SLC31A1 Protein (AA 1-196) (Strep Tag)

Catalog No. ABIN3126302

Product Details

Target: SLC31A1 (Solute Carrier Family 31 (Copper Transporters), Member 1 (SLC31A1))

Protein Type: Recombinant

Protein Characteristics: AA 1-196

Origin: Mouse

Source: Tobacco (Nicotiana tabacum)

Purification tag / Conjugate: This SLC31A1 protein is labelled with Strep Tag.

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

Sequence: MNHMGMNHME MHHHMGMNHT DDNITMPPHH HPTTSASHSH GGGDSMMMMP MTFYFDFKNV NLLFSGLVIN TPGEMAGAFV AVFLLAMFYE GLKIAREGLL RKSQVSIRYN SMPVPGPNGT ILMETHKTVG QQMLSFPHLL QTVLHIIQVV ISYFLMLIFM TYNGYLCIAV AAGAGTGYFL FSWKKAVVVD ITEHCH
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.

Characteristics: 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.

Purity: ≥ 80 % as determined by SDS PAGE, Size Exclusion Chromatography and Western Blot.

Endotoxin Level: Low Endotoxin less than 1 EU/mg (< 0.1 ng/mg)

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 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. If you have a special request, please contact us.

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: SLC31A1 (Solute Carrier Family 31 (Copper Transporters), Member 1 (SLC31A1))

Alternative Name: Slc31a1 (SLC31A1 Products)

Synonyms: SLC31A1 Protein, Xctr1 Protein, copt1 Protein, ctr1 Protein, hctr1 Protein, K19M22.24 Protein, copper transporter 1 Protein, Slc31a1 Protein, COPT1 Protein, CTR1 Protein, Ctr1 Protein, LRRGT00200 Protein, ctr-1 Protein, zgc:76839 Protein, 4930445G01Rik Protein, AI787263 Protein, AU016967 Protein, solute carrier family 31 member 1 Protein, copper transporter 1 Protein, solute carrier family 31 (copper transporter), member 1 Protein, solute carrier family 31, member 1 Protein, SLC31A1 Protein, LOC100281410 Protein, LOC100286321 Protein, slc31a1 Protein, COPT1 Protein, Slc31a1 Protein

Background: High affinity copper uptake protein 1 (Copper transporter 1) (CTR1) (Solute carrier family 31 member 1) [Cleaved into: Truncated CTR1 form],FUNCTION: [High affinity copper uptake protein 1]: Uniporter that mediates the transport of copper(1+) from the extracellular space to the cytoplasm, across the plasma membrane (PubMed:11391005, PubMed:12177073, PubMed:16847145, PubMed:24167251). Then, delivers directly copper(1+) to specific chaperone such as ATOX1, via a copper(1+)- mediated transient interaction between the C-terminal domain and a copper(1+) chaperone, thus controlling intracellular copper(1+) levels (By similarity). May function in copper(1+) import from the apical membrane thus may drive intestinal copper absorption (PubMed:16950140). The copper(1+) transport mechanism is sodium-independent, saturable and of high-affinity (By similarity). Also mediates the uptake of silver(1+) (PubMed:20569931). May function in the influx of the platinum-containing chemotherapeutic agents (PubMed:16847145, PubMed:19144690, PubMed:12370430). The platinum-containing chemotherapeutic agents uptake is saturable (By similarity). Also participates in the first step of copper(2+) acquisition by cells through a direct transfer of copper(2+) from copper(2+) carriers in blood, such as ALB to the N-terminal domain of SLC31A1, leading to copper(2+) reduction and probably followed by copper(1+) stabilization (By similarity). In addition, functions as a redox sensor to promote angiogenesis in endothelial cells, in a copper(1+) transport independent manner, by transmitting the VEGF-induced ROS signal through a sulfenylation at Cys-195 leading to a subsequent disulfide bond formation between SLC31A1 and KDR (PubMed:35027734). The SLC31A1-KDR complex is then co-internalized to early endosomes, driving a sustained VEGFR2 signaling (By similarity). {ECO:0000250|UniProtKB:O15431, ECO:0000250|UniProtKB:Q9JK41, ECO:0000269|PubMed:11391005, ECO:0000269|PubMed:12177073, ECO:0000269|PubMed:12370430, ECO:0000269|PubMed:16847145, ECO:0000269|PubMed:16950140, ECO:0000269|PubMed:19144690, ECO:0000269|PubMed:20569931, ECO:0000269|PubMed:24167251, ECO:0000269|PubMed:35027734}., FUNCTION: [Truncated CTR1 form]: Mobilizes copper(1+) out of the endosomal compartment, making copper(1+) available for export out of the cells. {ECO:0000269|PubMed:24167251}.

Molecular Weight: 22.0 kDa

UniProt: Q8K211