You searched for: Proteins and Peptides

Supplier: MP Biomedicals

Below 35 to 40 °C gelatin swells and absorbs approximately 5 to 10 times its weight of water to form a gel. Gelatin is soluble in glycerol and acetic acid, and more soluble in hot than in cold water. It is practically insoluble in most organic solvents such as alcohol, chloroform, carbon disulphide, carbon tetrachloride, ether, benzene, acetone and oils. Sterile solutions of gelatin stored cold are stable indefinitely, but at elevated temperatures hydrolysis or rupture of peptide bonds occurs, increasing the number of free amino groups. Gel strength and viscosity gradually weaken upon prolonged heating in solution above ~40 °C; this degradation is accelerated by extremes in pH, proteolytic enzymes and bacterial action.

Supplier: MP Biomedicals

Cytochrome C is an electron-carrying mitochondrial protein. The transition of Cytochrome C between the ferrous and ferric states within the cell makes it an efficient biological electron-transporter and it plays a vital role in cellular oxidations in both plants and animals. It is generally regarded as a universal catalyst of respiration, forming an essential electron-bridge between the respirable substrates and oxygen.

Supplier: MP Biomedicals

MP offers this grade of albumin as a more highly purified product than our traditional True Cohn Fraction V Powder. This grade of albumin also varies in its fatty acids content (1 to 2 mg/gm). Due to lower manufacturing costs, this grade is available at a substantial savings relative to our True Cohn Fraction V Powder.

Supplier: MP Biomedicals

Agglutinin is isolated from wheat germ and purified by affinity chromatography.

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Soluble in water(25 mg/ml).

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Actin is a purified protein from Rabbit muscle, for use as a high molecular weight marker or as a standard.

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Streptavidin effectively binds to biotin with an isoelectric point close to neutral and it contains no carbohydrate residues.

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Soluble in acetic acid 80% (50 mg/ml - clear colourless solution)

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Casein from bovine milk is a phosphoprotein. It make up approximately 80% of the total protein in bovine milk. It is proposed to be the main protective constituent in milk.

Supplier: MP Biomedicals

AlbumiNZ™ Protease-reduced BSA is useful for immunoassays where proteases may degrade proteins or where peroxidase or alkaline phospahatase may hydrolyse substrates.

Supplier: MP Biomedicals

Casein from bovine milk is a phosphoprotein. It make up approximately 80% of the total protein in bovine milk. It is proposed to be the main protective constituent in milk.

Supplier: MP Biomedicals

AlbumiNZ™ Protease-reduced BSA is useful for immunoassays where proteases may degrade proteins or where peroxidase or alkaline phospahatase may hydrolyse substrates.

Supplier: MP Biomedicals

Pepstatin A is a reversible inhibitor of aspartic proteases, pepsin, renin, cathepsin D, cathepsin G, and other acid proteases. It does not inhibit thiol proteases, neutral proteases or serine proteases.

Supplier: MP Biomedicals

Interleukin-2 is an immunomodulatory factor produced by certain subsets of T lymphocytes. This lympho­kine promotes long term growth of activated T cells and related cell types.

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Lipoprotein- cholesterol is a mixture of lipoprotein cholesterol, phospholipids and fatty acids.

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Streptavidin is soluble in water at 1 mg/ml (clear to hazy), or in phosphate buffered saline (PBS). Readily soluble in water or salt-containing buffers (50 mg/ml or more).

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Soluble in 1:1 CHCl₃:methanol (50 mg/ml), soluble in DMF ((25 mg/ml).

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Typically prepared as a suspension in water adjusted to pH 5,0 with acetic acid. A 1% w/v solution will appear turbid.

Supplier: MP Biomedicals

Casein from bovine milk is a phosphoprotein. It make up approximately 80% of the total protein in bovine milk. It is proposed to be the main protective constituent in milk.

Supplier: MP Biomedicals

Aprotinin is a single chain polypeptide (58 amino-acids) crosslinked by three disulfide bridges, showing competitive and reversible inhibiton of proteolytic and esterolytic activity. Aprotinin forms stable complexes with, and blocks the active sites of serine protease enzymes. It is found in bovine lymph nodes, lung, parotid gland, spleen, liver, pancreas, seminal vesicles, thyroid gland, kidney, mucous membranes of the trachea and esophagus, ovaries, heart, posterior pituitary and cartilage.
Aprotinin is a competitive serine protease inhibitor that inhibits trypsin, chymotrypsin, kallikrein and plasmin. Aprotinin forms stable complexes with and blocks the active sites of enzymes. Binding is reversible with most aprotinin-protease complexes dissociating at pH >10 or < 3.

