a time when 2F11 foregut labeling is robust. The precipitated proteins were separated by PAGE electrophoresis under reducing conditions, and a clear band resolving between 28 and 39 kDa was identified. This band was in-gel digested to yield small peptides, which were then subjected to tandem mass spectrometry. The peptide sequences obtained accurately matched several regions of the zebrafish Annexin A4 protein (Anxa4).

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Plasma levels of annexin A5 were measured in 175 patients with systemic lupus erythematosus, 104 of whom had antiphospholipid antibodies and 23 of whom had primary antiphospholipid syndrome. Plasma levels of annexin A5 also were measured in a large number of citrated, heparinized and unheparinized plasma and serum samples from healthy individuals.

The annexin A5 levels were significantly elevated in the groups of patients with SLE and PAPS, but not in the group of controls without SLE or PAPS. This suggests that annexin A5 is not removed from cellular surfaces in vivo by antiphospholipid antibodies, and indicates that plasma levels of this protein are regulated by other mechanisms.