Carboxypeptidase B (E.C. 3.4.17.2) was first discovered and isolated by Folk in 1960 in the pancreas of pigs and cattle. It is a class of digestive enzymes that can hydrolyze the substrate C-terminal arginine and lysine, synthesized in the form of inactive enzymes in the pancreas, each molecule contains a Zn atom, selectively hydrolyzed proteins and amino acids containing the carboxyl terminus of the polypeptide, its basic function is to decompose the peptides produced by trypsin degradation proteins, because the hydrolyzed amino acids are basic amino acids, carboxypeptidase B was initially named alkaline carboxypeptidase, in order to distinguish it from the earlier discovery of carboxypeptidase A, and finally renamed it carboxypeptidase B. Alkaline carboxypeptidase is also found in other tissues, such as the liver, lungs, intestines, brain, etc. [1].
Our carboxypeptidase B is recombinant expression by Pichia yeast without any tags, the theoretical molecular weight is 35kDa, the optimal digestion pH is 7.5~8.5, and the optimal digestion temperature is 37°C>. At a certain temperature (<60°C), enzyme cleavage activity can increase with increasing temperature. Recombinant carboxypeptidase B activity was inhibited by metal chelating agents such as EDTA, Cu2+, and Hg2+, while metal ions such as Zn2+ and Mn2+ could increase enzyme activity to varying degrees.
Applications of carboxypeptidase B
In the field of medical pharmaceuticals, CPB has the biological characteristic of preferentially cutting basic amino acids, so it can be used in the production of recombinant insulin products and participate in the digestion of proinsulin as an important tool enzyme [2]. 02Food manufacturing In the field of food manufacturing, it can be used to prepare high F-value oligopeptides.
the removal of ochratmycin from food and feed and the debittering of soybean protein hydrolysate [3].
In the field of biotechnology, carboxypeptidase B can be used to determine the synthesis of peptides and the amino acid sequence of peptides, and can also be used as a specific model enzyme, such as the design of zinc protease-specific inhibitors, to provide relevant help to other types of enzymes.
Our advantages:
High purity and high specific activity.
Good stability: Freeze-dried powder, easy to store and transport.
No animal origin: recombinant production, no exogenous virus contamination, no animal origin raw materials are used in the production process.
3,000L fermentation scale under the GMP quality management system: the batch output scale is large and the batch consistency is high, and the batch output can reach 500-1,000g, which can meet the quality requirements of scientific research customers and the requirements of industrialization customers for product quality, output and GMP conditions during industrialization.
Complete quality documentation: Relevant regulatory support documents can be provided according to customer needs.
A matching carboxypeptidase B content detection kit can be provided at the same time.

For any enquiries about P29/diapeptides/side chain/semaglutide api/tirzepatide api, plz feel free to contact me.
Tel: +8618575536586
Email: haoran.tse@gmail.com

Recombinant bibasic amino acid endopeptidase (Kex2; E.C.3.4.21.61) is a precursor processing enzyme belonging to the subtilis protease family, capable of specifically recognizing and cleaving the carboxyltelopeptide bonds of Lys-Arg and Arg-Arg bibasic amino acids. This enzyme is widely used in the processing of insulin analogue precursors and other enzymatic digestion processes for peptide or protein drugs.
Precursor processing enzymes are a class of proteolytic enzymes that are widely present in living organisms and play a shear processing role in the maturation of many peptides and proteins, and the concept of precursor processing was proposed by two laboratories more than 50 years ago [1,2]. Later, it was gradually discovered that the substrates processed by precursor processing enzymes include not only polypeptide hormones, but also neurotransmitters, growth factors, plasma proteins, viral coat glycoproteins, cell surface receptor proteins, and bacterial exotoxins. In recent years, the understanding of various precursor processing enzymes has gradually deepened, and the genes of various precursor processing enzymes have also been discovered, which has also shown their importance in cell cycle, apoptosis, antiviral drugs and gene regulation.
Our recombinant bibasic amino acid endopeptidase amino acid sequence is derived from Saccharomyces cerevisiae, recombinant expression by Pichia Pichia, theoretical molecular weight is 74kDa, optimal digestion pH is 8.0~10.0, optimal digestion temperature is 37°C, digestion activity is not inhibited by serine protease inhibitors such as PMSF, TPCK, etc., and is stable under pH 5.0~6.0 conditions.
Application of Kex2
Kex2 has great potential for application in the biopharmaceutical industry. At present, there are mainly the following aspects:

