Structure of Recombinant trypsin EC 3.4.21.4 CAS 9002 07 7 - Recombinant trypsin EC 3.4.21.4 CAS 9002-07-7

Iden­ti­fi­ca­tion

CAS Number

9002-07-7

EC Number

3.4.21.4

Name

Recom­bi­nant trypsin

Syn­onyms

Trypsin-EDTA Solu­tion 1X ;
α-and β-trypsin ;
Tryprar ;
Tryp­sevas ;
Trypsin Pow­der, Porcine 1:250 ;
TRYPSIN TYPE V-S :
ACETY­LAT­ED FROM*BOVINE PAN­CREAS ;
TRYPSIN, PRO­TEOMICS SEQUENC­ING GRADE ;

SMILES

CC1=CC(=CC2=C1C=CC(=O)O2)NC(=O)C(CCCN=C(N)N)NC(=O)C(CO)NC(=O)C(CC3=CC=CC=C3)NC(=O)OC(C)(C)C.CC(=O)O

InChI

InChI=1S/C33H43N7O8.C2H4O2/c1-19-15-21(17-26-22(19)12-13-27(42)47-26)37-28(43)23(11-8-14-36-31(34)35)38-30(45)25(18-41)39-29(44)24(16-20-9-6-5-7-10-20)40-32(46)48-33(2,3)4;1-2(3)4/h5-7,9-10,12-13,15,17,23-25,41H,8,11,14,16,18H2,1-4H3,(H,37,43)(H,38,45)(H,39,44)(H,40,46)(H4,34,35,36);1H3,(H,3,4)/t23-,24-,25-;/m0./s1

InChI Key

WGWZNYK­OUX­OZTC-NAGNLM­CH­SA-N

Mol­e­c­u­lar Formula

C35H47N7O10

Mol­e­c­u­lar Weight

725.78858

EINECS

232-650-8

MDL Number

MFCD00082094

Prop­er­ties

Appear­ance

White or off white, or yel­low­ish powder

Safe­ty Data

Sym­bol

exclamation mark jpg - Recombinant trypsin EC 3.4.21.4 CAS 9002-07-7health hazard jpg - Recombinant trypsin EC 3.4.21.4 CAS 9002-07-7GHS07,GHS08

Sig­nal Word

Dan­ger

Haz­ard statements

H315H319H334H335

Pre­cau­tion­ary Statements

P302 + P352P305 + P351P338

Tar­get organs 

Res­pi­ra­to­ry system

Per­son­al Pro­tec­tive Equipment

dust mask type N95 (US), Eye­shields, Faceshields, Gloves

RIDADR 

NONH for all modes of transport

WGK Germany

1

RTECS 

YN5075000

Spec­i­fi­ca­tions and Oth­er Infor­ma­tion of Our Recom­bi­nant trypsin EC 3.4.21.4 CAS 9002-07-7

