COMMD1 Protein (AA 1-188) (Strep Tag)

N° du produit ABIN3136611

Détail du produit

Antigène: COMMD1 (Copper Metabolism (Murr1) Domain Containing 1 (COMMD1))

Type de proteíne: Recombinant

Attributs du protein: AA 1-188

Origine: Souris

Source: Tobacco (Nicotiana tabacum)

Purification/Conjugué: Cette COMMD1 protéine est marqué à la Strep Tag.

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

Séquence: MAGDLEGGKS LSGLLSGLAQ NAFHGHSGVT EELLHSQLYP EVPPEEFRPF LAKMRGLLKS IASADMDFNQ LEAFLTAQTK KQGGITSEQA AVISKFWKSH KIKIRESLMK QSRWDNGLRG LSWRVDGKSQ SRHSTQIHSP VAIIELEFGK NGQESEFLCL EFDEVKVKQI LKKLSEVEES INRLMQAA
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: COMMD1 (Copper Metabolism (Murr1) Domain Containing 1 (COMMD1))

Autre désignation: Commd1 (COMMD1 Produits)

Synonymes: C2orf5 Protein, MURR1 Protein, murr1 Protein, commd1 Protein, si:ch211-213b8.2 Protein, DDBDRAFT_0184206 Protein, DDBDRAFT_0266452 Protein, DDB_0184206 Protein, DDB_0266452 Protein, COMMD1 Protein, MGC114682 Protein, AI256843 Protein, Murr1 Protein, U2/Mu Protein, copper metabolism domain containing 1 Protein, copper metabolism (Murr1) domain containing 1 Protein, COMM domain-containing protein 1 Protein, copper metabolism domain containing 1 L homeolog Protein, COMM domain containing 1 Protein, COMMD1 Protein, commd1 Protein, comd1 Protein, Commd1 Protein, commd1.L Protein

Sujet: COMM domain-containing protein 1 (Protein Murr1),FUNCTION: Proposed scaffold protein that is implicated in diverse physiological processes and whose function may be in part linked to its ability to regulate ubiquitination of specific cellular proteins. Can modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes by displacing CAND1, in vitro promotes CRL E3 activity and dissociates CAND1 from CUL1 and CUL2. Promotes ubiquitination of NF-kappa-B subunit RELA and its subsequent proteasomal degradation. Down-regulates NF-kappa-B activity. Involved in the regulation of membrane expression and ubiquitination of SLC12A2. Modulates Na(+) transport in epithelial cells by regulation of apical cell surface expression of amiloride-sensitive sodium channel (ENaC) subunits and by promoting their ubiquitination presumably involving NEDD4L. Promotes the localization of SCNN1D to recycling endosomes. Promotes CFTR cell surface expression through regulation of its ubiquitination. Down-regulates SOD1 activity by interfering with its homodimerization. Plays a role in copper ion homeostasis. Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery, the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes. Can bind one copper ion per monomer. May function to facilitate biliary copper excretion within hepatocytes. Binds to phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). Involved in the regulation of HIF1A-mediated transcription, competes with ARNT/Hif-1-beta for binding to HIF1A resulting in decreased DNA binding and impaired transcriptional activation by HIF-1. Negatively regulates neuroblastoma G1/S phase cell cycle progression and cell proliferation by stimulating ubiquitination of NF-kappa-B subunit RELA and NF-kappa-B degradation in a FAM107A- and actin-dependent manner. {ECO:0000250|UniProtKB:Q8N668}.

Poids moléculaire: 21.0 kDa

UniProt: Q8K4M5

Pathways: Transition Metal Ion Homeostasis