Aprotinin is used as a proteolytic inhibitor in radioimmunoassays of polypeptide hormones.

Supplier: MP Biomedicals

Concanavalin A is a pure Canavalia ensiformis lectin, FITC conjugated proteins or glycoproteins of non-immune origin that agglutinate cells and precipitate complex carbohydrates. They are capable of binding glycoproteins even in presence of various detergents.

Supplier: MP Biomedicals

Phytohemagglutinin PHA agglutinates the erythrocytes of all human blood groups as well as those of rabbit, dog, cat, mouse, sheep, and guinea pig.

Supplier: MP Biomedicals

Stem Cell Factor (SCF) is a hematopoietic growth factor that exerts its activity at the early stages of hematopoiesis. It stimulates the proliferation of myeloid, erythroid, and lymphoid progenitors in bone marrow cultures and has been shown to act synergistically with colony stimulating factors.

Supplier: MP Biomedicals

There is approximately one HBr or HCl per lysine unit. The HBr/HCl allows it to be a crystalline solid and soluble in water. To remove the HBr/HCl, solubilise the product in a neutral buffer and dialyse away the salts.

Supplier: MP Biomedicals

Chymostatin ([(S)-1-Carboxy-2-phenylethyl]-carbamoyl-α-[2-iminohexahydro-4(S)-pyrimidyl]-(S)-Gly-X-Phe-al) Source/Species: Microbial A mixture of type A, B, and C. X = Leu (Type A); Ile (Type B); Val (Type C). Ref: 1. Umezawa, H., et al., J. Antibiot., 23: 425 (1970). 2. Tatsuta, K., et al., J. Antibiot., 26: 625 (1973).

Supplier: MP Biomedicals

Aprotinin is a protein consisting of 58 amino acids, arranged in a single polypeptide chain that is cross-linked by three disulphide bridges. It is found in bovine lymph nodes, lung, parotid gland, spleen, liver, pancreas, seminal vesicles, thyroid gland, kidney, mucous membranes of the trachea and esophagus, ovaries, heart, posterior pituitary and cartilage.

Supplier: MP Biomedicals

Poly-L-lysine is a positively charged amino acid polymer. Poly-lysine binds to DNA, red cell membrane and any negatively charged protein. It is typically used as a coating substrate for culture dishes, slides, etc. It enhances electrostatic interaction between negatively charged ions of the cell membrane and the culture surface. When adsorbed to the culture surface, poly-lysine increases the number of positively charged sites available for cell binding.

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AlbumiNZ™ Low Fatty Acid BSA is chromatographically purified from New Zealand-sourced bovine plasma in an ISO quality system assuring complete traceability and consistent high quality. This albumin has very low endotoxin and low free fatty acids, is tested for the absence of viruses according to 9CFR and has the highest possible biosafety level.

Supplier: MP Biomedicals

Gelatin is a heterogeneous mixture of water-soluble proteins of high average molecular weights, present in collagen. The proteins are extracted by boiling skin, tendons, ligaments, bones, etc. in water. Type A gelatin is derived from acid hydrolysed tissue. The charge on a gelatin molecule and its isoelectric point are primarily due to the carboxyl amino and guanidino groups on the side chains. Type A gelatin has 78 to 80 millimoles of free carboxyl groups per 100 g of protein and a pI of 7,0 to 9,0.

Supplier: MP Biomedicals

A modified tripeptide reversible protease inhibitor of trypsin-like proteases and some cysteine proteases including endoproteinase Lys-C, kallikrein, papain, thrombin, cathepsin B, cathepsins H and L, trypsin, calpain, trypsin and plasmin. Little to no inhibition is seen against pepsin, cathepsins A and D and alpha-chymotrypsin. When adjusted for molarity, all three salt forms are equally effective; however, the hydrochloride salt is usually less invasive in biological settings. Leupeptin, because of its aldehyde group, may act as a reducing agent and therefore interfere in protein determinations such as Lowry and, to a lesser extent, Bradford.