LNPEP Protein (AA 155-1025) (rho-1D4 tag)

Catalog No. ABIN3093475

Product Details

Target: LNPEP (Leucyl/cystinyl Aminopeptidase (LNPEP))

Protein Type: Recombinant

Protein Characteristics: AA 155-1025

Origin: Human

Source: Insect Cells

Purification tag / Conjugate: This LNPEP protein is labelled with rho-1D4 tag.

Application: Western Blotting (WB), SDS-PAGE (SDS), ELISA, Crystallization (Crys)

Sequence: ATNGKLFPWA QIRLPTAVVP LRYELSLHPN LTSMTFRGSV TISVQALQVT WNIILHSTGH NISRVTFMSA VSSQEKQAEI LEYAYHGQIA IVAPEALLAG HNYTLKIEYS ANISSSYYGF YGFSYTDESN EKKYFAATQF EPLAARSAFP CFDEPAFKAT FIIKIIRDEQ YTALSNMPKK SSVVLDDGLV QDEFSESVKM STYLVAFIVG EMKNLSQDVN GTLVSIYAVP EKIGQVHYAL ETTVKLLEFF QNYFEIQYPL KKLDLVAIPD FEAGAMENWG LLTFREETLL YDSNTSSMAD RKLVTKIIAH ELAHQWFGNL VTMKWWNDLW LNEGFATFME YFSLEKIFKE LSSYEDFLDA RFKTMKKDSL NSSHPISSSV QSSEQIEEMF DSLSYFKGSS LLLMLKTYLS EDVFQHAVVL YLHNHSYASI QSDDLWDSFN EVTNQTLDVK RMMKTWTLQK GFPLVTVQKK GKELFIQQER FFLNMKPEIQ PSDTSYLWHI PLSYVTEGRN YSKYQSVSLL DKKSGVINLT EEVLWVKVNI NMNGYYIVHY ADDDWEALIH QLKINPYVLS DKDRANLINN IFELAGLGKV PLKRAFDLIN YLGNENHTAP ITEALFQTDL IYNLLEKLGY MDLASRLVTR VFKLLQNQIQ QQTWTDEGTP SMRELRSALL EFACTHNLGN CSTTAMKLFD DWMASNGTQS LPTDVMTTVF KVGAKTDKGW SFLLGKYISI GSEAEKNKIL EALASSEDVR KLYWLMKSSL NGDNFRTQKL SFIIRTVGRH FPGHLLAWDF VKENWNKLVQ KFPLGSYTIQ NIVAGSTYLF STKTHLSEVQ AFFENQSEAT FRLRCVQEAL EVIQLNIQWM EKNLKSLTWW L
Sequence without tag. Tag location is at the discretion of the manufacturer. If you have a special request, please contact us.

Characteristics:

• Made in Germany - from design to production - by highly experienced protein experts.
• Human LNPEP 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: Three step purification of membrane proteins expressed in baculovirus infected SF9 insect cells:

1. Membrane proteins are fractioned by ultracentrifugation and subsequently solubilized with different detergents (detergent screen). Samples are analyzed by Western blot.
2. 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.
3. 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

Application Details

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:

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

Handling

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)

Target Details

Target: LNPEP (Leucyl/cystinyl Aminopeptidase (LNPEP))

Alternative Name: LNPEP (LNPEP Products)

Synonyms: fb73h12 Protein, wu:fb73h12 Protein, zgc:66103 Protein, 2010309L07Rik Protein, 4732490P18Rik Protein, CAP Protein, IRAP Protein, PLAP Protein, gp160 Protein, vp165 Protein, P-LAP Protein, Vp165 Protein, LNPEP Protein, leucyl and cystinyl aminopeptidase Protein, leucyl/cystinyl aminopeptidase L homeolog Protein, leucyl/cystinyl aminopeptidase Protein, LNPEP Protein, lnpep.L Protein, lnpep Protein, Lnpep Protein

Background: Release of an N-terminal amino acid, cleaves before cysteine, leucine as well as other amino acids. Degrades peptide hormones such as oxytocin, vasopressin and angiotensin III, and plays a role in maintaining homeostasis during pregnancy. May be involved in the inactivation of neuronal peptides in the brain. Cleaves Met-enkephalin and dynorphin. Binds angiotensin IV and may be the angiotensin IV receptor in the brain. {ECO:0000269|PubMed:11389728, ECO:0000269|PubMed:11707427, ECO:0000269|PubMed:1731608}.

Molecular Weight: 101.2 kDa Including tag.

UniProt: Q9UIQ6

Pathways: Regulation of long-term Neuronal Synaptic Plasticity