RLIM Protein (His tag)
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- Antigène Voir toutes RLIM Protéines
- RLIM (Ring Finger Protein, LIM Domain Interacting (RLIM))
- Type de proteíne
- Recombinant
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Origine
- Humain
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Source
- Escherichia coli (E. coli)
- Purification/Conjugué
- Cette RLIM protéine est marqué à la His tag.
- Application
- Antibody Production (AbP), Standard (STD)
- Attributs du produit
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- Recombinant human RNF12 / RLIM (full length, N-term HIS tag, transcript variant 2) protein expressed in E.coli.
- Produced with end-sequenced ORF clone
- Pureté
- > 80 % as determined by SDS-PAGE and Coomassie blue staining
- Top Product
- Discover our top product RLIM Protéine
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- Indications d'application
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Recombinant human proteins can be used for:
Native antigens for optimized antibody production
Positive controls in ELISA and other antibody assays - Commentaires
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The tag is located at the N-terminal.
- Restrictions
- For Research Use only
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- Concentration
- 50 μg/mL
- Buffer
- 25 mM Tris, pH 8.0, 150 mM NaCl, 10 % glycerol, 1 % Sarkosyl.
- Stock
- -80 °C
- Stockage commentaire
- Store at -80°C. Thaw on ice, aliquot to individual single-use tubes, and then re-freeze immediately. Only 2-3 freeze thaw cycles are recommended.
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- Antigène
- RLIM (Ring Finger Protein, LIM Domain Interacting (RLIM))
- Autre désignation
- Rnf12,rlim (RLIM Produits)
- Synonymes
- NY-REN-43 Protein, RNF12 Protein, AL022832 Protein, AW743871 Protein, Ha1r Protein, Rnf12 Protein, R-LIM Protein, ring finger protein, LIM domain interacting Protein, XRnf12C protein Protein, RLIM Protein, Rlim Protein, xrnf12c Protein, rlim Protein
- Sujet
- The protein encoded by this gene is a RING-H2 zinc finger protein. It has been shown to be an E3 ubiquitin protein ligase that targets LIM domain binding 1 (LDB1/CLIM), and causes proteasome-dependent degradation of LDB1. This protein and LDB1 are co-repressors of LHX1/LIM-1, a homeodomain transcription factor. Multiple alternatively spliced variants, encoding the same protein, have been identified.
- Poids moléculaire
- 68.4 kDa
- NCBI Accession
- NP_899196
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