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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:
Bartonella 26kDa
- 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:
50ug/100ug/1mg
| 规格: | 50ug | 产品价格: | ¥10143.0 |
|---|---|---|---|
| 规格: | 100ug | 产品价格: | ¥14500.0 |
| 规格: | 1mg | 产品价格: | ¥87906.0 |

CATALOGUE NUMBER
PRO-2569
INTRODUCTION
Numerous forms of Bartonellosis are caused by Bartonella henselae as well as Cat Scratch Disease & Bacillary Angiomatosis. It has been found that up to 95% of patients with Cat Scratch Disease show antibodies against Bartonella henselae antigens.
Highly immunoreactive proteins which are produced by the Bartonella henselae are the most important antigens used for the diagnosis of Cat Scratch Disease.
Bartonella henselae of outer membrane protein p26 has an important nucleotide identity with orthologs in Bartonella spp, Br.uc.ell.a spp in addition to more than a few plant-associated bacteria.
DESCRIPTION
Recombinant Bartonella Henselae 26kDa produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 25kDa.
Bartonella 26kDa is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.
SOURCE
Escherichia Coli.
PHYSICAL APPEARANCE
FORMULATION
Bartonella 26kDa is supplied at a 20mM HEPES buffer pH-8.0, 200mM NaCl and 20% Glycerol.
STABILITY
Store at 4°C if entire vial will be used within 2-4 weeks.
Store, frozen at -20°C for longer periods of time.
Avoid multiple freeze-thaw cycles.
PURITY
Greater than 95% as determined by SDS-PAGE.
SAFETY DATA SHEET
SDS
USAGE
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文献和实验Recombinant Bartonella Henselae 26kDa produced in E.Coli is a single, non-glycosylated polypeptide chain having a molecular mass of 25kDa.
Bartonella 26kDa is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.
Bartonella henselae is the causative agent of cat-scratch disease (CSD), usually presenting itself as a �self-limiting lymphadenopathy. In this chapter an internally controlled Taqman probe-based real-time PCR targeting the groEL gene
The Use of a Flagellar Export Signal for the Secretion of Recombinant Proteins in Salmonella
within the disordered N-terminal region of flagellar axial proteins are recognized by the flagellum-specific export apparatus. Recently, we have demonstrated that the 26–47 segment of Salmonella typhimurium flagellin is capable of mediating flagellar export. N-terminal
Purification of Recombinant Chemokines from E. coli
The majority of chemokines are highly basic, small proteins, with a molecular mass of around 8–10 kDa. Although they do not necessarily have a high level of homology at the primary sequence level, which can be as low as 20
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