SLCO4A1 Protein (AA 1-722) (Strep Tag)

Catalog No. ABIN3117230

This Recombinant SLCO4A1 protein is expressed in Cell-free protein synthesis (CFPS).

Quick Overview for SLCO4A1 Protein (AA 1-722) (Strep Tag) (ABIN3117230)

Target: SLCO4A1 (OATP-E) (Organic Anion Transporter E (OATP-E))

Protein Type: Recombinant

Origin: Human

Source: Cell-free protein synthesis (CFPS)

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

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

Grade: custom-made

Product Details

Protein Characteristics: AA 1-722

Purification tag / Conjugate: This SLCO4A1 protein is labelled with Strep Tag.

Sequence: MPLHQLGDKP LTFPSPNSAM ENGLDHTPPS RRASPGTPLS PGSLRSAAHS PLDTSKQPLC QLWAEKHGAR GTHEVRYVSA GQSVACGWWA FAPPCLQVLN TPKGILFFLC AAAFLQGMTV NGFINTVITS LERRYDLHSY QSGLIASSYD IAACLCLTFV SYFGGSGHKP RWLGWGVLLM GTGSLVFALP HFTAGRYEVE LDAGVRTCPA NPGAVCADST SGLSRYQLVF MLGQFLHGVG ATPLYTLGVT YLDENVKSSC SPVYIAIFYT AAILGPAAGY LIGGALLNIY TEMGRRTELT TESPLWVGAW WVGFLGSGAA AFFTAVPILG YPRQLPGSQR YAVMRAAEMH QLKDSSRGEA SNPDFGKTIR DLPLSIWLLL KNPTFILLCL AGATEATLIT GMSTFSPKFL ESQFSLSASE AATLFGYLVV PAGGGGTFLG GFFVNKLRLR GSAVIKFCLF CTVVSLLGIL VFSLHCPSVP MAGVTASYGG SLLPEGHLNL TAPCNAACSC QPEHYSPVCG SDGLMYFSLC HAGCPAATET NVDGQKVYRD CSCIPQNLSS GFGHATAGKC TSTCQRKPLL LVFIFVVIFF TFLSSIPALT ATLRCVRDPQ RSFALGIQWI VVRILGGIPG PIAFGWVIDK ACLLWQDQCG QQGSCLVYQN SAMSRYILIM GLLYKVLGVL FFAIACFLYK PLSESSDGLE TCLPSQSSAP DSATDSQLQS SV
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..

Characteristics: 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.

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

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 guarantee though.

Comment:

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

Handling

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.

Handling Advice: Avoid repeated freeze-thaw cycles.

Storage: -80 °C

Storage Comment: Store at -80°C.

Expiry Date: 12 months

Target Details

Target: SLCO4A1 (OATP-E) (Organic Anion Transporter E (OATP-E))

Alternative Name: SLCO4A1

Background: Solute carrier organic anion transporter family member 4A1 (OATP4A1) (Colon organic anion transporter) (Organic anion transporter polypeptide-related protein 1) (OATP-RP1) (OATPRP1) (POAT) (Organic anion-transporting polypeptide E) (OATP-E) (Sodium-independent organic anion transporter E) (Solute carrier family 21 member 12),FUNCTION: Organic anion antiporter with apparent broad substrate specificity. Recognizes various substrates including thyroid hormones 3,3',5-triiodo-L-thyronine (T3), L-thyroxine (T4) and 3,3',5'-triiodo-L-thyronine (rT3), conjugated steroids such as estrone 3-sulfate and estradiol 17-beta glucuronide, bile acids such as taurocholate and prostanoids such as prostaglandin E2, likely operating in a tissue-specific manner (PubMed:10873595, PubMed:19129463, PubMed:30343886). May be involved in uptake of metabolites from the circulation into organs such as kidney, liver or placenta. Possibly drives the selective transport of thyroid hormones and estrogens coupled to an outward glutamate gradient across the microvillous membrane of the placenta (PubMed:30343886). The transport mechanism, its electrogenicity and potential tissue-specific counterions remain to be elucidated (Probable). {ECO:0000269|PubMed:10873595, ECO:0000269|PubMed:19129463, ECO:0000269|PubMed:30343886, ECO:0000305}.

Molecular Weight: 77.2 kDa

UniProt: Q96BD0

Pathways: Hormone Transport