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DEPDC5 Protein (AA 1-1603) (Strep Tag)

Crystallography grade DEPDC5 Origine: Humain Hôte: Tobacco (Nicotiana tabacum) Recombinant >80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot. ELISA, SDS, WB
N° du produit ABIN3092139
  • Antigène Tous les produits DEPDC5
    DEPDC5 (DEP Domain Containing 5 (DEPDC5))
    Type de proteíne
    Recombinant
    Attributs du protein
    AA 1-1603
    Origine
    Humain
    Source
    • 1
    Tobacco (Nicotiana tabacum)
    Purification/Conjugué
    Cette DEPDC5 protéine est marqué à la Strep Tag.
    Application
    ELISA, SDS-PAGE (SDS), Western Blotting (WB)
    Séquence
    MRTTKVYKLV IHKKGFGGSD DELVVNPKVF PHIKLGDIVE IAHPNDEYSP LLLQVKSLKE DLQKETISVD QTVTQVFRLR PYQDVYVNVV DPKDVTLDLV ELTFKDQYIG RGDMWRLKKS LVSTCAYITQ KVEFAGIRAQ AGELWVKNEK VMCGYISEDT RVVFRSTSAM VYIFIQMSCE MWDFDIYGDL YFEKAVNGFL ADLFTKWKEK NCSHEVTVVL FSRTFYDAKS VDEFPEINRA SIRQDHKGRF YEDFYKVVVQ NERREEWTSL LVTIKKLFIQ YPVLVRLEQA EGFPQGDNST SAQGNYLEAI NLSFNVFDKH YINRNFDRTG QMSVVITPGV GVFEVDRLLM ILTKQRMIDN GIGVDLVCMG EQPLHAVPLF KLHNRSAPRD SRLGDDYNIP HWINHSFYTS KSQLFCNSFT PRIKLAGKKP ASEKAKNGRD TSLGSPKESE NALPIQVDYD AYDAQVFRLP GPSRAQCLTT CRSVRERESH SRKSASSCDV SSSPSLPSRT LPTEEVRSQA SDDSSLGKSA NILMIPHPHL HQYEVSSSLG YTSTRDVLEN MMEPPQRDSS APGRFHVGSA ESMLHVRPGG YTPQRALINP FAPSRMPMKL TSNRRRWMHT FPVGPSGEAI QIHHQTRQNM AELQGSGQRD PTHSSAELLE LAYHEAAGRH SNSRQPGDGM SFLNFSGTEE LSVGLLSNSG AGMNPRTQNK DSLEDSVSTS PDPILTLSAP PVVPGFCCTV GVDWKSLTTP ACLPLTTDYF PDRQGLQNDY TEGCYDLLPE ADIDRRDEDG VQMTAQQVFE EFICQRLMQG YQIIVQPKTQ KPNPAVPPPL SSSPLYSRGL VSRNRPEEED QYWLSMGRTF HKVTLKDKMI TVTRYLPKYP YESAQIHYTY SLCPSHSDSE FVSCWVEFSH ERLEEYKWNY LDQYICSAGS EDFSLIESLK FWRTRFLLLP ACVTATKRIT EGEAHCDIYG DRPRADEDEW QLLDGFVRFV EGLNRIRRRH RSDRMMRKGT AMKGLQMTGP ISTHSLESTA PPVGKKGTSA LSALLEMEAS QKCLGEQQAA VHGGKSSAQS AESSSVAMTP TYMDSPRKDG AFFMEFVRSP RTASSAFYPQ VSVDQTATPM LDGTSLGICT GQSMDRGNSQ TFGNSQNIGE QGYSSTNSSD SSSQQLVASS LTSSSTLTEI LEAMKHPSTG VQLLSEQKGL SPYCFISAEV VHWLVNHVEG IQTQAMAIDI MQKMLEEQLI THASGEAWRT FIYGFYFYKI VTDKEPDRVA MQQPATTWHT AGVDDFASFQ RKWFEVAFVA EELVHSEIPA FLLPWLPSRP ASYASRHSSF SRSFGGRSQA AALLAATVPE QRTVTLDVDV NNRTDRLEWC SCYYHGNFSL NAAFEIKLHW MAVTAAVLFE MVQGWHRKAT SCGFLLVPVL EGPFALPSYL YGDPLRAQLF IPLNISCLLK EGSEHLFDSF EPETYWDRMH LFQEAIAHRF GFVQDKYSAS AFNFPAENKP QYIHVTGTVF LQLPYSKRKF SGQQRRRRNS TSSTNQNMFC EERVGYNWAY NTMLTKTWRS SATGDEKFAD RLLKDFTDFC INRDNRLVTF WTSCLEKMHA SAP
    Sequence without tag. The proposed Strep-Tag is based on experience s with the expression system, a different complexity of the protein could make another tag necessary. In case you have a special request, please contact us.
    Attributs du produit
    Key Benefits:
    • Made in Germany - from design to production - by highly experienced protein experts.
    • Protein expressed with ALiCE® and purified by multi-step, protein-specific process to ensure correct folding and modification.
    • These proteins are normally active (enzymatically functional) as our customers have reported (not tested by us and not guaranteed).
    • 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.


