Recombinant Mouse Clusterin protein (ab194035)
Key features and details
- Expression system: HEK 293 cells
- Purity: > 95% SDS-PAGE
- Endotoxin level: < 0.100 Eu/µg
- Tags: His tag C-Terminus
- Suitable for: HPLC, SDS-PAGE
Description
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Product name
Recombinant Mouse Clusterin protein
See all Clusterin proteins and peptides -
Purity
> 95 % SDS-PAGE.
Determined by SEC-HPLC and reducing SDS-PAGE. -
Endotoxin level
< 0.100 Eu/µg -
Expression system
HEK 293 cells -
Accession
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Protein length
Full length protein -
Animal free
No -
Nature
Recombinant -
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Species
Mouse -
Sequence
EQEVSDNELQELSTQGSRYINKEIQNAVQGVKHIKTLIEKTNAERKSLLN SLEEAKKKKEDALEDTRDSEMKLKAFPEVCNETMMALWEECKPCLKHTCM KFYARVCRSGSGLVGQQLEEFLNQSSPFYFWMNGDRIDSLLESDRQQSQV LDAMQDSFARASGIIDTLFQDRFFARELHDPHYFSPIGFPHKRPHFLYPK SRLVRSLMSPSHYGPPSFHNMFQPFFEMIHQAQQAMDVQLHSPAFQFPDV DFLREGEDDRTVCKEIRRNSTGCLKMKGQCEKCQEILSVDCSTNNPAQAN LRQELNDSLQVAERLTEQYKELLQSFQSKMLNTSSLLEQLNDQFNWVSQL ANLTQGEDKYYLRVSTVTTHSSDSEVPSRVTEVVVKLFDSDPITVVLPEE VSKDNPKFMDTVAEKALQEYRRKSRAEVDHHHHHH -
Predicted molecular weight
50 kDa including tags -
Amino acids
22 to 448 -
Tags
His tag C-Terminus -
Additional sequence information
This product is for the mature full length protein, from aa 22 to 448. The signal peptide is not included.
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Associated products
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Related Products
Specifications
Our Abpromise guarantee covers the use of ab194035 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
HPLC
SDS-PAGE
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Form
Lyophilized -
Concentration information loading...
Preparation and Storage
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Stability and Storage
Shipped at 4°C. The lyophilized protein is stable for a few weeks at room temperature. Store at -20°C. Reconstitute for long term storage.
pH: 7.40
Constituents: 99% Phosphate Buffer, 0.87% Sodium chloride
Lyophilized from a 0.2 µM filtered solution. -
ReconstitutionAlways centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100 µg/ml.Dissolve the lyophilized protein in 1X PBS. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
General Info
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Alternative names
- 40
- AAG 4
- AAG4
see all -
Function
Isoform 1 functions as extracellular chaperone that prevents aggregation of nonnative proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partially unfolded proteins in a state appropriate for subsequent refolding by other chaperones, such as HSPA8/HSC70. Does not refold proteins by itself. Binding to cell surface receptors triggers internalization of the chaperone-client complex and subsequent lysosomal or proteasomal degradation. Secreted isoform 1 protects cells against apoptosis and against cytolysis by complement. Intracellular isoforms interact with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes and promote the ubiquitination and subsequent proteasomal degradation of target proteins. Promotes proteasomal degradation of COMMD1 and IKBKB. Modulates NF-kappa-B transcriptional activity. Nuclear isoforms promote apoptosis. Mitochondrial isoforms suppress BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis. Plays a role in the regulation of cell proliferation. -
Tissue specificity
Detected in blood plasma, cerebrospinal fluid, milk, seminal plasma and colon mucosa. Detected in the germinal center of colon lymphoid nodules and in colon parasympathetic ganglia of the Auerbach plexus (at protein level). Ubiquitous. Detected in brain, testis, ovary, liver and pancreas, and at lower levels in kidney, heart, spleen and lung. -
Sequence similarities
Belongs to the clusterin family. -
Post-translational
modificationsIsoform 1 is proteolytically cleaved on its way through the secretory system, probably within the Golgi lumen.
Polyubiquitinated, leading to proteasomal degradation.
Heavily N-glycosylated. About 30% of the protein mass is comprised of complex N-linked carbohydrate. -
Cellular localization
Secreted. Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress and Nucleus. Cytoplasm. Mitochondrion membrane. Cytoplasm, cytosol. Microsome. Endoplasmic reticulum. Cytoplasmic vesicle, secretory vesicle, chromaffin granule. Isoforms lacking the N-terminal signal sequence have been shown to be cytoplasmic and/or nuclear. Secreted isoforms can retrotranslocate from the secretory compartments to the cytosol upon cellular stress. Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins. Detected at the mitochondrion membrane upon induction of apoptosis. - 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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Datasheet download
References (0)
ab194035 has not yet been referenced specifically in any publications.