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Recombinant Protease Enzymes
Recombinant Enzymes / Sequencing Grade Enzyme

https://en.wikipedia.org/wiki/Protease
https://en.wikipedia.org/wiki/Protein_production

A protease (also called a peptidase or proteinase) is any enzyme that performs proteolysis,
that is, begins protein catabolism by hydrolysis of the peptide bonds that link amino acids together in a polypeptide chain.
Proteases can be found in animals, plants, bacteria, archaea and viruses.
Proteases have evolved multiple times, and different classes of protease can perform the same reaction by completely different catalytic mechanisms.
The field of protease research is enormous. in 2004, approximately 8000 papers related to this field were published each year.
Proteases are used in industry, medicine and as a basic biological research tool.
Digestive proteases are part of many laundry detergents and are also used extensively in the bread industry in bread improver.
A variety of proteases are used medically both for their native function (e.g. controlling blood clotting)
or for completely artificial functions (e.g. for the targeted degradation of pathogenic proteins).
Highly specific proteases are commonly used to cleave fusion proteins and affinity tags in a controlled fashion. 

Guideline for Industry:

Leading with Quality, Performance and Cost :

Our partners, the Yaxin Biotechnology is a high-tech enterprise that focuses on researching and producing the recombinant enzymes.
http://www.yaxinbio.com/en/
YaxinBio is the first and only a professional company on researching and producing the recombinant carboxypeptidase B and recombinant trypsin in China.
Both of the two recombinant enzymes are specially used in the recombinant human insulin production, and exporting abroad.
Recombinant trypsin is used in the cell culturing process, which conforms to the 2014 USP.
Animal original free is very important for the production of antibody and vaccine .
Usage of recombinant trypsin fundamentally solves the problem of animal original virus contamination in the recombinant human insulin production.
Insisting on “scientific and technological innovation”, our team have focused on researching and manufacturing
the animal free Biological pharmaceutical raw materials, and have developed high performance recombinant
enzymes and sequencing grade enzymes with global quality, independent intellectual property rights and much helpful costs.

Products List:

Product
Information
Product Number Performance Packing Specifications Applications
Sequencing Grade Carboxypeptidase B SRCPB01 NLT 200 unit/mg pro 100μg;1mg protein structure and sequence analysis, antibody quality control.
Recombinant carboxypeptidase B RCPB01170 NLT 170 unit/mg pro 10mg;100mg;1g Insulin and antibody production
Sequencing Grade Modified Recombinant Trypsin SRT0202 NLT 4500 USP unit/mg pro 100μg;1mg Peptide mapping Peptide mass fingerprinting MS/MS spectral matching
Recombinant Trypsin RPT0201 NLT 3800 USP unit/mg pro 10mg;100mg;1g Cell culture, Insulin production, Animal cells culture example
Recombinant Trypsin(Human) RHT03 NLT 2500 USP unit/mg pro 10mg;100mg;1g Cell culture, Insulin production, Animal cells culture example
Reecombinant Chymotrypsin RCT10 NLT 1000 unit/mg pro 10mg;100mg;1g Peptide mapping, fingerprinting and sequence analysis
Sequencing Grade Recombinant Chymotrypsin SRCT03 NLT 1500 unit/mg pro 100μg;1mg Peptide mapping Protein identification MS/MS spectral matching
Recombinant Protein A RSPA05 E275/250 ≥1.2, E0.1% at 275nm=0.17-0.23 10mg;1g Antibody, Detection kit as ELISA, and Affinity gel productions. Research
Recombinant Enterokinase REK08 5U/μl 100U;500U;1KU; 10KU;20KU;100KU Recombinant protein production, R & D
Trypsin solution RTS04 2000BAEE unit/ml 100ml;500ml Cell culture, Insulin production, Animal cells culture example
Recombinant Aprotinin RTI16 NLT 3.0EPU/mg pro 10mg;100mg Cell culture, Vaccine production
Recombinant Kex2 Protease Re15 ≥10u/mg 50µg/each
  Kex2 is a Ca2+-dependent serine protease and cleaves at C-terminal site of Lys-Arg, Arg-Arg, Pro-Arg in pro-α-factor and killer-toxin precursors maturing.
V8(Endoproteinase Glu-C) V813 20U/mg 50μg,2mg Protein structure and sequence analysis
Recombinant Proteinase K RPK09 ≥30 u/mg 1g,100g,or bulk A serine protease that displays the ability to digest native proteins
More for inquiry......        


