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R4877

Sigma-Aldrich

Rennin from calf stomach

≥20 units/mg protein

Sinonimo/i:

Chymosin

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About This Item

Numero CAS:
Classificazione EC (Enzyme Commission):
Numero CE:
Numero MDL:
Codice UNSPSC:
12352204
NACRES:
NA.54

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.

Pittogrammi

Health hazardExclamation mark

Avvertenze

Danger

Indicazioni di pericolo

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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Proteasi Type VIII, lyophilized powder, 7-15 units/mg solid

Sigma-Aldrich

P5380

Proteasi

Pepsina powder, ≥250 units/mg solid

Sigma-Aldrich

P7000

Pepsina

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
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
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
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
Jung-Feng Hsieh et al.
Journal of agricultural and food chemistry, 60(8), 2039-2045 (2012-02-07)
Chymosin-induced coagulation of individual milk proteins during incubation at 30 °C was investigated using a proteomic approach. The addition of chymosin (0.006 units/mL) caused the milk proteins to coagulate after a 3 h incubation period. Approximately 88% of the milk

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