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ERVW-1 Protein (AA 21-538) (rho-1D4 tag)

Crystallography grade ERVW-1 Origin: Human Host: Insect Cells Recombinant >95 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot. ELISA, WB, Crys, SDS
Catalog No. ABIN3095753
  • Target See all ERVW-1 Proteins
    ERVW-1 (Endogenous Retrovirus Group W, Member 1 (ERVW-1))
    Protein Type
    Recombinant
    Protein Characteristics
    AA 21-538
    Origin
    Human
    Source
    • 4
    • 1
    Insect Cells
    Purification tag / Conjugate
    This ERVW-1 protein is labelled with rho-1D4 tag.
    Application
    ELISA, Western Blotting (WB), Crystallization (Crys), SDS-PAGE (SDS)
    Sequence
    APPPCRCMTS SSPYQEFLWR MQRPGNIDAP SYRSLSKGTP TFTAHTHMPR NCYHSATLCM HANTHYWTGK MINPSCPGGL GVTVCWTYFT QTGMSDGGGV QDQAREKHVK EVISQLTRVH GTSSPYKGLD LSKLHETLRT HTRLVSLFNT TLTGLHEVSA QNPTNCWICL PLNFRPYVSI PVPEQWNNFS TEINTTSVLV GPLVSNLEIT HTSNLTCVKF SNTTYTTNSQ CIRWVTPPTQ IVCLPSGIFF VCGTSAYRCL NGSSESMCFL SFLVPPMTIY TEQDLYSYVI SKPRNKRVPI LPFVIGAGVL GALGTGIGGI TTSTQFYYKL SQELNGDMER VADSLVTLQD QLNSLAAVVL QNRRALDLLT AERGGTCLFL GEECCYYVNQ SGIVTEKVKE IRDRIQRRAE ELRNTGPWGL LSQWMPWILP FLGPLAAIIL LLLFGPCIFN LLVNFVSSRI EAVKLQMEPK MQSKTKIYRR PLDRPASPRS DVNDIKGTPP EEISAAQPLL RPNSAGSS
    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 ERVW-1 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
    Top Product
    Discover our top product ERVW-1 Protein
  • 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
  • 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
    ERVW-1 (Endogenous Retrovirus Group W, Member 1 (ERVW-1))
    Alternative Name
    ERVW-1 (ERVW-1 Products)
    Synonyms
    ENV Protein, ENVW Protein, ERVWE1 Protein, HERV-7q Protein, HERV-W-ENV Protein, HERV7Q Protein, HERVW Protein, HERVWENV Protein, endogenous retrovirus group W member 1, envelope Protein, ERVW-1 Protein
    Background
    This endogenous retroviral envelope protein has retained its original fusogenic properties and participates in trophoblast fusion and the formation of a syncytium during placenta morphogenesis. May induce fusion through binding of SLC1A4 and SLC1A5 (PubMed:10708449, PubMed:12050356, PubMed:23492904). {ECO:0000269|PubMed:10708449, ECO:0000269|PubMed:12050356, ECO:0000269|PubMed:23492904}., Endogenous envelope proteins may have kept, lost or modified their original function during evolution. Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. The surface protein (SU) mediates receptor recognition, while the transmembrane protein (TM) acts as a class I viral fusion protein. The protein may have at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of membranes.
    Molecular Weight
    58.7 kDa Including tag.
    UniProt
    Q9UQF0
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