Certificate of Registration / Honor / Licence / COA example:

ISO 9001:2008, Scope of Registration: 
Development and Manufacture of Recombinant Protein
High-tech Enterprise Certificate

Business License COA example

International Business and Service:
As the Global Sales agency partners and Taiwan Branch(Yaxinbio_ABDC),
we take forward the international business, that include:
1.Direct marketing and services.
2.Services to dealers in the countries with counseling and assistance.
3.Integration of international technical cooperation projects.
We sincerely look forward to your associated enforcement,
for the establishment of more helpful product services and cooperations.

Papers, Application Guides and Application notes:

Products Descriptions:

Sequencing Grade Carboxypeptidase B
   
https://en.wikipedia.org/wiki/Carboxypeptidase

Catalog Number:SRCPB01

CAS: 9025-24-5
EC: 3.4.17.2
Source: Rat carboxypeptidase B, expressed in E. Coli.


DESCRIPTION

Carboxypeptidase B catalyzes hydrolysis of the basic amino acids lysine, arginine and histidine from the C-terminal end of polypeptides. 
The molecular weight is 34,500 daltons, the pH optimum is 8.0, and pI is 6.0. 

Carboxypeptidase B is competitively inhibited by arginine and lysine. 
The enzyme is also inhibited by metal chelating agents, e.g., EDTA.

Recombinant Carboxypeptidase B is expressed in E.Coli and purified by high pressure liquid chromatography. 

There is no trace of other enzyme 
activity.(such as carboxypeptidase A and chymotrypsin)
No protease inhibitors such as PMSF are present in the preparation.

 
MAIN FEATURES 

Source

E. Coli

Purity by HPLC

≥ 95%

Format

Lyophilized

Specific activity

≥ 200 units/mg pro

Contaminant activity

No chymotrypsin, carboxypeptidase A, or other proteases contaminant. 

APPLICATION
Protein structure and sequence analysis, such as hydrolyze basic amino acids lysine, arginine and histidine from the C-terminal end of polypeptides. 
Antibody quality control.
 
RECOMMEND USAGE 
To prepare 1-10mg/ml carboxypeptidase B with sterile water or 25mM Tris-HCl pH 7.65. 
The ratio to aimed protein is 1:50 to 1:1000 (w/w), the optimum pH is pH 7.0-9.0. 

 
STORAGE INSTRUCTIONS
Recommend recombinant carboxypeptidase B lyophilized should be stored under 2-8
in sealed container.
It is stable within 24 months.After dissolved, it should be stored under -20
,
It is stable within 24 months and no activity lose after 10 times repeated freezing and thawing. 


Recombinant Carboxypeptidase B
   

Catalog Number:RCPB01
CAS: 9025-24-5
EC: 3.4.17.2
Source: Expressed in E. Coli.
 
DESCRIPTION
Carboxypeptidase B catalyzes hydrolysis of the basic amino acids lysine, arginine and histidine from the C-terminal end of polypeptides. The molecular weight is 34,500 daltons, the pH optimum is 8.0, and pI is 6.0.
Carboxypeptidase B is competitively inhibited by arginine and lysine. 

The enzyme is also inhibited by metal chelating agents, e.g., EDTA. 
Recombinant Carboxypeptidase B (EC 3.4.17.2) is expressed in E.Coli and purified by high pressure liquid chromatography.
There is no trace of other enzyme (such as carboxypeptidase A and chymotrypsin) activity.
No protease inhibitors such as PMSF are present in the preparation.

ADVANTAGES
Animal origin free:YaxinBio recombinant carboxypeptidase B belongs to the AOF level 3, eliminate the risk of virus presence, 
or of any other potential adventitious agents found in animal-derived carboxypeptitase B

StabilityA sterile recombinant carboxypeptidase B lyophilized eliminates the risk of contamination and decreases 
he chances of activity loss in the process of transport and storage. 

High purity:
1) Recombinant carboxypeptidase B provides increased specific activity and eliminates contaminating protease
activities found in extracted enzymes with lower purity level. 

2) No other contaminating proteases such as chymotrypsin and carboxypeptidase A. 
3
Less than 10ppm of recombinant trypsin. 

MAIN FEATURES

Source

E. Coli

Purified by

HPLC 

Format

White or white-like or yellowish lyophilized

Additives

Tris salts, NaCl salts and carbohydrates

Protein content

35%  60%

Specific activity

 ≥170 units/mg pro.

