SLC26A5 Protein (AA 1-744) (Strep Tag)

N° du produit ABIN3136992

Détail du produit

Antigène: SLC26A5 (Solute Carrier Family 26, Member 5 (Prestin) (SLC26A5))

Type de proteíne: Recombinant

Attributs du protein: AA 1-744

Origine: Souris

Source: Tobacco (Nicotiana tabacum)

Purification/Conjugué: Cette SLC26A5 protéine est marqué à la Strep Tag.

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

Séquence: MDHAEENEIP AETQRYYVER PIFSHPVLQE RLHVKDKVTE SIGDKLKQAF TCTPKKIRNI IYMFLPITKW LPAYKFKEYV LGDLVSGIST GVLQLPQGLA FAMLAAVPPV FGLYSSFYPV IMYCFFGTSR HISIGPFAVI SLMIGGVAVR LVPDDIVIPG GVNATNGTEA RDALRVKVAM SVTLLSGIIQ FCLGVCRFGF VAIYLTEPLV RGFTTAAAVH VFTSMLKYLF GVKTKRYSGI FSVVYSTVAV LQNVKNLNVC SLGVGLMVFG LLLGGKEFNE RFKEKLPAPI PLEFFAVVMG TGISAGFNLH ESYSVDVVGT LPLGLLPPAN PDTSLFHLVY VDAIAIAIVG FSVTISMAKT LANKHGYQVD GNQELIALGI CNSIGSLFQT FSISCSLSRS LVQEGTGGKT QLAGCLASLM ILLVILATGF LFESLPQAVL SAIVIVNLKG MFMQFSDLPF FWRTSKIELT IWLTTFVSSL FLGLDYGLIT AVIIALLTVI YRTQSPSYKV LGQLPDTDVY IDIDAYEEVK EIPGIKIFQI NAPIYYANSD LYSSALKRKT GVNPALIMGA RRKAMRKYAK EVGNANVANA TVVKVDAEVD GENATKPEEE DDEVKFPPIV IKTTFPEELQ RFLPQGENVH TVILDFTQVN FVDSVGVKTL AGIVKEYGDV GIYVYLAGCS PQVVNDLTRN NFFENPALKE LLFHSIHDAV LGSQVREAMA EQEATASLPQ EDMEPNATPT TPEA
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

Information d'application

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

Stockage

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)

Détail du antigène

Antigène: SLC26A5 (Solute Carrier Family 26, Member 5 (Prestin) (SLC26A5))

Autre désignation: Slc26a5 (SLC26A5 Produits)

Synonymes: pres Protein, fb73d12 Protein, fb74g12 Protein, wu:fb73d12 Protein, wu:fb74g12 Protein, DFNB61 Protein, PRES Protein, Pres Protein, prestin Protein, solute carrier family 26 (anion exchanger), member 5 Protein, solute carrier family 26 member 5 Protein, solute carrier family 26, member 5 Protein, slc26a5 Protein, SLC26A5 Protein, Slc26a5 Protein

Sujet: Prestin (Solute carrier family 26 member 5),FUNCTION: Voltage-sensitive motor protein that drives outer hair cell (OHC) electromotility (eM) and participates in sound amplification in the hearing organ (PubMed:12239568). Converts changes in the transmembrane electric potential into mechanical displacements resulting in the coupling of its expansion to movement of a charged voltage sensor across the lipid membrane (PubMed:12239568). The nature of the voltage sensor is not completely clear, and two models compete (By similarity). In the first model, acts as an incomplete transporter where intracellular chloride anion acts as extrinsic voltage sensor that drives conformational change in the protein which is sufficient to produce a length change in the plane of the membrane and hence in the length of the OHC (By similarity). The second model in which multiple charged amino acid residues are distributed at the intracellular and extracellular membrane interfaces that form an intrinsic voltage sensor, whose movement produces the non-linear capacitance (NLC) (By similarity). However, the effective voltage sensor may be the result of a hybrid voltage sensor, assembled from intrinsic charge (charged residues) and extrinsic charge (bound anion) (By similarity). Notably, binding of anions to the anion-binding pocket partially neutralizes the intrinsic positive charge rather than to form an electrically negative sensor, therefore remaining charge may serve as voltage sensor that, after depolarization, moves from down (expanded state) to up (contracted) conformation, which is accompanied by an eccentric contraction of the intermembrane cross-sectional area of the protein as well as a major increase in the hydrophobic thickness of the protein having as consequences the plasma membrane thickening and the cell contraction after membrane depolarization (By similarity). The anion-binding pocket transits from the inward-open (Down) state, where it is exposed toward the intracellular solvent in the absence of anion, to the occluded (Up) state upon anion binding (By similarity). Salicylate competes for the anion-binding site and inhibits the voltage-sensor movement, and therefore inhibits the charge transfer and electromotility by displacing Cl(-) from the anion-binding site and by preventing the structural transitions to the contracted state (By similarity). In addition, can act as a weak Cl(-)/HCO3(-) antiporter across the cell membrane and so regulate the intracellular pH of the outer hair cells (OHCs), while firstly found as being unable to mediate electrogenic anion transport (By similarity). Moreover, supports a role in cardiac mechanical amplification serving as an elastic element to enhance the actomyosin- based sarcomere contraction system (PubMed:33951436). {ECO:0000250|UniProtKB:D7PC76, ECO:0000250|UniProtKB:P58743, ECO:0000250|UniProtKB:Q9EPH0, ECO:0000250|UniProtKB:Q9JKQ2, ECO:0000269|PubMed:12239568, ECO:0000269|PubMed:33951436}.

Poids moléculaire: 81.3 kDa

UniProt: Q99NH7

Pathways: Sensory Perception of Sound, Dicarboxylic Acid Transport