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- Prospecbio
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- enz-135
- 2026年01月08日
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- 详细信息
- 文献和实验
- 技术资料
- 保存条件：
for future use below -18°C
- 保质期：
See instructions
- 英文名：
TPX
- 库存：
常规产品有备货
- 供应商：
上海经科化学科技有限公司
- CAS号：
无
- 规格：
5ug/20ug/1mg
| 规格： | 5ug | 产品价格： | ￥1080.0 |
|---|---|---|---|
| 规格： | 20ug | 产品价格： | ￥2415.0 |
| 规格： | 1mg | 产品价格： | ￥45885.0 |
CATALOGUE NUMBER
ENZ-135
SYNONYMS
Thiol peroxidase, Scavengase P20, tpx, yzzJ, b1324, JW1317.
INTRODUCTION
Lipid hydroperoxide peroxidase (TPX) belongs to the peroxiredoxin family of antioxidant enzymes, which reduce hydrogen peroxide and alkyl hydroperoxides. TPX has an imperative role in thioredoxin peroxidase activity.
DESCRIPTION
TPX produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-168 a.a.) and having a molecular mass of 19.9kDa.
TPX is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
SOURCE
PHYSICAL APPEARANCE
FORMULATION
STABILITY
TPX E.Coli Recombinant although stable at 4°C for 1 week, should be stored below -18°C.
Please prevent freeze thaw cycles.
PURITY
AMINO ACID SEQUENCE
MG./S-SHHHHHH SSGLVPRGSH MSQTVHFQGN PVTVANSIPQ AGSKAQTFTL VAKDLSDVTL GQFAGKRKVL NIFPSIDTGV CAASVRKFNQ LATEIDNTVV LCISADLPFA QSRFCGAEGL NNVITLSTFR NAEFLQAYGV AIADGPLKGL AARAVVVIDE NDNVIFSQLV DEITTEPDYE AALAVLKA.
SAFETY DATA SHEET
SDS
USAGE
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文献和实验TPX produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-168 a.a.) and having a molecular mass of 19.9kDa.
TPX is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Generation of Recombinant Baculovirus DNA in E.coli Using a Baculovirus Shuttle Vector
of the Autographa californica nuclear polyhedrosis virus (AcNPV) are abundantly expressed during the late stages of infection. The recombinant proteins are usually soluble and functionally similar to their authentic counterparts (l –7 ). In the following sections
Expression of Recombinant Cytochromes c in E. coli
for proper folding and stability. However, significant advances in expression of recombinant cytochromes c have been made during the last decade. It has been shown that a single gene cluster, ccmA–H , is responsible for cytochrome c maturation in Escherichia
Expression of Recombinant Alkaline Phosphatase Conjugates in Escherichia coli
The methods described in this article are relative to the use of a positive cloning/screening recombinant system for the generation in Escherichia coli of foreign proteins fused to a highly active bacterial alkaline phosphatase (PhoA) variant
技术资料