Purity

Single main band on SDS-PAGE

M.W.

35kD

Contaminant activity

Less than 10 ppm of recombinant trypsin.

NIT DEFINITIONOne Unit of carboxypeptidase B activity hydrolyzes one micromole of hippuryl-L-arginine per minute at 25, pH 7.65.
RECOMMEND USAGE :
To prepare 1-10mg/ml carboxypeptidase B with sterile water or 25mM& Tris-HCl pH 7.65.
The ratio to ;aimed protein is 1:50 to 1:1000 (w/w), the optimum pH is pH7-9. 

STORAGE INSTRUCTIONS
Recommend recombinant carboxypeptidase B lyophilized should be stored under 2
-8 in sealed container.
It is stable within 24 months.After dissolved, it should be stored under -20
,
It is stable within 24 months and above 90% activity remained after 10 times repeated freezing and thawing.

Sequencing Grade Modified Recombinant Trypsin
 
 
https://en.wikipedia.org/wiki/Trypsin

Catalog Number:SRT0202
CAS: 9002-07-7
EC: 3.4.21.4
Source: Expressed in E. Coli, methylation modified.
 
DESCRIPTION
Trypsin specifically hydrolyzes peptide bonds at the carboxyl side of lysine and arginine residues. 
Recombinant trypsin is free of any other proteases activities, and TPCK is unnecessary and not contained. 
Unmodified trypsin is subject to auto-proteolysis, generating fragments that can interfere with protein sequencing or HPLC/MS peptides analysis. 

YaxinBio’s sequencing grade modified trypsin is recombinant porcine trypsin modified by reductive methylation, 
rendering it resistant to proteolytic digestion. 


MAIN FEATURES

Source

E. Coli

Format

Liquid in 50mM HAc, or fluffy solid.

Protein concentration

0.5mg/ml in 50mM HAc

Specific activity

≥ 4500 USP units/mg pro

PurityRP-HPLC)

≥99% by HPLC

Contaminant activity

Recombinant porcine trypsin. 
No any other proteases activities contaminant. 

UNIT DEFINITIONOne USP unit of trypsin activity will produce a Delta A253 of 0.003 per minute in a reaction volume of 3.0ml at pH7.6 and 25
with BAEE as a substrate (1cm light path).


APPLICATION
Protein digests for peptide mapping applications or protein identification by peptide mass fingerprinting or MS/MS spectral matching. 
It is suitable for digestion reactions in-solution or in-gel.


RECOMMEND USAGE 
1. To dilute recombinant modified trypsin with 50mM HAc if needed. When used, dilute it with 50mM NH
4HCO3 or pH7-8 buffers directly. 1mM CaCl2 is recommended to be contained in digestion buffer. 
The ratio to aimed protein is 1:20 to 1:100 (w/w), the optimum pH is pH7-8.
2. To use this product, thaw at room temperature, mix gently before use. 
3. No activity lost when freeze-thaw 5 cycles. 

STORAGE INSTRUCTIONS
1. The solution should be stored under -70
, It is stable within 24 months.
2. Above 95% activity remained after 5 times repeated freezing and thawing.
3. A 0.05 mg/ml solution of sequencing grade modified recombinant trypsin retained above 95% after a 3 hours incubation
at 37 
 in 50mM NH4HCOFor long-term such as 20hours incubation, 1mM CaCl2 is recommended to be contained.

Recombinant Trypsin
 
 

Catalog Number:RPT0201
CAS: 9002-07-7
EC: 3.4.21.4
Source: Porcine trypsin,
expressed in E.coli.
 
DESCRIPTION
Trypsin is a member of the serine protease family.

Trypsin cleaves peptides on the C-terminal end of lysine

and arginine amino acid residues.
The pH optimum of trypsin is pH 7 - 10. The enzyme is inhibited by serine protease inhibitors, e.g. PMSF, and by metal chelating agents,
e.g., EDTA.
Recombinant Porcine Trypsin is a genetically engineered protein expressed in E.coli
and purified by high pressure liquid chromatography.
There are no contaminating enzyme activities such as carboxypeptidase A and chymotrypsin.
No protease inhibitors such as PMSF are contained in the preparation.