1. When designing the protein sequence, the Kex2 cleavage site is introduced, and the expression system is applied to Pichia yeast expression system, which is recognized and digested by the yeast's own Kex2 enzyme in the later secretion and expression process, so as to achieve a large amount of expression of recombinant protein. There are many relevant literatures in China, such as the secretion and expression of recombinant human insulin in Pichia [3], the secretion and expression of recombinant human parathyroid hormone pTH (1-34) in Pichia [4], and the secretion and expression of human epidermal growth factor (hEGF) in Pichia [5].
2. When designing the protein sequence, the Kex2 cleavage site is introduced, the protein is expressed by the Escherichia coli expression system, and the enzyme cleavage is performed with Kex2 in the later preparation process to obtain the target protein. The cutting of amino acid residues in this type of protein usually uses chemical method or enzyme cleavage method, while most of the chemical methods in the more general methods cannot avoid the modification of the target peptide and increase the purification cost, while the enzyme method is more likely to use such as achromatic bacillus enzyme I or trypsin, etc., these enzymes usually recognize an amino acid residue in use, which is highly restrictive to the sequence of the target protein, and may cause problems such as miscleavage, so the production and preparation of enzymes such as Kex2 that recognize several amino acid residues and have high specificity is particularly important. After review, it has been reported that the chimeric protein βGal-117S4HPPTH34 expressed by Kex2 enzyme can be used to cleave, from which recombinant human parathyroid hormone pTH (1-34) has been cleaved [6]. 3. Process digestion in peptide drug production, biological research: enzymatic digestion of proteins and peptide mapping analysis, sequencing, etc.

Our Kex2 product features:
High purity, high specific activity, and host protein residue is less than the limit requirements of biological products.
Good stability: Freeze-dried powder, easy to store and transport.
No animal origin: recombinant production, no exogenous virus contamination, no animal origin raw materials are used in the production process.
3,000L fermentation scale under the GMP quality management system: the batch output scale is large and the batch consistency is high, and the batch output can reach 500-1,000g, which can meet the quality requirements of scientific research customers and the requirements of industrialization customers for product quality, output and GMP conditions during industrialization.
Complete quality documentation: Relevant regulatory support documents can be provided according to customer needs.
Matching Kex2 trace residue detection kits are also available.

For any enquiries about P29/diapeptides/side chain/semaglutide api/tirzepatide api, plz feel free to contact me.
Tel: +8618575536586
Email: haoran.tse@gmail.com

The synthesis of Tirzepatide mainly adopts the strategy of solid-phase fragment condensation and solid-liquid binding, which focuses on solving the static hindrance effect of unnatural amino acids (such as Aib) in its 39 amino acid long chains, complex modifications of side chains (such as C20 diacid-PEG-γ-Glu-double AEEA-Lys²⁰), and racemic impurity control. The following are specific synthesis methods and technical points:

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The synthesis of semaglutide is an extremely complex process because it is a large, chemically modified peptide class (consisting of 31 amino acids). It is not easily done by pure chemical synthesis like small molecule drugs. Its synthesis can relies on a combination of solid-phase peptide synthesis(SPPS) and selective liquid-phase chemical modification. Here's an overview of the key steps of its synthesis route:

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The recombinant production of semaglutide is a "semi-recombinant" process that combines genetic engineering fermentation and chemical modification, and the core is to express intermediate peptides through microorganisms, and then enzymatic digestion, chemical modification and purification to obtain the final product. Here are the key process steps and technical points:

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