OASL2 Protein (AA 1-508) (Strep Tag)

N° du produit ABIN3137635

Détail du produit

Antigène: OASL2 (2'-5' Oligoadenylate Synthetase-Like 2 (OASL2))

Type de proteíne: Recombinant

Attributs du protein: AA 1-508

Origine: Souris

Source: Tobacco (Nicotiana tabacum)

Purification/Conjugué: Cette OASL2 protéine est marqué à la Strep Tag.

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

Séquence: MDPFPDLYAT PGDSLDHFLE HSLQPQRDWK EEGQDAWERI ERFFREQCFR DELLLDQEVR VIKVVKGGSS GKGTTLNHRS DQDMILFLSC FSSFEEQARN REVVISFIKK RLIHCSRSLA YNIIVLTHRE GKRAPRSLTL KVQSRKTDDI IWMDILPAYD ALGPISRDSK PAPAIYETLI RSKGYPGDFS PSFTELQRHF VKTRPVKLKN LLRLVKFWYL QCLRRKYGRG AVLPSKYALE LLTIYAWEMG TESSDSFNLD EGFVAVMELL VNYRDICIYW TKYYNFQNEV VRNFLKKQLK GDRPIILDPA DPTNNLGRRK GWEQVAAEAA FCLLQVCCTT VGPSERWNVQ RARDVQVRVK QTGTVDWTLW TNPYSPIRKM KAEIRREKNF GGELRISFQE PGGERQLLSS RKTLADYGIF SKVNIQVLET FPPEILVFVK YPGGQSKPFT IDPDDTILDL KEKIEDAGGP CAEDQVLLLD DEELEDDESL KELEIKDCDT IILIRVID
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: OASL2 (2'-5' Oligoadenylate Synthetase-Like 2 (OASL2))

Autre désignation: Oasl2

Synonymes: M1204 Protein, Mmu-OASL Protein, Oasl Protein, 2'-5' oligoadenylate synthetase-like 2 Protein, Oasl2 Protein

Sujet: 2'-5'-oligoadenylate synthase-like protein 2 (EC 2.7.7.84) (54 kDa 2'-5'-oligoadenylate synthase-like protein) (p54 OASL) (M1204),FUNCTION: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. Synthesizes oligomers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L. {ECO:0000269|PubMed:12396720, ECO:0000269|PubMed:12799444}.

Poids moléculaire: 58.8 kDa

UniProt: Q9Z2F2