ADVANTAGES

Animal origin free:
The use of recombinant Porcine Trypsin eliminates the risk of virus presence,
and other potential adventitious agents found in animal derived trypsin.
YaxinBio Recombinant Porcine Trypsin belongs to the AOF level 3.

Stablility:
A sterile recombinant trypsin lyophilized eliminates the contamination risks and decreases the chance of activity loss
in the process of transport and storage.

High purity:
1)Recombinant porcine trypsin provides increased specific activity and eliminates contaminating proteases activities
found in extracted enzymes.
2)No other contaminating proteases such as chymotrypsin or carboxypeptidase A.

MAIN FEATURES

Source

E. Coli

Purified by

HPLC

Format

White lyophilized

Additives

Carbohydrates

Protein content

35% 70%

Specific activity

  ≥3800 USP units/mg pro

PurityRP-HPLC)

NLT 70% β-trysin, NMT 20% α-trypsin

Contaminant activity

 No chymotrypsin, carboxypeptidase A, and other protease contaminant.

UNIT DEFINITIONOne USP unit of trypsin activity will produce a Delta A253 of 0.003 per minute
in a reaction volume of 3.0ml at pH7.6 and 25, with BAEE as a substrate (1cm light path).

RECOMMEND USAGE
To prepare 1-10mg/ml recombinant trypsin with 1mM HCl.
The ratio to aimed protein is 1:50 to 1:1000(w/w), the optimum pH is pH7-10.


STORAGE INSTRUCTIONS
Recombinant trypsin lyophilized should be stored under 2
-8 in sealed container. It is stable within 24 months.
After dissolved, it should be stored under -20.
It is stable within 24 months and above 90% activity remained after 10 times repeated freezing and thawing.

Recombinant Trypsin (Human)
 
 
Catalog Number:RHT03
CAS: 9002-07-7
EC: 3.4.21.4
Source: human trypsin, expressed in E. Coli.
 
DESCRIPTION
Trypsin is a member of the serine protease family. 
Trypsin cleaves peptides on the C-terminal end of lysin
e and arginine amino acid residues. 

The pH optimum of trypsin is pH 7 - 10. The enzyme is inhibited by serine protease inhibitors, 
e.g. PMSF, and by metal chelating agents, e.g., EDTA. 

Recombinant Human Trypsin is a genetically engineered protein expressed in E.coli and purified 
by high pressure liquid chromatography. 

There are no contaminating enzyme activities such as carboxypeptidase A and chymotrypsin. 
No protease inhibitors such as PMSF are contained in the preparation.


ADVANTAGES

Animal origin free:The use of recombinant Human Trypsin eliminates the risk of virus presence, 
and of any other potential adventitious agents found in animal pancreas-derived trypsin. 

YaxinBio Recombinant Human Trypsin belongs to the AOF level 3.
Recombinant human trypsin:The amino acid sequence is the same as the Human Trypsin 2.

Stable:
A sterile recombinant human trypsin lyophilized eliminates the contamination risks
and decreases the chance of activity loss in the process of transport and storage.


High purity:
1) Recombinant human trypsin provides increased specificity and eliminates
   contaminating activities found in lower purity enzymes.
2) No other contaminating proteases such as chymotrypsin or carboxypeptidase A.
3) Purity is more than 95% by HPLC.

MAIN FEATURES

Source 

E. Coli

Purified by

HPLC

Format

White or White-like lyophilized

Specific activity

≥ 2500 USP u/mg pro.

Purity

≥ 95% by HPLC

Contaminant activity

No chymotrypsin, carboxypeptidase A, and other protease contaminant. 

UNIT DEFINITION
One USP unit of trypsin activity will produce a Delta A253 of 0.003 per minute in a reaction volume
of 3.0ml at pH7.6 and 25
, with BAEE as a substrate (1cm light path).

TORAGE INSTRUCTIONS
Recombinant human trypsin lyophilized should be stored under 2
-8 in sealed container.
It is stable within 24 months.
After dissolved, it should be stored under -20
It is stable within 24 months and above 90% activity remained after 10 times repeated freezing and thawing. 

Recombinant Human Chymotrypsin
 
 
https://en.wikipedia.org/wiki/Chymotrypsin

Catalog Number:RCT10
CAS: 9004-07-3
EC: 3.4.21.1
Source: human chymotrypsin, expressed in E. Coli.


