ATG4C Protein (AA 1-458) (Strep Tag)

Catalog No. ABIN3089550

Product Details

Target: ATG4C (Autophagy related 4C Cysteine Peptidase (ATG4C))

Protein Type: Recombinant

Protein Characteristics: AA 1-458

Origin: Human

Source: Tobacco (Nicotiana tabacum)

Purification tag / Conjugate: This ATG4C protein is labelled with Strep Tag.

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

Sequence: MEATGTDEVD KLKTKFISAW NNMKYSWVLK TKTYFSRNSP VLLLGKCYHF KYEDEDKTLP AESGCTIEDH VIAGNVEEFR KDFISRIWLT YREEFPQIEG SALTTDCGWG CTLRTGQMLL AQGLILHFLG RAWTWPDALN IENSDSESWT SHTVKKFTAS FEASLSGERE FKTPTISLKE TIGKYSDDHE MRNEVYHRKI ISWFGDSPLA LFGLHQLIEY GKKSGKKAGD WYGPAVVAHI LRKAVEEARH PDLQGITIYV AQDCTVYNSD VIDKQSASMT SDNADDKAVI ILVPVRLGGE RTNTDYLEFV KGILSLEYCV GIIGGKPKQS YYFAGFQDDS LIYMDPHYCQ SFVDVSIKDF PLETFHCPSP KKMSFRKMDP SCTIGFYCRN VQDFKRASEE ITKMLKFSSK EKYPLFTFVN GHSRDYDFTS TTTNEEDLFS EDEKKQLKRF STEEFVLL
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: ATG4C (Autophagy related 4C Cysteine Peptidase (ATG4C))

Alternative Name: ATG4C (ATG4C Products)

Synonyms: apg4c Protein, atg4cl Protein, zgc:86888 Protein, wu:fc56g07 Protein, APG4-C Protein, APG4C Protein, AUTL1 Protein, AUTL3 Protein, Apg4-C Protein, Apg4c Protein, Atg4cl Protein, Autl1 Protein, autophagy related 4C cysteine peptidase Protein, autophagy related 4C, cysteine peptidase Protein, cysteine protease ATG4C Protein, ATG4C Protein, atg4c Protein, Tsp_15996 Protein, Atg4c Protein

Background: Cysteine protease ATG4C (EC 3.4.22.-) (AUT-like 3 cysteine endopeptidase) (Autophagy-related cysteine endopeptidase 3) (Autophagin-3) (Autophagy-related protein 4 homolog C) (HsAPG4C),FUNCTION: Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins (PubMed:21177865, PubMed:29458288, PubMed:30661429). The protease activity is required for proteolytic activation of ATG8 family proteins: cleaves the C-terminal amino acid of ATG8 proteins MAP1LC3 and GABARAPL2, to reveal a C-terminal glycine (PubMed:21177865). Exposure of the glycine at the C-terminus is essential for ATG8 proteins conjugation to phosphatidylethanolamine (PE) and insertion to membranes, which is necessary for autophagy (By similarity). In addition to the protease activity, also mediates delipidation of ATG8 family proteins (PubMed:29458288, PubMed:33909989). Catalyzes delipidation of PE-conjugated forms of ATG8 proteins during macroautophagy (PubMed:29458288, PubMed:33909989). Compared to ATG4B, the major protein for proteolytic activation of ATG8 proteins, shows weaker ability to cleave the C-terminal amino acid of ATG8 proteins, while it displays stronger delipidation activity (PubMed:29458288). In contrast to other members of the family, weakly or not involved in phagophore growth during mitophagy (PubMed:33773106). {ECO:0000250|UniProtKB:Q9Y4P1, ECO:0000269|PubMed:21177865, ECO:0000269|PubMed:29458288, ECO:0000269|PubMed:30661429, ECO:0000269|PubMed:33773106, ECO:0000269|PubMed:33909989}.

Molecular Weight: 52.5 kDa

UniProt: Q96DT6

Pathways: Autophagy