Description

  • Product name

    Recombinant Human Clusterin protein (Fc Chimera)
    See all Clusterin proteins and peptides
  • Purity

    > 95 % SDS-PAGE.

  • Endotoxin level

    < 1.000 Eu/µg
  • Expression system

    Mammalian
  • Accession

  • Protein length

    Full length protein
  • Animal free

    No
  • Nature

    Recombinant
    • Species

      Human
    • Sequence

      DQTVSDNELQEMSNQGSKYVNKEIQNAVNGVKQIKTLIEKTNEERKTLLS NLEEAKKKKEDALNETRESETKLKELPGVCNETMMALWEECKPCLKQTCM KFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLENDRQQTHM LDVMQDHFSRASSIIDELFQDRFFTREPQDTYHYLPFSLPHRRPHFFFPK SRIVRSLMPFSPYEPLNFHAMFQPFLEMIHEAQQAMDIHFHSPAFQHPPT EFIREGDDDRTVCREIRHNSTGCLRMKDQCDKCREILSVDCSTNNPSQAK LRRELDESLQVAERLTRKYNELLKSYQWKMLNTSSLLEQLNEQFNWVSRL ANLTQGEDQYYLRVTTVASHTSDSDVPSGVTEVVVKLFDSDPITVTVPVE VSRKNPKFMETVAEKALQEYRKKHREEVDDIEGRMDEPKSCDKTHTCPPC PAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYV DGVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALP APIEKTISKAKGQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAV EWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKSRWQQGNVFSCSVMH EALHNHYTQKSLSLSPGKHHHHHH
    • Predicted molecular weight

      78 kDa including tags
    • Amino acids

      23 to 449
    • Tags

      His tag C-Terminus
    • Additional sequence information

      FC-6xHis tag

Associated products

Specifications

Our Abpromise guarantee covers the use of ab185421 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    SDS-PAGE

    HPLC

  • Form

    Lyophilised
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. The lyophilized protein is stable for a few weeks at room temperature. Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle.

    pH: 7.4
    Constituent: 100% PBS

  • Reconstitution
    Always 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 3X PBS. Aliquot the reconstituted solution to minimize freeze-thaw cycles.

General Info

  • Alternative names

    • 40
    • AAG 4
    • AAG4
    • Aging associated protein 4
    • Aging-associated gene 4 protein
    • AI893575
    • APO J
    • Apo-J
    • APOJ
    • ApoJalpha
    • ApoJbeta
    • Apolipoprotein J
    • ApolipoproteinJ
    • CLI
    • CLU
    • CLU1
    • CLU2
    • CLUS_HUMAN
    • Clusterin
    • Clusterin alpha chain
    • Clusterin beta chain
    • Complement associated protein SP 40
    • Complement associated protein SP 40 40
    • Complement associated protein SP40
    • Complement cytolysis inhibitor
    • Complement cytolysis inhibitor a chain
    • Complement cytolysis inhibitor b chain
    • Complement lysis inhibitor
    • Complement-associated protein SP-40
    • D14Ucla3
    • Dimeric acid glycoprotein
    • Glycoprotein 80
    • Glycoprotein III
    • GP80
    • Ku70-binding protein 1
    • KUB 1
    • KUB1
    • MGC24903
    • NA1/NA2
    • RATTRPM2B
    • SGP 2
    • SGP2
    • SP 40
    • SP40
    • Sugp-2
    • Sulfated glycoprotein 2
    • Testosterone repressed prostate message 2
    • Testosterone-repressed prostate message 2
    • TRPM 2
    • TRPM-2
    • TRPM2
    • TRPM2B
    • Trpmb
    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
    modifications

    Isoform 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

References

ab185421 has not yet been referenced specifically in any publications.

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