DESCRIPTION

Chymotrypsin is a recombinant serine endopeptidase expressed in E.coli, purified with HPLC, 
the gene sequence is the same as human chymotrypsin. 
Recombinant chymotrypsin hydrolyzes at the carboxyl side of aromatic amino acids residues: 
Tyr, Phe and Trp. Cleavage may also be observed, but at a lower rate, at Leu and Met. 
Chymotrypsin activity is optimal in pH 7.0–9.0. 

 
ADVANTAGES

Animal origin free
Recombinant human chymotrypsin eliminates the risk of virus presence, and other 
potential adventitious agents found in animal-derived chymotrypsin. 

High purity
Recombinant Chymotrypsin provides increased specificity and eliminates contaminated 
other proteases activities found in enzymes purified from pancreas.


Stable
A sterile recombinant human chymotrypsin lyophilized decreases the contamination risks and
chance of activity loss during transport and storage.

 
APPLICATION
Hydrolysis of proteins by chymotrypsin alone or in combination with other proteases. 
Suitable for peptide mapping, fingerprinting, and sequence analysis.
 
MAIN FEATURES 

Source

E. Coli

M.W.

26,950 Da  

Purified by

HPLC 

Format

White lyophilized 

Specific activity

≥1000 unit/mg pro

Purity

> 95% by HPLC

UNIT DEFINITION: One unit will hydrolyze 1.0 μmole of BTEE per min at pH 7.8 at 25 °C.
 
RECOMMEND USAGE
To prepare 1-10mg/ml with 1ml 50mM HAc, used within 2 days, or stored below -20
 after repacked 
 
STORAGE INSTRUCTIONS
Recombinant Chymotrypsin lyophilized should be stored under 2
-8 in sealed container.
It is stable within 24 months. After dissolved, it should be stored under -20.

Sequencing Grade Recombinant Chymotrypsin
   

Catalog Number:SRCT03
CAS: 9004-07-3
EC: 3.4.21.1
Source: human chymotrypsin, expressed in E. Coli.
 
DESCRIPTION
Chymotrypsin is a recombinant serine endopeptidase expressed in E.coli, purified with HPLC, 

the gene sequence is the same as human chymotrypsin. 
Recombinant chymotrypsin hydrolyzes at the carboxyl side of aromatic amino acids residues: 
Tyr, Phe and Trp. Cleavage may also be observed, but at a lower rate, at Leu and Met. 
Chymotrypsin activity is optimal in pH 7.0-9.0.

The sequencing grade human chymotrypsin can be used alone or in combination with other 
proteases to produce protein digests for peptide mapping applications or protein identification 
by peptide mass fingerprinting or MS/MS spectral matching. 

It is suitable for digestion reactions in-solution or in-gel.

MAIN FEATURES 

Source

E. Coli

M.W.

26,950 Da  

Purity

≥ 98 % by HPLC. 

Format

Lyophilized 

Specific activity

≥ 1500 units/mg pro

APPLICATION 
1) Protein digests for peptide mapping applications or protein identification by peptide mass fingerprinting
or MS/MS spectral matching. It is suitable for digestion reactions in-solution or in-gel.

2) This sequencing grade enzyme can be used alone or in combination with other proteases to produce.

RECOMMEND USAGE
For dissolving buffer ,it is 50mMHAC, to get the terminal concentration of 0.5μg/μl,
used once time or stored below -20.
For the digestion buffer,
in general, it is 50mM or 100mM H4HCOto dissolve the aim protein and then
added chymotrypsin (in general,
W:W=1:50) .
Self digestion may occur if temperatures above 37°C.

STORAGE INSTRUCTIONS
Recombinant Chymotrypsin lyophilized should be stored under 2
-8 in sealed container.
It is stable within 24 months. After dissolved, it should be stored under -20
It is stable within 24 months and above 90% activity remained after 10 times repeated freezing and thawing. 


Recombinant Protein A
   
https://en.wikipedia.org/wiki/Protein_A

Catalog Number:RSPA05
CAS: 91932-65-9
Source:
Protein A mutant of Staphylococcus aureus , expressed in E. Coli.
 
APPLICATION:
The recombinant Protein A is a genetically engineering protein containing IgG-binding domains.

Recombinant Protein A is ideal for purification of polyclonal or monoclonal IgG antibodies.

Protein A binds to most human and mouse IgG subclasses (e.g., human IgG1, IgG2, IgG4;
mouse IgG2, IgG2a, IgG2b,IgG3).  It also binds to cow, guinea pig, hamster, house,
pig and rabbit total IgG form.

