F162A Protein (AA 1-155) (Strep Tag)

Produktnummer ABIN3129173

Produktdetails

Target: F162A (FAM162A) (Family with Sequence Similarity 162, Member A (FAM162A))

Protein-Typ: Recombinant

Proteineigenschaft: AA 1-155

Spezies: Maus

Quelle: Tobacco (Nicotiana tabacum)

Aufreinigungstag / Konjugat: Dieses F162A Protein ist gelabelt mit Strep Tag.

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

Sequenz: MWSLGGLRLA AGHCLRLYER NASSSLRFTR NTDLKRINGF CTKPQESPKT PTQSYRHGVP LHKPTDFEKK ILLWSGRFKK EEEIPETISF EMLDAAKNKL RVKVSYLMIA LTVAGCIYMV IEGKKAAKRH ESLTSLNLER KARLREEAAM KAKTD
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.

Produktmerkmale: 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.

Aufreinigung: 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.

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

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

Güteklasse: Crystallography grade

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

Handhabung: Avoid repeated freeze-thaw cycles.

Lagerung: -80 °C

Informationen zur Lagerung: Store at -80°C.

Haltbarkeit: Unlimited (if stored properly)

Antigendetails

Target: F162A (FAM162A) (Family with Sequence Similarity 162, Member A (FAM162A))

Andere Bezeichnung: Fam162a (FAM162A Produkte)

Synonyme: C3orf28 Protein, E2IG5 Protein, HGTD-P Protein, 2310056P07Rik Protein, family with sequence similarity 162 member A Protein, family with sequence similarity 162, member A Protein, FAM162A Protein, Fam162a Protein

Hintergrund: Protein FAM162A (E2-induced gene 5 protein homolog) (Growth and transformation-dependent protein) (HGTD-P),FUNCTION: Proposed to be involved in regulation of apoptosis, the exact mechanism may differ between cell types/tissues (PubMed:15082785). May be involved in hypoxia-induced cell death of transformed cells implicating cytochrome C release and caspase activation (such as CASP9) and inducing mitochondrial permeability transition (PubMed:15082785). May be involved in hypoxia-induced cell death of neuronal cells probably by promoting release of AIFM1 from mitochondria to cytoplasm and its translocation to the nucleus, however, the involvement of caspases has been reported conflictingly (PubMed:17316997). {ECO:0000269|PubMed:15082785, ECO:0000269|PubMed:17316997}.

Molekulargewicht: 17.7 kDa

UniProt: Q9D6U8

Pathways: Positive Regulation of Endopeptidase Activity, SARS-CoV-2 Protein Interaktom