Recombinant-Bacillus-subtilis-
Branched-chain-amino-acid-transport-protein-AzlDazlDBranched-chain amino acid transport protein AzlD- ￥9758
- CUSABIO
- CN
- CSB-CF519220BRJ
- 2025年07月14日
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- 详细信息
- 文献和实验
- 技术资料
- 保存条件：
"-20°C/-80°C"
- 保质期：
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
- 英文名：
Customized Bacillus subtilis azlD Protein (in vitro E.coli)
- 库存：
200
- 供应商：
武汉华美生物工程有限公司
- 规格：
20ug
Alternative Name(s)
Branched-chain amino acid transport protein AzlDEditorial/Sponsord
EditorialUniprot ID
O07923Gene Names
azlDOrganism
Bacillus subtilisAASequence
MTMTMTQQMITIAMVVLGTMLTRFLPFMIFPSGKPTPKYVQYLGKVLPSAVIGLLVIYCL KDVSLLSGSHGIPELVGAAAVVLLHLWKKNMLLSIAGGTVVYMVLVQLVFExpression Region
1-110aaSequence Info
Full lengthSource
in vitro E.coliSource Notice
Mammalian cell expression systems and other species are available. Please inquire.Tag Info
InquireMW
InquireList Price
1394Purity
Greater than 85% as determined by SDS-PAGE.Storage Buffer
Tris/PBS-based buffer, 6% TrehaloseStorage
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.Endotoxin
Not Test. Endotoxin removal service is available for free upon you request.产品类型
Transmembrane-Protein备注
**产品信息可能有变动，请以官网信息为准
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文献和实验**产品信息可能有变动，请以官网信息为准
concentrations. D-Amino acid treatment caused the release of amyloid fibers that linked cells in the biofilm together. Mutants able to form biofilms in the presence of D-Amino acids contained alterations in a protein (YqxM) required for the formation
-ribose) modification. As a result, the accurate determination of poly(ADP-ribosyl)ation amino acid specificity, as well as, a detailed characterization of the structural �complexity of the protein-bound ADP-ribose polymers generated, e.g., linear
Assay for Protein Modification by Poly-ADP-Ribose In Vitro
Glu, Asp, and/or Lys residues within the target protein. Identification of the unique amino acid acceptors of pADPr in these nuclear proteins is an active area of study. Because of the heterogeneity of pADPr chain on modified �protein targets
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