Product: CLU Antibody
Catalog: DF6421
Description: Rabbit polyclonal antibody to CLU
Application: WB IHC IF/ICC
Reactivity: Human, Mouse, Rat
Mol.Wt.: 53kDa; 52kD(Calculated).
Uniprot: P10909
RRID: AB_2838384

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Product Info

Source:
Rabbit
Application:
WB 1:500-1:2000, IHC 1:50-1:200, IF/ICC 1:100-1:500
*The optimal dilutions should be determined by the end user.
*Tips:

WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.

Reactivity:
Human,Mouse,Rat
Clonality:
Polyclonal
Specificity:
CLU Antibody detects endogenous levels of total CLU.
RRID:
AB_2838384
Cite Format: Affinity Biosciences Cat# DF6421, RRID:AB_2838384.
Conjugate:
Unconjugated.
Purification:
The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).
Storage:
Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol. Store at -20 °C. Stable for 12 months from date of receipt.
Alias:

Fold/Unfold

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 alpha chain; Clusterin; Clusterin beta chain; Complement associated protein SP 40 40; Complement associated protein SP 40; Complement associated protein SP40; Complement cytolysis inhibitor a chain; Complement cytolysis inhibitor; 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;

Immunogens

Immunogen:
Uniprot:
Gene(ID):
Expression:
P10909 CLUS_HUMAN:

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.

Description:
The protein encoded by this gene is a secreted chaperone that can under some stress conditions also be found in the cell cytosol. It has been suggested to be involved in several basic biological events such as cell death, tumor progression, and neurodegenerative disorders. Alternate splicing results in both coding and non-coding variants.[provided by RefSeq, May 2011]
Sequence:
MMKTLLLFVGLLLTWESGQVLGDQTVSDNELQEMSNQGSKYVNKEIQNAVNGVKQIKTLIEKTNEERKTLLSNLEEAKKKKEDALNETRESETKLKELPGVCNETMMALWEECKPCLKQTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLENDRQQTHMLDVMQDHFSRASSIIDELFQDRFFTREPQDTYHYLPFSLPHRRPHFFFPKSRIVRSLMPFSPYEPLNFHAMFQPFLEMIHEAQQAMDIHFHSPAFQHPPTEFIREGDDDRTVCREIRHNSTGCLRMKDQCDKCREILSVDCSTNNPSQAKLRRELDESLQVAERLTRKYNELLKSYQWKMLNTSSLLEQLNEQFNWVSRLANLTQGEDQYYLRVTTVASHTSDSDVPSGVTEVVVKLFDSDPITVTVPVEVSRKNPKFMETVAEKALQEYRKKHREE

PTMs - P10909 As Substrate

Site PTM Type Enzyme
K54 Ubiquitination
K57 Sumoylation
K57 Ubiquitination
K68 Ubiquitination
T69 Phosphorylation
S72 Phosphorylation
K78 Acetylation
K78 Ubiquitination
N86 N-Glycosylation
T88 Phosphorylation
N103 N-Glycosylation
S133 Phosphorylation
N145 N-Glycosylation
S185 Phosphorylation
S210 O-Glycosylation
K222 Ubiquitination
N291 N-Glycosylation
S310 Phosphorylation
S314 Phosphorylation
T315 Phosphorylation
S319 Phosphorylation
K322 Ubiquitination
K340 Ubiquitination
K346 Ubiquitination
N354 N-Glycosylation
N374 N-Glycosylation
T387 Phosphorylation
S391 Phosphorylation
T393 Phosphorylation
S394 Phosphorylation
S396 Phosphorylation
S412 Phosphorylation

Research Backgrounds

Function:

Functions as extracellular chaperone that prevents aggregation of non native 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. Protects cells against apoptosis and against cytolysis by complement. Intracellular forms 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. A mitochondrial form suppresses BAX-dependent release of cytochrome c into the cytoplasm and inhibit apoptosis. Plays a role in the regulation of cell proliferation. An intracellular form suppresses stress-induced apoptosis by stabilizing mitochondrial membrane integrity through interaction with HSPA5. Secreted form does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity. Secreted form act as an important modulator during neuronal differentiation through interaction with STMN3 (By similarity). Plays a role in the clearance of immune complexes that arise during cell injury (By similarity).

Does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity.

Does not affect caspase or BAX-mediated intrinsic apoptosis and TNF-induced NF-kappa-B-activity. Promotes cell death through interaction with BCL2L1 that releases and activates BAX.

PTMs:

Proteolytically cleaved on its way through the secretory system, probably within the Golgi lumen. Proteolytic cleavage is not necessary for its chaperone activity. All non-secreted forms are not proteolytically cleaved. Chaperone activity of uncleaved forms is dependent on a non-reducing envoronment.

Polyubiquitinated, leading to proteasomal degradation. Under cellular stress, the intracellular level of cleaved form is reduced due to proteasomal degradation.