    Expression System:
    • ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
    • During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein!

    Concentration:
    • 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.
    • We use the Expasy's ProtParam tool to determine the absorption coefficient of each protein.

    Purification
    Two step purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®):
    1. In a first purification step, the protein is purified from the cleared cell lysate using StrepTag capture material. Eluate fractions are analyzed by SDS-PAGE.
    2. Protein containing fractions of the best purification are subjected to second purification step through size exclusion chromatography. Eluate fractions are analyzed by SDS-PAGE and Western blot.
    Pureté
    >80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.
    niveau d'endotoxine
    Low Endotoxin less than 1 EU/mg (< 0.1 ng/mg)
    Classe de qualité
    Crystallography grade
  • Indications d'application
    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 guarantee though.
    Commentaires

    ALiCE®, our Almost Living Cell-Free Expression System is based on a lysate obtained from Nicotiana tabacum c.v.. This contains all the protein expression machinery needed to produce even the most difficult-to-express proteins, including those that require post-translational modifications.
    During lysate production, the cell wall and other cellular components that are not required for protein production are removed, leaving only the protein production machinery and the mitochondria to drive the reaction. During our lysate completion steps, the additional components needed for protein production (amino acids, cofactors, etc.) are added to produce something that functions like a cell, but without the constraints of a living system - all that's needed is the DNA that codes for the desired protein!

    Restrictions
    For Research Use only
  • Format
    Liquid
    Buffer
    The buffer composition is at the discretion of the manufacturer. If you have a special request, please contact us.
    Conseil sur la manipulation
    Avoid repeated freeze-thaw cycles.
    Stock
    -80 °C
    Stockage commentaire
    Store at -80°C.
    Date de péremption
    Unlimited (if stored properly)
  • Antigène
    DEPDC5 (DEP Domain Containing 5 (DEPDC5))
    Autre désignation
    DEPDC5 (DEPDC5 Produits)
    Synonymes
    DEPDC5 Protein, DEP.5 Protein, FFEVF Protein, AV016528 Protein, DEP domain containing 5 Protein, DEP domain-containing protein 5 Protein, Depdc5 Protein, DEPDC5 Protein, LOC100434001 Protein, LOC100576879 Protein
    Sujet
    GATOR1 complex protein DEPDC5 (DEP domain-containing protein 5),FUNCTION: As a component of the GATOR1 complex functions as an inhibitor of the amino acid-sensing branch of the mTORC1 pathway (PubMed:23723238, PubMed:25457612, PubMed:29769719, PubMed:31548394, PubMed:29590090, PubMed:35338845). In response to amino acid depletion, the GATOR1 complex has GTPase activating protein (GAP) activity and strongly increases GTP hydrolysis by RagA/RRAGA (or RagB/RRAGB) within heterodimeric Rag complexes, thereby turning them into their inactive GDP-bound form, releasing mTORC1 from lysosomal surface and inhibiting mTORC1 signaling (PubMed:23723238, PubMed:25457612, PubMed:29769719, PubMed:29590090, PubMed:35338845). In the presence of abundant amino acids, the GATOR1 complex is negatively regulated by GATOR2, the other GATOR subcomplex, in this amino acid-sensing branch of the TORC1 pathway (PubMed:23723238, PubMed:25457612, PubMed:29769719). Within the GATOR1 complex, DEPDC5 mediates direct interaction with the nucleotide-binding pocket of small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD) and coordinates their nucleotide loading states by promoting RagA/RRAGA or RagB/RRAGB into their GDP-binding state and RagC/RRAGC or RagD/RRAGD into their GTP-binding state (PubMed:29590090, PubMed:35338845). However, it does not execute the GAP activity, which is mediated by NPRL2 (PubMed:29590090). {ECO:0000269|PubMed:23723238, ECO:0000269|PubMed:25457612, ECO:0000269|PubMed:29590090, ECO:0000269|PubMed:29769719, ECO:0000269|PubMed:31548394, ECO:0000269|PubMed:35338845}.
    Poids moléculaire
    181.3 kDa
    UniProt
    O75140
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