LRRC8E Protein (AA 1-796) (Strep Tag)

Catalog No. ABIN3093677

Product Details

Target: LRRC8E (Leucine Rich Repeat Containing 8 Family, Member E (LRRC8E))

Protein Type: Recombinant

Protein Characteristics: AA 1-796

Origin: Human

Source: Tobacco (Nicotiana tabacum)

Purification tag / Conjugate: This LRRC8E protein is labelled with Strep Tag.

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

Sequence: MIPVAEFKQF TEQQPAFKVL KPWWDVLAEY LTVAMLMIGV FGCTLQVTQD KIICLPNHEL QENLSEAPCQ QLLPRGIPEQ IGALQEVKGL KNNLDLQQYS FINQLCYETA LHWYAKYFPY LVVIHTLIFM VCTSFWFKFP GTSSKIEHFI SILGKCFDSP WTTRALSEVS GENQKGPAAT ERAAATIVAM AGTGPGKAGE GEKEKVLAEP EKVVTEPPVV TLLDKKEGEQ AKALFEKVKK FRMHVEEGDI LYTMYIRQTV LKVCKFLAIL VYNLVYVEKI SFLVACRVET SEVTGYASFC CNHTKAHLFS KLAFCYISFV CIYGLTCIYT LYWLFHRPLK EYSFRSVREE TGMGDIPDVK NDFAFMLHLI DQYDSLYSKR FAVFLSEVSE SRLKQLNLNH EWTPEKLRQK LQRNAAGRLE LALCMLPGLP DTVFELSEVE SLRLEAICDI TFPPGLSQLV HLQELSLLHS PARLPFSLQV FLRDHLKVMR VKCEELREVP LWVFGLRGLE ELHLEGLFPQ ELARAATLES LRELKQLKVL SLRSNAGKVP ASVTDVAGHL QRLSLHNDGA RLVALNSLKK LAALRELELV ACGLERIPHA VFSLGALQEL DLKDNHLRSI EEILSFQHCR KLVTLRLWHN QIAYVPEHVR KLRSLEQLYL SYNKLETLPS QLGLCSGLRL LDVSHNGLHS LPPEVGLLQN LQHLALSYNA LEALPEELFF CRKLRTLLLG DNQLSQLSPH VGALRALSRL ELKGNRLEAL PEELGNCGGL KKAGLLVEDT LYQGLPAEVR DKMEEE
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: LRRC8E (Leucine Rich Repeat Containing 8 Family, Member E (LRRC8E))

Alternative Name: LRRC8E (LRRC8E Products)

Synonyms: 1810049O03Rik Protein, C87354 Protein, RGD1311979 Protein, leucine rich repeat containing 8 VRAC subunit E L homeolog Protein, leucine rich repeat containing 8 VRAC subunit E Protein, leucine rich repeat containing 8 family, member E Protein, lrrc8e.L Protein, LRRC8E Protein, Lrrc8e Protein

Background: Volume-regulated anion channel subunit LRRC8E (Leucine-rich repeat-containing protein 8E),FUNCTION: Non-essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes (PubMed:24790029, PubMed:26824658, PubMed:28193731). The VRAC channel conducts iodide better than chloride and can also conduct organic osmolytes like taurine (PubMed:24790029, PubMed:26824658). Mediates efflux of amino acids, such as aspartate, in response to osmotic stress (PubMed:28193731). The VRAC channel also mediates transport of immunoreactive cyclic dinucleotide GMP-AMP (2'-3'-cGAMP), an immune messenger produced in response to DNA virus in the cytosol (PubMed:33171122). Channel activity requires LRRC8A plus at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E), channel characteristics depend on the precise subunit composition (PubMed:24790029, PubMed:26824658, PubMed:28193731). Also plays a role in lysosome homeostasis by forming functional lysosomal VRAC channels in response to low cytoplasmic ionic strength condition: lysosomal VRAC channels are necessary for the formation of large lysosome-derived vacuoles, which store and then expel excess water to maintain cytosolic water homeostasis (PubMed:33139539). {ECO:0000269|PubMed:24790029, ECO:0000269|PubMed:26824658, ECO:0000269|PubMed:28193731, ECO:0000269|PubMed:33139539, ECO:0000269|PubMed:33171122}.

Molecular Weight: 90.2 kDa

UniProt: Q6NSJ5