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NCBI References of Lab recombinants

HAMSTER ANTI HUMAN EMR1
MBS224708-02mg MyBiosource 0.2mg 500 EUR
HAMSTER ANTI HUMAN EMR1
MBS224708-5x02mg MyBiosource 5x0.2mg 2070 EUR
HAMSTER ANTI HUMAN EMR1:RPE
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HAMSTER ANTI HUMAN EMR1:RPE
MBS224415-5x100Tests MyBiosource 5x100Tests 2160 EUR
Emr1/ Rat Emr1 ELISA Kit
ELI-04863r Lifescience Market 96 Tests 1063.2 EUR
Anti-Human ADGRE1/EMR1 Antibody
MBS1569564-01mg MyBiosource 0.1mg 405 EUR
Anti-Human ADGRE1/EMR1 Antibody
MBS1569564-5x01mg MyBiosource 5x0.1mg 1520 EUR
EMR1
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EMR1 Antibody
8G090 AAT Bioquest 50ug 368 EUR
EMR1 antibody
70R-21531 Fitzgerald 50 ul 289 EUR
EMR1 antibody
70R-31369 Fitzgerald 100 ug 294 EUR
EMR1 antibody
70R-12624 Fitzgerald 100 ul 550 EUR
EMR1 Antibody
ABD4874 Lifescience Market 100 ug 525.6 EUR
EMR1 Antibody
ABD2789 Lifescience Market 100 ug 525.6 EUR
EMR1 antibody
22512 SAB 100ul 479 EUR
EMR1 antibody
22512-100ul SAB 100ul 468 EUR
emr1 Antibody
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emr1 Antibody
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EMR1 Antibody
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EMR1 Antibody
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EMR1 Antibody
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EMR1 Antibody
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EMR1 Antibody
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EMR1 Antibody
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EMR1 Antibody
E11-090G EnoGene 100μg 225 EUR
EMR1 Antibody
E38PA6191 EnoGene 100ul 225 EUR
EMR1 Antibody
E19-4874 EnoGene 100μg/100μl 225 EUR
EMR1 Antibody
MBS5311834-01mL MyBiosource 0.1mL 1070 EUR
EMR1 Antibody
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emr1 Antibody
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EMR1 Antibody
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EMR1 Antibody
MBS7118176-01mg MyBiosource 0.1mg 190 EUR
EMR1 Antibody
MBS7118176-5x01mg MyBiosource 5x0.1mg 845 EUR
EMR1 Antibody
MBS8515576-01mg MyBiosource 0.1mg 305 EUR
EMR1 Antibody
MBS8515576-01mLAF405L MyBiosource 0.1mL(AF405L) 465 EUR
EMR1 Antibody
MBS8515576-01mLAF405S MyBiosource 0.1mL(AF405S) 465 EUR
EMR1 Antibody
MBS8515576-01mLAF610 MyBiosource 0.1mL(AF610) 465 EUR
EMR1 Antibody
MBS8515576-01mLAF635 MyBiosource 0.1mL(AF635) 465 EUR
EMR1 Antibody
MBS9606326-01mL MyBiosource 0.1mL 260 EUR
EMR1 Antibody
MBS9606326-02mL MyBiosource 0.2mL 305 EUR
EMR1 Antibody
MBS9606326-5x02mL MyBiosource 5x0.2mL 1220 EUR
EMR1 Antibody
MBS9604303-01mL MyBiosource 0.1mL 260 EUR
EMR1 Antibody
MBS9604303-02mL MyBiosource 0.2mL 305 EUR
EMR1 Antibody
MBS9604303-5x02mL MyBiosource 5x0.2mL 1220 EUR
EMR1 Antibody
MBS8583880-01mL MyBiosource 0.1mL 305 EUR
EMR1 Antibody
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EMR1 Antibody
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EMR1 Antibody
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EMR1 Antibody
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EMR1 Antibody
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EMR1 Antibody
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EMR1 Antibody
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EMR1 Antibody
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EMR1 Antibody
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EMR1 antibody
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EMR1 antibody
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EMR1 Antibody
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EMR1 Antibody
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EMR1 Antibody
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EMR1 Antibody
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EMR1 Antibody
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EMR1 Antibody
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EMR1 Antibody (RPE)
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EMR1 (AP)
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EMR1 (AP)
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EMR1 (HRP)
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Rat Cholesterol ELISA ELISA

