Product nameRecombinant Human Clusterin alpha chain protein
See all Clusterin alpha chain proteins and peptides
Purity> 95 % SDS-PAGE.
Purity is greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE.
Endotoxin level< 0.100 Eu/µg
Expression systemHEK 293 cells
Protein lengthFull length protein
SequenceDQTVSDNELQEMSNQGSKYVNKEIQNAVNGVKQIKTLIEKTNEERKTLLS NLEEAKKKKEDALNETRESETKLKELPGVCNETMMALWEECKPCLKQTCM KFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLENDRQQTHM LDVMQDHFSRASSIIDELFQDRFFTREPQDTYHYLPFSLPHRRPHFFFPK SRIVRSLMPFSPYEPLNFHAMFQPFLEMIHEAQQAMDIHFHSPAFQHPPT EFIREGDDDRTVCREIRHNSTGCLRMKDQCDKCREILSVDCSTNNPSQAK LRRELDESLQVAERLTRKYNELLKSYQWKMLNTSSLLEQLNEQFNWVSRL ANLTQGEDQYYLRVTTVASHTSDSDVPSGVTEVVVKLFDSDPITVTVPVE VSRKNPKFMETVAEKALQEYRKKHREEVDHHHHHH
Predicted molecular weight51 kDa including tags
Amino acids23 to 449
TagsHis tag C-Terminus
- Anti-Clusterin antibody (ab104652)
- Anti-Clusterin antibody [CLI-9] (ab16077)
- Anti-6X His tag® antibody [HIS.H8] (ab18184)
- Anti-Clusterin antibody (ab39991)
- Anti-6X His tag® antibody [4D11] (ab5000)
- Anti-Clusterin antibody (ab69644)
- Anti-Clusterin antibody (ab7621)
- Anti-6X His tag® antibody (ab9108)
- Anti-Clusterin antibody [EPR2911] (ab92548)
Our Abpromise guarantee covers the use of ab151899 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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Preparation and Storage
Stability and Storage
Shipped at 4°C. The lyophilized protein is stable for a few weeks at room temperature. Store at -20°C long term.
Constituents: 99% Phosphate Buffer, 0.88% Sodium chloride
ReconstitutionAlways centrifuge tubes before opening. Do not mix by vortex or pipetting. Dissolve the lyophilized protein in 1X PBS. It is not recommended to reconstitute to a concentration less than 100 µg/ml.
Reconstituted protein solution can be stored at 4-7°C for 2-7 days. For long term storage aliquot and store at < -20°C.
- Aging-associated gene 4 protein
FunctionIsoform 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 specificityDetected 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 similaritiesBelongs to the clusterin family.
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 localizationNucleus. 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 and Secreted. Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress.
- Information by UniProt
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.
ab151899 has not yet been referenced specifically in any publications.