Structure of Recombinant V8 protease EC 3.4.21.19 CAS 66676 43 5 - Recombinant V8 protease EC 3.4.21.19 CAS 66676-43-5

Iden­ti­fi­ca­tion

CAS Number

66676-43-5

EC Number

3.4.21.19

Name

Recom­bi­nant V8 protease

Syn­onyms

STAPHY­LO­COC­CAL SER­INE PRO­TEASE PRO­TEASE V8 ;
STAPHY­LO­COC­CAL SER­INE PRO­TEINASE ;
PRO­TEASE V8 ;
PRO­TEASE, S AUREUS ;
PRO­TEASE TYPE XVII-B ;
V8 PRO­TEASE ;
EC 3.4.21.19 ;
ENDO­PRO­TEINASE GLU-C

EINECS

620-751-3

Prop­er­ties

Appear­ance

White or off white, or yel­low­ish powder

Safe­ty Data

Per­son­al Pro­tec­tive Equipment

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

RIDADR 

NONH for all modes of transport

WGK Germany

3

Spec­i­fi­ca­tions and Oth­er Infor­ma­tion of Our Recom­bi­nant V8 pro­tease EC 3.4.21.19 CAS 66676-43-5

Puri­ty(SDS-PAGE)

Sin­gle major band

Spe­cif­ic activity

≥ 5.0 AU /​mg pro

Mol­e­c­u­lar Weight(SDS-PAGE)

24.0±2.4 kDa

Unit def­i­n­i­tion

One unit is defined as the amount of enzyme required to cat­alyt­ic sub­strate Z-Phe-Leu-Glu-4-nitranilide pro­duced 1μmol of 4-nitroani­­line per minute at 25°C and pH 7.8

Descrip­tion

Recom­bi­nant V8 pro­tease is the ser­ine pro­tease fam­i­ly and can specif­i­cal­ly hydrolyz­ing glu­tam­ic acid or aspar­tic acid residues car­boxy side pep­tide bonds. The Glu car­boxy ter­mi­nal pep­tide bond can be iden­ti­fied and cleaved in CH4COONHbuffer (pH 7.8) and NH4HCO(pH 4.0 ).Iden­ti­fy and cleave the Glu or Asp car­boxy ter­mi­nal pep­tide bond in phos­phate buffer (pH 7.8),and the hydrol­y­sis rate of Glu was high­er than that of Glu Asp. Recom­bi­nant V8 pro­tease has activ­i­ty between pH 4.0-10.0, and the opti­mum pH is 8.0-8.5. It can be used alone or in com­bi­na­tion with oth­er pro­teas­es when used in pro­tein diges­tion, pep­tide pro­fil­ing and pep­tide mass fin­ger­print­ing analy­sis. The inhibitors of V8 pro­tease are diiso­propy­l­flu­o­rophos­phate (DFP), α2-macroglob­u­lin and Nα-P-tosyl-L-lysine chloromethyl ketone (TLCK).

Source

Recom­bi­nant V8 pro­tease is a genet­i­cal­ly engi­neered pro­tein expressed in E.coli

Pro­tein Sequence

The amino acid sequence of recom­bi­nant trypsin is iden­ti­cal to porcine pan­creas-derived trypsin

Rec­om­mend­ed usage

Note that before using : (1) Divide the mate­r­i­al in accord­ing to usage quan­ti­ty to avoid pol­lu­tion or self-cut­t­ing. (2) Dis­solve tar­get pro­tein.
The tar­get pro­tein is dis­solved by cleav­age buffer, for exam­ple 25-50 mM NH4HCO3 pH 7.8, if the sol­u­bil­i­ty of tar­get pro­tein is not good, the tar­get pro­tein will be dena­tured by adding urea, SDS, DTT or heat­ing. The effects of urea and SDS on V8 pro­tease are shown in.(3) Digest : The rec­om­mend­ed ratio of V8 pro­tease and tar­get pro­tein is 1:20-1:100 (W/W).At 25 °C or 37 °C digest the pro­tein 2-18h.

Sta­bil­i­ty of storage

Recom­bi­nant V8 pro­tease should be stored under 2-8°C in sealed con​tain​er​.It is sta­ble with­in 6 months after dis­solved with1mM HCl and 50mM HAC at -20°C or below. It is sta­ble with­in 2 months after dis­solved with 1mM HCl and 50mM HAC at 4°C.85% activ­i­ty above can be kept after dis­solved with 1mM HCl and 50mM HAC at 25°C or 37°C 12h. It is no activ­i­ty loss after 10 times repeat­ed freez­ing and thawing.

Sta­bil­i­ty of transport

The prod­uct is sta­ble by blue ice insu­la­tion transport.

Advan­tage

1.Sequence grade recom­bi­nant pro­tein : high specificity,good sta­bil­i­ty.
2.Animal ori­gin free : Recom­bi­nant V8 Pro­tease is no exoge­nous virus contamination,and any ani­mal ori­gin mate­r­i­al is not used in the pro­duc­tion process.
3.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.
4.High puri­ty : High­er spe­cif­ic activ​i​ty​.Host pro­tein residues is less than the lim­its of bio­log­i­cal products.

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​-​v​8​-​p​r​o​t​e​a​s​e​-​e​c​-​3​-​4​-​2​1​-​1​9​-​c​a​s​-​6​6​6​7​6​-​4​3​-5/

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