SREBF chaperone Protein (SCAP) (AA 1-1279) (Strep Tag)

Produktnummer ABIN3114499

Recombinant SREBF chaperone-Protein exprimiert in Cell-free protein synthesis (CFPS).

Kurzübersicht für SREBF chaperone Protein (SCAP) (AA 1-1279) (Strep Tag) (ABIN3114499)

Target: SREBF chaperone (SCAP)

Protein-Typ: Recombinant

Spezies: Human

Quelle: Cell-free protein synthesis (CFPS)

Applikation: ELISA, SDS-PAGE (SDS), Western Blotting (WB)

Reinheit: approximately 70-80 % as determined by SDS PAGE, Western Blot and analytical SEC (HPLC).

Güteklasse: custom-made

Produktdetails

Proteineigenschaft: AA 1-1279

Aufreinigungstag / Konjugat: Dieses SREBF chaperone Protein ist gelabelt mit Strep Tag.

Sequenz: MTLTERLREK ISRAFYNHGL LCASYPIPII LFTGFCILAC CYPLLKLPLP GTGPVEFTTP VKDYSPPPVD SDRKQGEPTE QPEWYVGAPV AYVQQIFVKS SVFPWHKNLL AVDVFRSPLS RAFQLVEEIR NHVLRDSSGI RSLEELCLQV TDLLPGLRKL RNLLPEHGCL LLSPGNFWQN DWERFHADPD IIGTIHQHEP KTLQTSATLK DLLFGVPGKY SGVSLYTRKR MVSYTITLVF QHYHAKFLGS LRARLMLLHP SPNCSLRAES LVHVHFKEEI GVAELIPLVT TYIILFAYIY FSTRKIDMVK SKWGLALAAV VTVLSSLLMS VGLCTLFGLT PTLNGGEIFP YLVVVIGLEN VLVLTKSVVS TPVDLEVKLR IAQGLSSESW SIMKNMATEL GIILIGYFTL VPAIQEFCLF AVVGLVSDFF LQMLFFTTVL SIDIRRMELA DLNKRLPPEA CLPSAKPVGQ PTRYERQLAV RPSTPHTITL QPSSFRNLRL PKRLRVVYFL ARTRLAQRLI MAGTVVWIGI LVYTDPAGLR NYLAAQVTEQ SPLGEGALAP MPVPSGMLPP SHPDPAFSIF PPDAPKLPEN QTSPGESPER GGPAEVVHDS PVPEVTWGPE DEELWRKLSF RHWPTLFSYY NITLAKRYIS LLPVIPVTLR LNPREALEGR HPQDGRSAWP PPGPIPAGHW EAGPKGPGGV QAHGDVTLYK VAALGLATGI VLVLLLLCLY RVLCPRNYGQ LGGGPGRRRR GELPCDDYGY APPETEIVPL VLRGHLMDIE CLASDGMLLV SCCLAGHVCV WDAQTGDCLT RIPRPGRQRR DSGVGSGLEA QESWERLSDG GKAGPEEPGD SPPLRHRPRG PPPPSLFGDQ PDLTCLIDTN FSAQPRSSQP TQPEPRHRAV CGRSRDSPGY DFSCLVQRVY QEEGLAAVCT PALRPPSPGP VLSQAPEDEG GSPEKGSPSL AWAPSAEGSI WSLELQGNLI VVGRSSGRLE VWDAIEGVLC CSSEEVSSGI TALVFLDKRI VAARLNGSLD FFSLETHTAL SPLQFRGTPG RGSSPASPVY SSSDTVACHL THTVPCAHQK PITALKAAAG RLVTGSQDHT LRVFRLEDSC CLFTLQGHSG AITTVYIDQT MVLASGGQDG AICLWDVLTG SRVSHVFAHR GDVTSLTCTT SCVISSGLDD LISIWDRSTG IKFYSIQQDL GCGASLGVIS DNLLVTGGQG CVSFWDLNYG DLLQTVYLGK NSEAQPARQI LVLDNAAIVC NFGSELSLVY VPSVLEKLD
Sequence without tag. The proposed Strep-Tag is based on experience with the expression system. Our team may suggest an additional tag depending on the complexity of the protein. If you have a special request, please contact us..

Produktmerkmale: Key Benefits:

• Made in Germany - from design to production - by highly experienced protein experts.
• Protein expressed with ALiCE® and purified in one-step affinity chromatography
• State-of-the-art algorithm used for plasmid design (Gene synthesis).

This protein is a predefined custom protein and will be made for the first time for your order. Our experts in the lab try to ensure that you receive soluble protein.

The big advantage of ordering our predefined custom 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 against its specific reference buffer.
• We use the Expasy's ProtParam tool to determine the absorption coefficient of each protein.

Aufreinigung: One-step Strep-tag purification of proteins expressed in Almost Living Cell-Free Expression System (ALiCE®).

Anwendungsinformationen

Applikationshinweise: 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.

Kommentare:

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!

Beschränkungen: Nur für Forschungszwecke einsetzbar

Handhabung

Format: Liquid

Buffer: The buffer composition is at the discretion of the manufacturer.
Standard Storage Buffer: PBS pH 7.4, 10 % Glycerol Might differ depending on protein.

Handhabung: Avoid repeated freeze-thaw cycles.

Lagerung: -80 °C

Informationen zur Lagerung: Store at -80°C.

Haltbarkeit: 12 months

Antigendetails

Target: SREBF chaperone (SCAP)

Andere Bezeichnung: SCAP

Hintergrund: Sterol regulatory element-binding protein cleavage-activating protein (SCAP) (SREBP cleavage-activating protein),FUNCTION: Escort protein required for cholesterol as well as lipid homeostasis (By similarity). Regulates export of the SCAP-SREBP complex from the endoplasmic reticulum to the Golgi upon low cholesterol, thereby regulating the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2 (By similarity). At high sterol concentrations, formation of a ternary complex with INSIG (INSIG1 or INSIG2) leads to mask the ER export signal in SCAP, promoting retention of the complex in the endoplasmic reticulum (By similarity). Low sterol concentrations trigger release of INSIG, a conformational change in the SSD domain of SCAP, unmasking of the ER export signal, promoting recruitment into COPII-coated vesicles and transport of the SCAP-SREBP to the Golgi: in the Golgi, SREBPs are then processed, releasing the transcription factor fragment of SREBPs from the membrane, its import into the nucleus and up-regulation of LDLR, INSIG1 and the mevalonate pathway (By similarity). Binds cholesterol via its SSD domain (By similarity). {ECO:0000250|UniProtKB:P97260}.

Molekulargewicht: 139.7 kDa

UniProt: Q12770

Pathways: SARS-CoV-2 Protein Interaktom