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Goat Cholesterol ELISA ELISA

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Goat Cholesterol ELISA ELISA

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Mouse Cholesterol ELISA ELISA

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Human Cholesterol ELISA ELISA

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Our used recombinants in Pubmed.

rec Leptin (mouse)

4038284.02 Bachem 0.2 mg 102.27 EUR

rec Leptin (mouse)

4038284.1 Bachem 1 mg 271.85 EUR

rec Leptin (human)

H-5578.0200 Bachem 0.2mg 194.4 EUR

rec Leptin (human)

H-5578.1000 Bachem 1.0mg 457.2 EUR

rec Leptin (mouse)

H-5582.0200 Bachem 0.2mg 194.4 EUR

Lab Equipment including Hot Plates MediaStirrers

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K26 AB Vector LLC 1 Kit
Description: Protein expression

BV-Tau412. Recombinant baculovirus expressing 412 aa Tau isoform.

PD13 AB Vector LLC 1 ml
Description: Drug discovery, Protein folding diseases, baculovirus

BV-Tau412TR. Recombinant baculovirus expressing 412 aa Tau isoform. T39-R mutant.

PD14 AB Vector LLC 1 ml
Description: Drug discovery, Protein folding diseases, baculovirus

BV-Tau412KE. Recombinant baculovirus expressing 412 aa Tau isoform. K267-E mutant.

PD15 AB Vector LLC 1 ml
Description: Drug discovery, Protein folding diseases, baculovirus

BV-Synuclein. Recombinant baculovirus expressing alpha synuclein.

PD17 AB Vector LLC 1 ml
Description: Drug discovery, Protein folding diseases, baculovirus

BV-Syn-GFP. Recombinant baculovirus expressing alpha synuclein-GFP fusion.

PD21 AB Vector LLC 1 ml
Description: Drug discovery, Protein folding diseases, baculovirus

anti- Antibody^Polyclonal antibody control antibody

LSMab09882 Lifescience Market 100 ug 525.6 EUR

Lck antibody Antibody

GWB-250026 GenWay Biotech 0.05 ml Ask for price

H2B Antibody Antibody

E11-184659 EnoGene 100ug/100ul 225 EUR

H2B Antibody Antibody

MBS8529199-01mg MyBiosource 0.1mg 305 EUR

H2B Antibody Antibody

MBS8529199-01mLAF405L MyBiosource 0.1mL(AF405L) 465 EUR

H2B Antibody Antibody

MBS8529199-01mLAF405S MyBiosource 0.1mL(AF405S) 465 EUR

H2B Antibody Antibody

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H2B Antibody Antibody

MBS8529199-01mLAF635 MyBiosource 0.1mL(AF635) 465 EUR

Our used rec. in Pubmed.

Monoclonal DAO Antibody (monoclonal) (M01), Clone: 2F5

APR07497G Leading Biology 0.1mg 580.8 EUR

Monoclonal DLD Antibody (monoclonal) (M02), Clone: 3C1

APR07594G Leading Biology 0.1mg 580.8 EUR

Monoclonal DLD Antibody (monoclonal) (M05), Clone: 2D4

APR07595G Leading Biology 0.1mg 580.8 EUR

Monoclonal E2F8 Antibody (monoclonal) (M01), Clone: S1

APR07633G Leading Biology 0.1mg 580.8 EUR

Monoclonal HPD Antibody (monoclonal) (M07), Clone: 2F3

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NCBI Reference

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Monoclonal GR monoclonal antibody

AMM00029G Leading Biology 0.05mg 633.6 EUR

Monoclonal TBP monoclonal antibody

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Monoclonal EZH2 monoclonal antibody

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Monoclonal Rsf1 monoclonal antibody

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Monoclonal Rsf1 monoclonal antibody

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Monoclonal SirT1 monoclonal antibody

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Monoclonal HDAC2 monoclonal antibody

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Our used monoclonals in Pubmed.