Recombinant protein A can be coupled to solid separation medium (such as agarose) for monoclonal
and polyclonal antibody purification.
Recombinant protein A can be coupled to a variety of molecules (such as fluorescent molecules,
enzyme markers, biotin, colloidal gold and radioactive markers).
These coupled derivatives can be used in antibody test in the process of Western-blot, ELISA or immunohistochemical tests.


PRODUCT SPECIFICATION

Test/Method                    

Specification

Bioburden

No organisms detected.

12% SDS-PAGE 

Single major band

Coomassie Stain

25kD 

UV Spectrum 

E275/250 ≥1.2, E0.1% at 275nm=0.17-0.23 

UV spectrometry

No DNA or RNA detected

Triton Content

No Triton contaminant. 

Format

Lyophilized

pH stable range

pH 1-13

STORAGE INSTRUCTIONS
Recombinant Protein A lyophilized should be stored under 2-8
in sealed container. It is stable within 24 months.

USAGE:
For Research or Manufacturing Purpose Only. Not for Human.

Recombinant Enterokinase(Enteropeptidase)
 
 
https://en.wikipedia.org/wiki/Enteropeptidase

Catalog Number: REK08
CAS: 9017-74-8
EC: 3.4.21.9
Source: bovine enterokinase, expressed in E. Coli
 
DESCRIPTION
YaxinBio Enterokinase is a kind of highly purified recombinant bovine enterokinase. 

The enzyme has been extensively purified and there are no traces of other contaminating 
proteases. 
Enterokinase specifically hydrolyzes peptide bond at the carboxyl side of lysine residue preceded by four aspartic acids: Asp-Asp-Asp-Asp-Lys (DDDDK). So, Enterokinase can remove N-terminal fusion protein or tags 
to get aim protein with native amino acids sequence.

 
ADVANTAGES
1) Protease that cleaves specifically after a lysine preceded by four aspartic acids: Asp-Asp-Asp-Asp-Lys (DDDDK)
2) No any other contaminated proteases, no non-specific cutting sites.
 
Recommend Usage Condition:
Cutting condition:             given an example: 25mM Tris-HCl 8.0
Fusion protein concentration:  0.1-1mg/ml (total protein content: 0.5-1.0mg)
EK content:                   1-2U 
Temperature:                  25

Time:
over night or 12h-16h for digestion.
 
Common components influence the action of enterokinase

200mM imidazole or 200mM NaCl or 5%glycerin, the reaction may be effected.

The following suggestions are given:
 
1) To receive the optimum result, please dialyze the sample to 25 mMTris-HCl, pH 8.0.
 
2) If the dialysis is inconvenient, please dilute the sample to 100mM imidazole, 50mMNaCl,
5% glycerin, and the proportion of fusion protein and EK may not be changed (1U:0.5mg fusion protein).
 
3) If there are one or more components in samples, and cannot be removed,
suggest to increase the content of EK in reaction system or extend the reaction time.


MAIN FEATURES

Source

E.Coli

M.W.

25,850 Da  

Specific Activity

One unit is defined as the amount of enzyme needed to cleave 0.5mg of fusion protein in 12 to16 hours to get 95% completion at 25°C in 25mMTris-HCl,pH 8.0. Substrate: a special fusion protein.

Storage

-20°C or below.  

Stability

Keep cool with blue ice during shipping. Remained stable at 25°C for one week without activity lost. No activity lost after 5 cycles of frozen-thawing.

PRODUCT INFORMATION

Product

Cat.No

 Activity

Packaging

Manufacturer

Recombinant Enterokinase

REK08

≥5 U/μl

100U;500U;1KU;
10KU;20KU;100KU

YaxinBio

Trypsin Solution
 
 

DESCRIPTION
Recombinant trypsin solution, is an animal component free trypsin solution optimized for cell dissociation. It is formulated with recombinant human trypsin expressed in E.Coli and refolded and purified by chromatography.
The sequence of recombinant human trypsin is same as human trypsin 2 sequence.


FEATURES AND BENEFITS
Recombinant trypsin, Animal component-free, eliminate the risk of virus and mycoplasma contamination
Recombinant trypsin, no bacteria, mycoplasma, mold and virus was found and bio-burden is conform to biological standard, eliminates the risk of viruses, or other potential adventitious agents.