ItemsRecom­bi­nant TrypsinRecom­bi­nant Trypsin (Liq­uid)Recom­bi­nant Human TrypsinSequenc­ing Grade Mod­i­fied Trypsin
Appear­anceWhite or off white, or yel­low­ish powderClear, col­or­less or shal­low yel­low liquidWhite or off white powderWhite or off white, or yel­low­ish powder
Pro­tein Concentration/70±10 mg/​ml//
Spe­cif­ic activity≥3800 USP units/​mg pro.≥3800 (U/​mg protein)≥2500 USP units/​mg pro.≥4500 USP units/​mg pro.
RP-HPLC/β-trypsin≥70%,α-trypsin ≤20%/≥95%
E. Coli host Cell pro­tein residue/≤0.01%//
Host Cell DNA residues/≤ 10 ng/​mg//
Puri­ty(SDS-PAGE)Sin­gle major band//Sin­gle major band
Mol­e­c­u­lar Weight(SDS-PAGE)24.0±2.4 kDa//24.0±2.4 kDa
Unit def­i­n­i­tionOne USP unit of trypsin activ­i­ty will pro­duce a Delta A253 of 0.003 per minute in a reac­tion vol­ume of 3.2ml at pH7.6 and 25℃, with BAEE as a sub­strate (1cm light path).One USP unit of trypsin activ­i­ty will pro­duce a Delta A253 of 0.003 per minute in a reac­tion vol­ume of 3.2ml at pH7.6 and 25℃, with BAEE as a sub­strate (1cm light path).//
Activ­i­ty unit25℃, pH7.6, 3.2 ml reac­tion solution(1 cm light path), one trypsin unit (USP) was defined as an increase of 0.003 in the absorp­tion val­ue at 253 nm by enzy­mat­ic hydrol­y­sis of BAEE per minute.
Rec­om­mend­ed usageThe ratio to aimed pro­tein is 1:50 to 1:1000 (w/w).The opti­mum pH is pH7.0-11.0.Pre­pare 1-10mg/ml recom­bi­nant human trypsin .The ratio to aimed pro­tein is 1:50 to 1:1000 (w/w).The opti­mum pH is pH7.0-11.0.It is rec­om­mend­ed to dis­solve or dilute with 50 mM HAc. When used, dilute in 50 mM NH4HCO3 or ph7.0-8.0 buffer solu­tion. 1 mM CaClis rec­om­mend­ed In the diges­tion buffer. The ratio to aimed pro­tein is 1:50 to 1:1000 (w/w).The opti­mum pH is pH7.0-8.0.
Sta­bil­i­ty of stor­age and transportRecom­bi­nant trypsin lyophilized should be stored under 2-8℃ in sealed con­tain­er.
It is sta­ble with­in 24 months.After dis­solved with 50mM HAC, it should be stored under -20℃. It is no activ­i­ty loss after 10 times repeat­ed freez­ing and thaw­ing.
The prod­uct is sta­ble by blue ice insu­la­tion transport.
The recom­bi­nant trypsin solu­tion was stored under -20℃ and was sta­ble for 12 months ;
Dry ice insu­la­tion trans­porta­tion, won’t melt dur­ing trans­porta­tion, sta­ble activity.
Recom­bi­nant human trypsin lyophilized should be stored under 2-8℃ in sealed con­tain­er. It is sta­ble with­in 24 months​.It is no activ­i­ty loss after 10 times repeat­ed freez­ing and thaw­ing.
The prod­uct is sta­ble by blue ice insu­la­tion transport.
Sequenc­ing grade trypsin lyophilized should be stored under 2-8℃ in sealed con​tain​er​.It is sta­ble with­in 24 months.After dis­solved with 1mM HCl or 50mM HAC, it should be stored under -20℃. It is no activ­i­ty loss after 5 times repeat­ed freez­ing and thaw­ing.
The prod­uct is sta­ble by blue ice insu­la­tion transport.
UsageThe amino acid sequence of recom­bi­nant trypsin is iden­ti­cal to porcine pan­creas-derived trypsin,with equiv­a­lent prop­er­ties com­pared to native trypsin .Recom­bi­nant trypsin can replace native trypsin for using in a vari­ety of biotech­no­log­i­cal processes,such as in insulin and vac­cine production.For cell cul­ture :
Tis­sue block diges­tion, pri­ma­ry cell acqui­si­tion ;
Pas­sage diges­tion of adher­ent cells ;
Cell cul­ture by micro­car­ri­er method ;
Gen­tly digest­ing stem cells ;
Immune cell ther­a­py, etc.
For recom­bi­nant pro­tein :
Recom­bi­nant insulin pro­duc­tion ;
Pro­tein sequenc­ing, pep­tide map­ping ;
Spe­cif­ic pro­te­olyt­ic process­es such as pro­teomics research.
Recom­bi­nant human trypsin is an endopep­ti­dase that can be used for lysine and argi­nine C-ter­mi­­nal cleav­age of pep­tide bonds to cleave macro­mol­e­cules into small pep­tides. Recom­bi­nant human trypsin is wide­ly used in a vari­ety of biotech­no­log­i­cal process­es, such as : cell cul­ture cell sep­a­ra­tion of var­i­ous tis­sues ; degra­da­tion of dena­tured pro­teins ; enzy­mat­ic hydrol­y­sis, sequenc­ing ; stem cell ther­a­py ; tumor cell therapy.The amino acid sequence of sequenc­ing grade recom­bi­nant trypsin is iden­ti­cal to porcine pan­creas-derived trypsin,with equiv­a­lent prop­er­ties com­pared to native trypsin, and there are many advan­tages, such as no enzyme activ­i­ty, high sta­bil­i­ty, non-self-cut­t­ing, high activity.When used, it is no non-spe­­cif­ic frag­ments and self-cut­t­ing fragments.Sequencing grade recom­bi­nant trypsin can replace native trypsin for using in a vari­ety of biotech­no­log­i­cal processes,such as spe­cif­ic pro­tein diges­tion, pro­tein sequenc­ing, pep­tide map­ping, pro­teomics stud­ies, Z-D pep­tides on the pep­ti­dase digestion.
SourceRecom­bi­nant trypsin is a genet­i­cal­ly engi­neered pro­tein expressed in E.coliRecom­bi­nant Trypsin (Porcine), pro­duced by genet­ic engi­neer­ing, have the same amino acid sequence as the porcine pan­creas trypsin.Recom­bi­nant human trypsin is a genet­i­cal­ly engi­neered pro­tein expressed in E.coliSequenc­ing grade mod­i­fied trypsin is a genet­i­cal­ly engi­neered methy­la­tion mod­i­fied pro­tein expressed in E.coli

Advan­tage

  1. Ani­mal ori­gin free : recom­bi­nant trypsin is no exoge­nous virus contamination,and any ani­mal ori­gin mate­r­i­al is not used in the pro­duc­tion process.
  2. Sta­ble qual­i­ty : Mass pro­duc­tion can ensure sta­ble and con­tin­u­ous batch pro​duc​tion​.It is no dif­fer­ence between the batch and the prod­uct qual­i­ty is stable.
  3. High puri­ty : High­er spe­cif­ic activ​i​ty​.Host pro­tein residues is less than the lim­its of bio­log­i­cal products.
  4. Lyophilized pow­der : The prod­uct is lyophilized pow­der and is easy to store and transport.
This prod­uct is devel­oped by our R&D com­pa­ny Wat­son Bio Ltd(https://​www​.wat​son​-bio​.com/), and here is the cor­re­spond­ing linkhttps://​www​.wat​son​-bio​.com/​r​e​c​o​m​b​i​n​a​n​t​-​t​r​y​p​s​i​n​-​e​c​-​3​-​4​-​2​1​-​4​-​c​a​s​-​9​0​0​2​-​0​7​-7/

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