Monoclonal DAO Antibody (monoclonal) (M01), Clone: 2F5

APR07497G Leading Biology 0.1mg 580.8 EUR

Monoclonal DLD Antibody (monoclonal) (M02), Clone: 3C1

APR07594G Leading Biology 0.1mg 580.8 EUR

Monoclonal DLD Antibody (monoclonal) (M05), Clone: 2D4

APR07595G Leading Biology 0.1mg 580.8 EUR

Monoclonal E2F8 Antibody (monoclonal) (M01), Clone: S1

APR07633G Leading Biology 0.1mg 580.8 EUR

Monoclonal HPD Antibody (monoclonal) (M07), Clone: 2F3

APR07791G Leading Biology 0.1mg 580.8 EUR

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Suppliers for Lab recombinants

MEK3 Rabbit Rabbit Polyclonal Antibody

ES8567-100ul ELK Biotech 100ul
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Nrf2 Rabbit Rabbit Polyclonal Antibody

ES8568-100ul ELK Biotech 100ul
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Nrf2 Rabbit Rabbit Polyclonal Antibody

ES8568-50ul ELK Biotech 50ul
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ATG5 Rabbit Rabbit Polyclonal Antibody

ES8572-100ul ELK Biotech 100ul
Description: IHC

ATG5 Rabbit Rabbit Polyclonal Antibody

ES8572-50ul ELK Biotech 50ul
Description: IHC

ATG7 Rabbit Rabbit Polyclonal Antibody

ES8573-100ul ELK Biotech 100ul
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Polyclonal ETO polyclonal antibody

APR00372G Leading Biology 0.05ml 580.8 EUR

Polyclonal SHH Polyclonal Antibody

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Polyclonal ETO polyclonal antibody

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Polyclonal G9a polyclonal antibody

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Polyclonal YY1 polyclonal antibody

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Polyclonal PML polyclonal antibody

AMR09397G Leading Biology 0.05mg 580.8 EUR

Polyclonal RARA polyclonal antibody

APR00370G Leading Biology 0.05ml 580.8 EUR

Our used TESTs in Pubmed.

DNASE TEST AGAR

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HBcAb Test Card

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monoclonal Lab Reagents for Research



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Our used polyclonals in Pubmed.

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Our used polyclonals in Pubmed.

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MARKET SCK6 Bacillus subtilis Strains

Keratinase has an incredible business esteem inferable from its applications in the enzymatic dehairing of goatskins. In this review, we took on a consolidated methodology to upgrade the extracellular recombinant keratinase movement in Bacillus subtilis SCK6.

Initial, nine sign peptides were screened to upgrade the declaration of extracellular keratinase. The recombinant strain with SPLipA displayed the most elevated extracellular keratinase action of 739.03 U per mL, which was two-overlap higher action of the wild kind.

Second, in view of the various arrangement with the bacterial antacid proteases, the freak (M123L/V149I/A242N) was brought into the keratinase. Contrasting and the wild kind of keratinase, the freak M123L/V149I/A242N showed an expansion in the extracellular keratinase action, which was around 1.2-crease higher movement of the wild sort.

At last, the keratinase articulation vector with SPLipA and freak M123L/V149I/A242N was developed, and the extracellular keratinase action revealed at 830.91 U per mL was a 2.2-overlay action of the wild sort. Then, the freak keratinase was filtered and described. The freak displayed properties like those of the wild kind at an ideal temperature of 60 °C and pH 10.0. Decisively, the extracellular articulation of keratinase was upgraded by means of a joined technique, and the freak keratinase showed properties like that of the wild sort of keratinase.