Recombinant trypsin
Recombinant trypsin owns a similar kinetic of cell detachment to native trypsin.
Soybean trypsin inhibitors and other inhibitors work the same way with recombinant human trypsin as they do with native trypsin.


High purity
Recombinant trypsin provides high specific activity and eliminates contaminated material found
in 1:250 trypsin or other animal origin trypsin.


High safety
The trypsin solution, ready to-use, eliminates the risk of activity loss in the process of transport
and storage. It also eliminates the contamination risk that a lyophilized powder has.


Convenient
Recombinant trypsin solution is formulated at an optimal concentration to dissociate adherent cells.

Good work without EDTA
No EDTA contained in buffer. And a good cell dissociation result can be obtained,
and then eliminate EDTA influence on cell apoptosis experimental analysis.


METHOD OF USE
Step 1. Pour 1 ml buffer solution into EP tube containing trypsin powder.
Step 2. Dissolve the trypsin powder, and then pour the solution into the vial containing buffer solution
 and mix. Best use it within 4 hours.


NOTES:
Note 1. Dissociate adherent cells under room temperature ; 37
is not recommended.
Note 2. If necessary, after dissolving, immediately dispense into suitable containers,
then stored under -20
. To use it, dissolve it at room temperature.
Note 3. The content of trypsin is 2000 BAEE unit/ml as above prepared.
If necessary, dilute it to 1000 unit/ml or others based on your experimental results.


PRODUCTS INFORMATION

Product

Cat. No.

Activity

Packaging

Manufacturer

Recombinant Trypsin Solution

RTS04

2000 BAEE u/ml

100 ml,500ml

YaxinBio

UNIT DEFINITIONOne BAEE unit of trypsin activity will produce a Delta A253 of 0.001 per minute
 in a reaction volume of 3.0ml at pH7.6 and 25
(1cm light path)

Recombinant Aprotinin
   
https://en.wikipedia.org/wiki/Aprotinin

Catalog Number: RTI16
Anonym: Trypsin Inhibitor
CAS: 9087-70-1
Source: Expressed in E. Coli
 
DESCRIPTION
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 and dissociating at pH >10 or <3. 
Effective concentration is equimolar with protease.

 
RECOMBINANT, ANIMAL COMPONENTS FREE
Recombinant aprotinin is expressed in E. Coli, and purified with HPLC. 
It contains no animal-derived components. This is a recombinant form of bovine lung aprotinin, 
which is traditionally isolated from bovine lung by methods involving fractional precipitation, gel filtration, 
and ion exchange chromatography. 


MAIN FEATURES

Source 

E. Coli

Purified by

HPLC 

Format

Liquid

Specific activity

≥ 3.0 EPU/mg pro. 

Purity

≥ 95% 

Contaminant activity

No any other protease contaminant. 


UNIT DEFINITION: One trypsin inhibitor unit (EPU) will decrease the activity of 2 trypsin units by 50%
where one trypsin unit will hydrolyze 1.0 μmole of N-benzoyl-L-arginineethyl ether(BAEE) per sec at pH 7.6 at 25 °C.

A conversion factor for Aprotinin is: 1 EPU = 1 USP Aprotinin Unit = 1800 KIU.
 
STORAGE INSTRUCTIONS
Recombinant aprotinin should be stored under -20°C or below in sealed container.
It is stable within 24 months.

Recombinant Kex2 Protease
   
https://en.wikipedia.org/wiki/Kexin

Catalog Number:Re15
EC: 3.4.21.61
Source:Saccharomyces cerevisiae Kex2, expressed in Pichia pastoris
 
DESCRIPTION

Kex2 is a Ca2+-dependent serine protease and cleaves at C-terminal site of Lys-Arg, Arg-Arg,

Pro-Arg in pro-α,factor and killer-toxin precursors maturing, it was discovered in Saccharomyces cerevisiae.
But Kex2 can’t recognize and cut a single basic amino acid,such as carboxyl end peptide bond of arginine and lysine.
Recombinant Kex2 is a genetically engineered protein expressed in Pichia pastoris and purified by high pressure liquid chromatography.
The optimal pH of Kex2 protease is 9.0, and the optimal temperature is 37 .
It is stable in buffer (pH 5.0-6.0).
The activity of Kex2 is not affected by the conventional serine protease inhibitors such as PMSF, TPCK, TLCK inhibition.