Extensively glycosylated with sulfated N-linked carbohydrates. About 30% of the protein mass is comprised of complex N-linked carbohydrate. Endoplasmic reticulum (ER) stress induces changes in glycosylation status and increases level of hypoglycosylated forms. Core carbohydrates are essential for chaperone activity. Non-secreted forms are hypoglycosylated or unglycosylated.

Subcellular Location:

Secreted.
Note: Can retrotranslocate from the secretory compartments to the cytosol upon cellular stress.

Cytoplasm.
Note: Keeps cytoplasmic localization in stressed and unstressed cell.

Cytoplasm.
Note: Keeps cytoplasmic localization in stressed and unstressed cell.

Nucleus. Cytoplasm. Mitochondrion membrane>Peripheral membrane protein>Cytoplasmic side. Cytoplasm>Cytosol. Microsome. Endoplasmic reticulum. Mitochondrion. Mitochondrion membrane. Cytoplasm>Perinuclear region. Cytoplasmic vesicle>Secretory vesicle>Chromaffin granule.
Note: Secreted isoforms can retrotranslocate from the secretory compartments to the cytosol upon cellular stress (PubMed:17451556). Detected in perinuclear foci that may be aggresomes containing misfolded, ubiquitinated proteins (PubMed:20068069). Detected at the mitochondrion membrane upon induction of apoptosis (PubMed:17689225). Under ER stress, a immaturely glycosylated pre-secreted form retrotranslocates from the endoplasmic reticulum (ER)-Golgi network to the cytoplasm to localize in the mitochondria through HSPA5 interaction (PubMed:22689054). ER stress reduces secretion (PubMed:22689054). Under the stress, minor amounts of non-secreted forms accumulate in cytoplasm (PubMed:24073260, PubMed:22689054, PubMed:17451556). Non-secreted forms emerge mainly from failed translocation, alternative splicing or non-canonical initiation start codon (PubMed:24073260, PubMed:12551933).

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionSubcellular location
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.

Subunit Structure:

Antiparallel disulfide-linked heterodimer of an alpha chain and a beta chain. Self-associates and forms higher oligomers. Interacts with a broad range of misfolded proteins, including APP, APOC2 and LYZ. Slightly acidic pH promotes interaction with misfolded proteins. Forms high-molecular weight oligomers upon interaction with misfolded proteins. Interacts with APOA1, LRP2, CLUAP1 and PON1. Interacts with the complement complex. Interacts (via alpha chain) with XRCC6 (By similarity). Interacts with SYVN1, COMMD1, BTRC, CUL1 and with ubiquitin and SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes. Interacts (via alpha chain) with BAX in stressed cells, where BAX undergoes a conformation change leading to association with the mitochondrial membrane. Does not interact with BAX in unstressed cells. Found in a complex with LTF, CLU, EPPIN and SEMG1. Interacts (immaturely glycosylated pre-secreted form) with HSPA5; this interaction promotes CLU stability and facilitates stress-induced CLU retrotranslocation from the secretory pathway to the mitochondria, thereby reducing stress-induced apoptosis by stabilizing mitochondrial membrane integrity. Interacts (isoform 4) with BCL2L1; this interaction releases and activates BAX and promotes cell death. Interacts with TGFBR2 and ACVR1. Interacts (secreted form) with STMN3; this interaction may act as an important modulator during neuronal differentiation (By similarity).

Family&Domains:

Belongs to the clusterin family.

Research Fields

· Organismal Systems > Immune system > Complement and coagulation cascades.   (View pathway)

References

1). Serum complement proteomics reveal biomarkers for hypertension disorder of pregnancy and the potential role of Clusterin. Reproductive Biology and Endocrinology, 2021 (PubMed: 33874952) [IF=4.4]

Application: WB    Species: Human    Sample: TEV-1 cells

Fig. 5 CLU is upregulated in the placenta from PE deliveries. a, Fixed placental tissue sections were used for immunohistochemical analysis. Student’s t-test, n = 6. b, LPS stimulation leads to increased expression of CLU in TEV-1 cells. The upper part shows a representative western blot band and below is the relative quantification after normalization. One-way ANOVA, n = 3. c, Total placental RNA was extracted for relative quantification of CLU mRNA levels by qRT-PCR (n = 19). d, Total placental RNA was extracted for relative quantification of MMP9 mRNA levels (n = 19). e, Placental CLU gene expression was negatively correlated with MMP9 via Pearson’s correlation. f, CLU inhibits TEV-1 cell invasion. The left panel is a representative micrograph of the Matrigel Transwell assay treated with CLU. The right panel represents quantitative results of cell invasion, and data are presented as the mean ± SD and were analysed by one-way ANOVA, n = 3. *P < 0.05, **P < 0.01, ***P < 0.001. PE = Preeclampsia, N=Normal pregnancy, CLU=Clusterin, MMP9 = Matrix metalloproteinases 9

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