Presentation

  1. Keratinolytic proteases are another age of proteolytic catalysts with a capacity to debase the headstrong keratin proteins, like plumes, horns, hooves, nails, and wool. These chemicals have been acquiring significance over the most recent couple of years for a considerable length of time applications, for example, in dehairing of stows away, materials and keratin squander the executives, and relationship with the hydrolysis of keratinous substrates.
  2.  Keratinolytic proteases are one of the amazing biocatalysts to hydrolyze the disulfide security rich proteins of hair and incur little harm to cowhide. Organic treatment with keratinolytic proteases could generally diminish the amount and poisonousness of wastewater gushing from the cowhide industry.
  3. Bacillus subtilis and Escherichia coli are the two significant hosts for cloning and overexpression of soluble proteases.
  4. B. subtilis is among the most generally involved has for protein creation in biotechnology inferable from its high proficiency of emission into the phone medium, high security, clear acquired foundations and mature maturation technology.
  5. The most ordinarily utilized technique to improve the extracellular articulation of proteins is the enhancement of the sign peptide.
  6. Yao et al. announced that the extracellular α-amylase action with an ideal sign peptide (SPYojL) was 3.5-crease more prominent than that of the control in the wake of screening the 173 sign peptides of B. subtilis. Essentially, the α-amylase-creating strain with the best-performing signal peptide (SPpel) yielded a limit of 1487.85 U per mL amylase after a 48 h development, and it was around 68.4% higher than that of the strain with the local sign peptide.
  7. Similar outcomes were found by Degering et al. at the point when the sign peptides with the 173 sign peptides of Bacillus subtilis and the 220 sign peptides of Bacillus licheniformis were screened, and the subtilisin BPN-delivering strain B. licheniformis H402 with the SPdBli00338 brought about a 9-overlap expansion in action in the medium supernatant when contrasted and the wild-type SP.
  8. Song et al. announced that the extracellular β-mannanase action with the ideal sign peptide (SPLipA) and 72 h of maturation was 533 ± 32 U for every mL after the screening of four sign peptides of Sec pathway and two sign peptides of the Tat pathway.10 moreover, the advancement of the sign peptide was additionally done to upgrade the extracellular creation of proteins, for example, L-asparaginase,11 β-galactosidase12 and xylanase.13
  9. In spite of the fact that improving the extracellular creation of protein by signal peptide improvement was plausible, anticipating the discharge effectiveness of various proteins with similar sign peptide and the particular sign peptide for the emission productivity of explicit proteins was troublesome. Also, there were a couple of reports to depict the adjustment of the developed protein to improve the extracellular articulation of catalyst.
  10. Coordinated advancement and site-coordinated mutagenesis were the most generally involved strategies for the change. Yao et al. portrayed that a recombinant B. subtilis containing a α-amylase with twofold change K82E/S405R showed a α-amylase movement, which was 2.1-overlap more prominent than that of the wild type.7 Feng et al. detailed that after the erasure of the N-terminal 25-buildups, the action of L-asparaginase with the sign peptide ASN was 100 percent higher than that of the intact.1
  11. However, a large portion of the freaks were built by working on the reactant properties, for example, activity,14 thermostability,cold adaptation17,18 and substrate specificity, concerning the alteration of the adult catalyst.

Already, a keratinase from Bacillus sp. LCB12, heterologously communicated by B. subtilis SCK6, was purged and portrayed. The portrayal of the recombinant keratinase uncovered that this protein was a serine protease with an ideal temperature of 60 °C and pH 10.0. The keratinase was utilized for the enzymatic dehairing of goatskins and displayed appealing properties that could create an effective and eco-accommodating enzymatic dehairing of creature skins or potentially conceals technique in the cowhide handling industry.20 However, the extracellular articulation of keratinase was low. In this review, the sign peptide streamlining and site-coordinated mutagenesis were utilized for further developing the extracellular recombinant keratinase movement.

Materials and strategies

Bacterial strains, plasmids and media

The strains in general and plasmids utilized in this study are summed up in Table 1. For cloning, plasmid pMA0911 and Escherichia coli DH5α were utilized. Bacillus subtilis SCK6 was utilized as the heterologous articulation host.21 Bacillus sp. LCB12 was recently detached from soluble soil.22 A LB-milk strong medium (tryptone 10 g L−1, yeast extricate 5 g L−1, NaCl 10 g L−1, non-fat powdered milk 20 g L−1, agar 20 g L−1, pH 7.2-7.4) was utilized for the utilitarian investigation of recombinant B. subtilis SCK6.

