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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 Caenorhabditis elegans dhhc-4 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)
Uncharacterized protein ZK757.4Editorial/Sponsord
EditorialUniprot ID
Q8I0G4Gene Names
dhhc-4Organism
Caenorhabditis elegansAASequence
MSCRDCTRKGGCVYTTFWLVRFLPVVLVSLATGWGIYAYTYELCILSIDNWPQRIIYLFI FYALLILFYTSYLRTVYTKAWKPPQKYCIEGASKATYESVKDDERQLQLFLSDIARERDL TLLVRGFDHGIRFCDKCCCIKPDRSHHCSMCEQCVLKFDHHCPWVNNCVNFGNYKYFILF LAYGFIFCIWIAATTLPSFIDFWRHEYDMNKKQYDSIDSVIQRNLKHLHTVLSNGRFPLV FLLFLSCMFSLSLSFLFFYHLYLTAKNRTTVESFRAPMIDGKYAKDAFNHGIRANYREIF GSHPLYWFLPVPSSIGDGCKFVMNDMTAMSAAAGNQVFVEMGNVPNGQSHAHPPIAQHHI NLYSEQSSSASEKEIKSVDDEITERSQVSTATTASPSHDSVTAExpression Region
1-403aaSequence Info
Full lengthSource
in vitro E.coliSource Notice
Mammalian cell expression systems and other species are available. Please inquire.Tag Info
InquireMW
InquireList Price
1766Purity
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
in the electrophoretic mobility of a DNA fragment when bound to an interacting protein. The assay can be used to test DNA binding of either purified or recombinant proteins or uncharacterized binding activities present in crude protein extracts from plant cells or nuclei
Protein Secondary Structure Prediction
developed for predicting protein structure from the amino acid sequence. The first of the four sections is an overview and brief history of structure prediction schemes. The second section describes four distinct prediction schemes, with emphasis
between crystals of protein?nucleic acid complexes and those containing protein alone is a common problem in structural studies of protein?nucleic acid interactions. Currently, there are several methods available for detecting nucleic acid in crystals, including
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