N-Cadherin Protein (AA 160-906) (rho-1D4 tag)
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- Target See all N-Cadherin (CDH2) Proteins
- N-Cadherin (CDH2) (Cadherin 2 (CDH2))
- Protein Type
- Recombinant
- Protein Characteristics
- AA 160-906
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Origin
- Human
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Source
- Insect Cells
- Purification tag / Conjugate
- This N-Cadherin protein is labelled with rho-1D4 tag.
- Application
- Western Blotting (WB), SDS-PAGE (SDS), ELISA, Crystallization (Crys)
- Sequence
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DWVIPPINLP ENSRGPFPQE LVRIRSDRDK NLSLRYSVTG PGADQPPTGI FIINPISGQL SVTKPLDREQ IARFHLRAHA VDINGNQVEN PIDIVINVID MNDNRPEFLH QVWNGTVPEG SKPGTYVMTV TAIDADDPNA LNGMLRYRIV SQAPSTPSPN MFTINNETGD IITVAAGLDR EKVQQYTLII QATDMEGNPT YGLSNTATAV ITVTDVNDNP PEFTAMTFYG EVPENRVDII VANLTVTDKD QPHTPAWNAV YRISGGDPTG RFAIQTDPNS NDGLVTVVKP IDFETNRMFV LTVAAENQVP LAKGIQHPPQ STATVSVTVI DVNENPYFAP NPKIIRQEEG LHAGTMLTTF TAQDPDRYMQ QNIRYTKLSD PANWLKIDPV NGQITTIAVL DRESPNVKNN IYNATFLASD NGIPPMSGTG TLQIYLLDIN DNAPQVLPQE AETCETPDPN SINITALDYD IDPNAGPFAF DLPLSPVTIK RNWTITRLNG DFAQLNLKIK FLEAGIYEVP IIITDSGNPP KSNISILRVK VCQCDSNGDC TDVDRIVGAG LGTGAIIAIL LCIIILLILV LMFVVWMKRR DKERQAKQLL IDPEDDVRDN ILKYDEEGGG EEDQDYDLSQ LQQPDTVEPD AIKPVGIRRM DERPIHAEPQ YPVRSAAPHP GDIGDFINEG LKAADNDPTA PPYDSLLVFD YEGSGSTAGS LSSLNSSSSG GEQDYDYLND WGPRFKKLAD MYGGGDD
Sequence without tag. Tag location is at the discretion of the manufacturer. If you have a special request, please contact us. - Characteristics
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- Made in Germany - from design to production - by highly experienced protein experts.
- Human CDH2 Protein (raised in Insect Cells) purified by multi-step, protein-specific process to ensure crystallization grade.
- State-of-the-art algorithm used for plasmid design (Gene synthesis).
This protein is a made to order protein and will be made for the first time for your order. Our experts in the lab will ensure that you receive a correctly folded protein.
The big advantage of ordering our made-to-order proteins in comparison to ordering custom made proteins from other companies is that there is no financial obligation in case the protein cannot be expressed or purified.
In the unlikely event that the protein cannot be expressed or purified we do not charge anything (other companies might charge you for any performed steps in the expression process for custom-made proteins, e.g. fees might apply for the expression plasmid, the first expression experiments or purification optimization).
When you order this made-to-order protein you will only pay upon receival of the correctly folded protein. With no financial risk on your end you can rest assured that our experienced protein experts will do everything to make sure that you receive the protein you ordered.
The concentration of our recombinant proteins is measured using the absorbance at 280nm. The protein's absorbance will be measured in several dilutions and is measured against its specific reference buffer.
The concentration of the protein is calculated using its specific absorption coefficient. We use the Expasy's protparam tool to determine the absorption coefficient of each protein.
- Purification
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Three step purification of membrane proteins expressed in baculovirus infected SF9 insect cells:
- Membrane proteins are fractioned by ultracentrifugation and subsequently solubilized with different detergents (detergent screen). Samples are analyzed by Western blot.
- The best performing detergent is used for solubilization and the proteins are purified via their rho1D4 tag via two rho1D4 antibody columns: one DTT resistant, the other one not. Eluate fractions are analyzed by Western blot.
- Protein containing fractions of the best purification are subjected to second purification step through size exclusion chromatograph. Eluate fractions are analyzed by SDS-PAGE and Western blot.
- Purity
- >95 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
- Sterility
- 0.22 μm filtered
- Endotoxin Level
- Protein is endotoxin-free.
- Grade
- Crystallography grade
- Top Product
- Discover our top product CDH2 Protein
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- Application Notes
- In addition to the applications listed above we expect the protein to work for functional studies as well. As the protein has not been tested for functional studies yet we cannot offer a gurantee though.
- Comment
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In cases in which it is highly likely that the recombinant protein with the default tag will be insoluble our protein lab may suggest a higher molecular weight tag (e.g. GST-tag) instead to increase solubility. We will discuss all possible options with you in detail to assure that you receive your protein of interest.
- Restrictions
- For Research Use only
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- Format
- Liquid
- Buffer
- 100 mM NaCL, 20 mM Hepes, 10% glycerol. pH value is at the discretion of the manufacturer.
- Handling Advice
- Avoid repeated freeze-thaw cycles.
- Storage
- -80 °C
- Storage Comment
- Store at -80°C.
- Expiry Date
- Unlimited (if stored properly)
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- Target
- N-Cadherin (CDH2) (Cadherin 2 (CDH2))
- Alternative Name
- CDH2 (CDH2 Products)
- Synonyms
- CD325 Protein, CDHN Protein, CDw325 Protein, NCAD Protein, N-cadherin Protein, cadherin-2 Protein, cdhn Protein, ncad Protein, cdw325 Protein, CDH2 Protein, Cadherin-2 Protein, Ncad Protein, glo Protein, lyr Protein, pac Protein, wu:fb47h04 Protein, cadherin 2 Protein, cadherin 2 S homeolog Protein, cadherin 2, type 1, N-cadherin (neuronal) Protein, CDH2 Protein, cdh2.S Protein, cdh2 Protein, Cdh2 Protein
- Background
- Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells, cadherins may thus contribute to the sorting of heterogeneous cell types. Acts as a regulator of neural stem cells quiescence by mediating anchorage of neural stem cells to ependymocytes in the adult subependymal zone: upon cleavage by MMP24, CDH2-mediated anchorage is affected, leading to modulate neural stem cell quiescence. CDH2 may be involved in neuronal recognition mechanism. In hippocampal neurons, may regulate dendritic spine density (By similarity). {ECO:0000250}.
- Molecular Weight
- 83.2 kDa Including tag.
- UniProt
- P19022
- Pathways
- Regulation of Muscle Cell Differentiation, Cell-Cell Junction Organization, Synaptic Membrane
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