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Granulocyte-macrophage colony-stimulating factor (GM-CSF) promotes cell proliferation and differentiation.
Recombinant protein A binds immunoglobulins (primarily IgG) at the Fc region with high affinity. In some cases, IgM and IgA will also bind. This property provides a rapid, simple and economical method for purification and analysis of a broad-spectrum of antibodies. Fractionation of IgG subclasses can also be performed using recombinant protein A. Because of its high affinity for immunoglobulins of many species and its low level of non-specific binding, recombinant protein A is useful for the study of cell surface antigens and receptors, and for detecting antibody-secreting cells. Recombinant protein A is produced in an E. coli strain which contains the gene for mature protein A from Staphylococcus aureus Cowan I strain.
Transferrin can be used as a supplement in certain cell cultures to maintain cell survival and proliferation in serum-free or low serum conditions.
Tested negative for the presence of Hepatitis B Surface Antigen (HBsAg), HIV I/II, HIV-1Ag, HCV, ALT and Syphilis
ALBUMIN, HUMAN is recommended for use in absorption, distribution, metabolism, and excretion (ADME) pharmacological research; cell culture; drug delivery research; and cryopreservation of cells. Prepared using Cohn method IV. The material is non-reactive for HbsAg, Anti-HCV 3.0, Anti-HIV-1/2 and STS (RPR). This material is also negative for HIV-1 and HCV by PCR. Product Description Albumins are a group of simple proteins found in the body fluids and tissues of animals, and in some plant seeds. It is a single polypeptide chain with one free sulfhydryl group (Cys34) and 17 intrachain disulfide bonds. Biochem/physiol Actions Albumins are soluble monomeric proteins found in the body fluids and tissues of animals and in some plant seeds. Serum albumin functions as a carrier protein for steroids, fatty acids, and thyroid hormones. Serum albumins are also vital in regulating the colloidal osmotic pressures of blood.
This human protein is prepared by a modification of the Cohn procedure. Albumin may be used to eliminate background interference in ELISA’s or other enzyme assay systems. It is also used in absorption, distribution, metabolism, and excretion (ADME) pharmacological research; cell culture; drug delivery research; and cryopreservation of cells. Human and bovine albumins contain 16% nitrogen and are often used as standards in protein calibration studies. Due to their free hydrophobic region fatty acid free albumins are used to solubilize lipids in tissue culture, and are also used as blocking agents in Western blots or ELISA applications. Globulin free albumins are suitable for use in applications where no other proteins should be present (e.g., electrophoresis). Serum albumin functions as a carrier protein for steroids, fatty acids, and thyroid hormones, and is vital in regulating the colloidal osmotic pressures of blood. Albumin is also seen to bind to exogenous substances, particularly drugs (e.g., ibuprofen, warfarin), and strongly influence their pharmacokinetics. Oxidative stress leading to changes in the redox state of albumin has widely varied effects on its physiological function.
Albumins are a group of simple proteins found in the body fluids and tissues of animals, and in some plant seeds. It is a single polypeptide chain with one free sulfhydryl group (Cys34) and 17 intrachain disulfide bonds.
10% Solution
Prepared from Fraction V human albumin, this solution is supplied at a pH of 7.1 ±0.3 and contains 0.05% sodium azide as a preservative.
See the Immunobiologicals Section for additional details.
Wheat germ agglutinin (WGA) is one of the most widely used lectins in cell biology.
A heterodimer composed of a- and ß- tubulin of 55 kDa (molecular weight ?110 kDa).
Lyophilized affinity-purified goat antibody to mouse IgG (H + L chains). HRP conjugate.
Protein G is a monomeric protein lacking cysteine residues. Recombinant Protein G is a highly stable surface receptor that is capable of binding the Fc portion of immunoglobulins, especially IgGs from a large number of species. Preparation:Protein G is from Streptococcus sp.expressed in E. coli.
Lyophilized rabbit antibody to porcine IgM (Mu specific)
Affinity-purified goat antibody to dog IgG (whole molecule)
Lyophilized hamster IgG with buffer salts.