R4877
Rennin from calf stomach
≥20 units/mg protein
Sinonimo/i:
Chymosin
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About This Item
Prodotti consigliati
Forma fisica
lyophilized powder
Attività specifica
≥20 units/mg protein
Purificato mediante
crystallization
Composizione
Protein, ≥40%
Temperatura di conservazione
−20°C
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Applicazioni
Rennin, also known as chymosin, is a milkclotting acid proteinase produced in the stomach of a calf. It is used in cheesemaking and to study neonatal gastric digestion .
Azioni biochim/fisiol
Rennin, a 323 amino acid chain, is secreted as an inactive precursor which is then converted into an active enzyme through limited proteolysis. It cleaves the peptide bond between phenylalanine and methionine in K-Casein.
Confezionamento
Package size based on protein content
Definizione di unità
One unit will coagulate 10 mL of milk per min at 30 °C.
Stato fisico
Lyophilized powder containing sodium chloride
Risultati analitici
Protein determined by biuret.
Avvertenze
Danger
Indicazioni di pericolo
Consigli di prudenza
Classi di pericolo
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Organi bersaglio
Respiratory system
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Certificati d'analisi (COA)
Cerca il Certificati d'analisi (COA) digitando il numero di lotto/batch corrispondente. I numeri di lotto o di batch sono stampati sull'etichetta dei prodotti dopo la parola ‘Lotto’ o ‘Batch’.
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I clienti hanno visto anche
B Foltmann et al.
The Journal of biological chemistry, 254(17), 8447-8456 (1979-09-10)
The complete amino acid sequence of calf chymosin (rennin) (EC 3.4.23.4) has been determined. The sequence consists of a single peptide chain of 323 amino acid residues. The primary structure of the precursor part of calf prochymosin was published previously
Kirsten Kastberg Møller et al.
Journal of agricultural and food chemistry, 60(21), 5454-5460 (2012-05-09)
Bovine chymosin constitutes a traditional ingredient for enzymatic milk coagulation in cheese making, providing a strong clotting capacity and low general proteolytic activity. Recently, these properties were surpassed by camel chymosin, but the mechanistic difference behind their action is not
Xin-ping Li et al.
Xi bao yu fen zi mian yi xue za zhi = Chinese journal of cellular and molecular immunology, 28(7), 715-717 (2012-07-10)
To optimize the prochymosin (pCHY) gene codons and express the gene in Escherichia coli (E.coli), and to prepare its antiserum and detect chymosin protein specifically. According to codon usage bias of E.coli, prochymosin gene sequence was synthesized based on the
Neil D Rawlings et al.
Nucleic acids research, 40(Database issue), D343-D350 (2011-11-17)
Peptidases, their substrates and inhibitors are of great relevance to biology, medicine and biotechnology. The MEROPS database (http://merops.sanger.ac.uk) aims to fulfil the need for an integrated source of information about these. The database has hierarchical classifications in which homologous sets
G L Gilliland et al.
Advances in experimental medicine and biology, 306, 23-37 (1991-01-01)
Many aspects of the structure of chymosin are quite unique even though structure comparisons indicate a high degree of structural homology with other eukaryotic aspartic proteinases. The structural homology is shown to be directly related to the sequence homology which
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