MAIN FEATURES

Source

Pichia pastoris

Purified by

HPLC 

Format

Liquid in10mM NaAc-HAc(PH 5.2) and 2mM Ca2+

Specific activity

≥10u/mg

12%SDS-PAGE

Single main stripe

Mol.weight

67 kD

UNIT DEFINITION: One USP unit of Kex2 activity will catalyze 1μmol Boc-QRR-pNA per minute
in a reaction volume of 3.0ml at pH8.0 and 25.


STORAGE INSTRUCTIONS
Recommended storage temperature: -20 °C or below.

It is stable after 5 cycles freezing and thawing. 

Transport temperature: ≤ 8 °C.
It should be stored in 10mM NaAc-HAc(PH 5.2) and 2mM Ca
2+.

PRODUCT INFORMATION

Product

 Specific activity

Packaging

Manufacturer

Recombinant Kex2 Protease

≥10u/mg

50µg/each

YaxinBio


V8(Endoproteinase Glu-C)

   
https://en.wikipedia.org/wiki/Glutamyl_endopeptidase

Catalog Number:V813
CAS:
66676-43-5
EC:3.4.21.19
Full Name:Endoproteinase Glu-C,from Staphylococcus aureus strain V8,V8 Protease
 
DESCRIPTION    
Staphylococcus aureus Protease V8 (Endoproteinase GluC) is a serine proteinase that selectively cleaves peptide bonds C-terminal
to glutamic acid residues. It also cleaves at aspartic acid residues.
The Optimum pH is 8.0 ~ 8.5. Its enzyme inhibitors are Phosphoric acid diisopropyl ester fluoride (DFP)
and alpha 2 - macroglobulin and Na-p-tosyl-L-lysine chloromethyl ketone (TLCK).

 
SPECIFIC ACTIITY 
Approx.20U/mg ar 25 with Z-Phe-Leu-Glu-4-nitranilide as the substrate(approx.500U/mg at 37 with casein as the substrate).

 
RECOMMEND
 USAGE
Cutting condition:PH 8.0~8.5
 
PACKAGING
1U/vial50µg/vial

 
STORAGE INSTRUCTIONS

V8 Protease should be stored under -20 in sealed container.

 
APPLICATION 
Protein structure and sequence analysis

Recombinant proteinase K
 
 
https://en.wikipedia.org/wiki/Proteinase_K

INTRODUCTION

Proteinase K is a non-specific endonuclease protein, belongs to the serine protease enzyme, can cut the ester and peptide bond on the carboxy-terminal of aliphatic, aromatic and hydrophobic amino acids, and is used for protein degradation in biological samples.
The Molecular weight is 28.9 kDa (monomer), is active under the conditions of pH4 to pH12 , is also very stable while the presence of SDS, urea, or EDTA.
This enzyme was purified by discoloration and chromatography to remove RNA and DNA, without other miscellaneous activity be detected.
Since the stability of proteinase K in urea and SDS, and also has the ability to degrade the natural proteins, it hydrolyses four peptide molecules at minimum.

PRODUCT BENEFITS

High purity: No other miscellaneous activity: Enzyme cutting with no other side effects. High yield.
High specific activity: specific activity of not less than 30u/mg protein
Electrophoresis purity: SDS-PAGE electrophoresis, more than 99%
Stability: lyophilized powder, easy to store and transport

USAGE
Mainly used in genetic diagnostic kits, genomic DNA extraction kit, RNA extraction kit for removing the nuclease in the preparation of DNA and RNA.
Also used for degradation of protein-containing impurities in the extraction of  nonprotein component in tissue,
such as  in the preparation of DNA vaccines and heparin , etc., may also be used for the preparation of chromosomal DNA and protein blotting.

PRODUCT FEATURES

Source

Tritirachium album limber

Molecular weight

Theoretical MW: 28.9 kDA

Activity

activity Unit Definition: under 37 , pH 7.5 conditions, proteinase K amount to generate 1 μmol tyrosine per minute by from the hydrolysis of the substrate casein is defined as one unit (U).

Storage

can be cryopreserved at 0 ~ 4 condition for dry powder status. With -20 storage for dissolved aliquot of appropriate volume.

Stability

transportation can be carried out at room temperature.

PRODUCT INFORMATION

Product Name

Catalog Code

Activity

Packaging

Origin

Recombinant proteinase K

RPK09

30 u/mg

1g,100g,or bulk

YaxinBio


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