Recombinant Human RNF34 protein (ab176063)
Key features and details
- Expression system: Escherichia coli
- Purity: > 90% SDS-PAGE
- Tags: His tag N-Terminus
- Suitable for: SDS-PAGE, MS
Description
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Product name
Recombinant Human RNF34 protein
See all RNF34 proteins and peptides -
Purity
> 90 % SDS-PAGE. -
Expression system
Escherichia coli -
Accession
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Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Sequence
MGSSHHHHHH SSGLVPRGSH MGSMRKAGAT SMWASCCGLL NEVMGTGAVR GQQSAFAGAT GPFRFTPNPE FSTYPPAATE GPNIVCKACG LSFSVFRKKH VCCDCKKDFC SVCSVLQENL RRCSTCHLLQ ETAFQRPQLM RLKVKDLRQY LILRNIPIDT CREKEDLVDL VLCHHGLGSE DDMDTSSLNS SRSQTSSFFT RSFFSNYTAP SATMSSFQGE LMDGDQTSRS GVPAQVQSEI TSANTEDDDD DDDEDDDDEE ENAEDRNPGL SKERVRASLS DLSSLDDVEG MSVRQLKEIL ARNFVNYSGC CEKWELVEKV NRLYKENEEN QKSYGERLQL QDEEDDSLCR ICMDAVIDCV LLECGHMVTC TKCGKRMSEC PICRQYVVRA VHVFKS -
Predicted molecular weight
44 kDa including tags -
Amino acids
1 to 373 -
Tags
His tag N-Terminus -
Additional sequence information
Isoform 2. NP_919247.1.
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Associated products
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Related Products
Specifications
Our Abpromise guarantee covers the use of ab176063 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
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Applications
SDS-PAGE
Mass Spectrometry
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Mass spectrometry
MALDI-TOF -
Form
Liquid -
Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped at 4°C. Store at +4°C short term (1-2 weeks). Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
pH: 8.00
Constituents: 0.58% Sodium chloride, 0.32% Tris-HCl buffer, 10% Glycerol (glycerin, glycerine), 0.02% DTT
General Info
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Alternative names
- CARP 1
- CARP-1
- CARP1
see all -
Function
E3 ubiquitin-protein ligase that regulates several biological processes through the ubiquitin-mediated proteasomal degradation of various target proteins. Ubiquitinates the caspases CASP8 and CASP10, promoting their proteasomal degradation, to negatively regulate cell death downstream of death domain receptors in the extrinsic pathway of apoptosis (PubMed:15069192). May mediate 'Lys-48'-linked polyubiquitination of RIPK1 and its subsequent proteasomal degradation thereby indirectly regulating the tumor necrosis factor-mediated signaling pathway (Ref.13). Negatively regulates p53/TP53 through its direct ubiquitination and targeting to proteasomal degradation (PubMed:17121812). Indirectly, may also negatively regulate p53/TP53 through ubiquitination and degradation of SFN (PubMed:18382127). Mediates PPARGC1A proteasomal degradation probably through ubiquitination thereby indirectly regulating the metabolism of brown fat cells (PubMed:22064484). Possibly involved in innate immunity, through 'Lys-48'-linked polyubiquitination of NOD1 and its subsequent proteasomal degradation (PubMed:25012219). -
Tissue specificity
Ubiquitous. Detected in heart, brain, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, colon and leukocytes. -
Pathway
Protein modification; protein ubiquitination. -
Sequence similarities
Contains 1 FYVE-type zinc finger.
Contains 1 RING-type zinc finger.
Contains 2 SAP domains. -
Domain
The RING-type zinc finger is required for the ubiquitination of target proteins.
The FYVE-type zinc finger domain is required for localization and may confer affinity for cellular compartments enriched in phosphatidylinositol 5-phosphate and phosphatidylinositol 3-phosphate phospholipids. -
Post-translational
modificationsAutoubiquitinated (in vitro).
Proteolytically cleaved by caspases upon induction of apoptosis by TNF. -
Cellular localization
Cell membrane. Endomembrane system. Nucleus. Nucleus speckle. Cytoplasm, cytosol. - Information by UniProt
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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SDS download
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Datasheet download
References (0)
ab176063 has not yet been referenced specifically in any publications.