The recombinant B. subtilis SCK6 was hatched in a Luria-Bertani medium (tryptone 10 g L−1, yeast separate 5 g L−1, NaCl 10 g L−1, agar 20 g L−1, pH 7.2-7.4) at 37 °C and 200 rpm for the development of heterologous keratinase. When appropriate, anti-infection agents, for example, 100 μg mL−1 ampicillin, 50 μg mL−1 kanamycin and 1 μg mL−1 erythromycin, were utilized.

Plasmid development and change

The articulation vector pMA0911-keratinase was already constructed.20 The keratinase quality without the sign peptide was enhanced from pMA0911-keratinase utilizing the preliminaries KF/KR (Table 2), and the PCR items were processed utilizing limitation proteins EcoR I and BamH I. Then, the articulation vector pMA0911 with various sign peptides (SPYnc M, SPYwe A, SPNpr E, SPVpr, SPYvg O, SPYwb N, SPLip A, SPAmy X and SPWap A) was processed utilizing the limitation catalysts EcoR I and BamH I.

Native Bacillus licheniformis Keratinase, feed grade: 70,000 U/g

FEED-0001 Creative Enzymes 1kg 246 EUR

Native Bacillus licheniformis Protease: 7-15 Units/mg, lyophilized powder

NATE-0633 Creative Enzymes 100mg 1858 EUR

Bacillus licheniformis

PGPR-0009BF Creative BioMart 25 kg 2450 EUR

Bacitracin (BCT) ex. Bacillus Licheniformis

17327 Sisco Laboratories 50000 Units 10.8 EUR

α-Amylase from Bacillus licheniformis

abx071103-100mg Abbexa 100 mg 150 EUR

NADH Oxidase from Bacillus licheniformis

23626-52 NACALAI TESQUE 25UNITS 369.6 EUR

alpha Amylase from Bacillus licheniformis

20-abx082217 Abbexa
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  • 100 mg
  • 1 g

Recombinant Bacillus licheniformis Enolase (eno)

MBS1285574-002mgBaculovirus MyBiosource 0.02mg(Baculovirus) 1300 EUR

Recombinant Bacillus licheniformis Enolase (eno)

MBS1285574-002mgEColi MyBiosource 0.02mg(E-Coli) 980 EUR

Recombinant Bacillus licheniformis Enolase (eno)

MBS1285574-002mgYeast MyBiosource 0.02mg(Yeast) 1095 EUR

Recombinant Bacillus licheniformis Enolase (eno)

MBS1285574-01mgEColi MyBiosource 0.1mg(E-Coli) 1145 EUR

Recombinant Bacillus licheniformis Enolase (eno)

MBS1285574-01mgYeast MyBiosource 0.1mg(Yeast) 1245 EUR

Bacillus licheniformis Subtilisin Carlsberg (apr)

1-CSB-EP365470BQT Cusabio
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  • 10ug
  • 50ug
  • 100ug
  • 200ug
  • 500ug
  • 1MG

Recombinant Bacillus licheniformis GTPase obg (obg)

MBS1284438-002mgBaculovirus MyBiosource 0.02mg(Baculovirus) 1300 EUR

Recombinant Bacillus licheniformis GTPase obg (obg)

MBS1284438-002mgEColi MyBiosource 0.02mg(E-Coli) 980 EUR

Recombinant Bacillus licheniformis GTPase obg (obg)

MBS1284438-002mgYeast MyBiosource 0.02mg(Yeast) 1090 EUR

Recombinant Bacillus licheniformis GTPase obg (obg)

MBS1284438-01mgEColi MyBiosource 0.1mg(E-Coli) 1145 EUR

Recombinant Bacillus licheniformis GTPase obg (obg)

MBS1284438-01mgYeast MyBiosource 0.1mg(Yeast) 1240 EUR

The sanitized keratinase quality section was embedded into the comparing articulation vector pMA0911 by utilizing the Takara’s DNA ligation unit (Takara, Dalian, China). The ligation items were changed into E. coli DH5α cells. The positive clones were chosen and enhanced. Then, the plasmids were extricated and sequenced by Sangon Biotech (Shanghai, China). The recombinant plasmids were changed into B. subtilis SCK6 as indicated by the past description.20 Then, the capable cells were spread on the LB-milk strong medium with kanamycin (50 μg mL−1) for the practical investigation of the recombinant B. subtilis SCK6.