Product: CtIP Antibody
Catalog: AF6546
Description: Rabbit polyclonal antibody to CtIP
Application: ELISA(peptide)
Reactivity: Human
Mol.Wt.: 110kD; 102kD(Calculated).
Uniprot: Q99708
RRID: AB_2847270

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Product Info

Source:
Rabbit
Application:
ELISA(peptide) 1:20000-1:40000
*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
Clonality:
Polyclonal
Specificity:
CtIP Antibody detects endogenous levels of total CtIP.
RRID:
AB_2847270
Cite Format: Affinity Biosciences Cat# AF6546, RRID:AB_2847270.
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

COM1; COM1_HUMAN; CtBP interacting protein; CtBP-interacting protein; CtIP; DNA endonuclease RBBP8; JWDS; RB binding protein 8 endonuclease; RBBP-8; RBBP8; Retinoblastoma-binding protein 8; Retinoblastoma-interacting protein and myosin-like; Rim; SAE2; SCKL2; Sporulation in the absence of SPO11 protein 2 homolog;

Immunogens

Immunogen:

A synthesized peptide derived from human CtIP.

Uniprot:
Gene(ID):
Expression:
Q99708 CTIP_HUMAN:

Expressed in ER-positive breast cancer lines, but tends to be down-regulated ER-negative cells (at protein level).

Sequence:
MNISGSSCGSPNSADTSSDFKDLWTKLKECHDREVQGLQVKVTKLKQERILDAQRLEEFFTKNQQLREQQKVLHETIKVLEDRLRAGLCDRCAVTEEHMRKKQQEFENIRQQNLKLITELMNERNTLQEENKKLSEQLQQKIENDQQHQAAELECEEDVIPDSPITAFSFSGVNRLRRKENPHVRYIEQTHTKLEHSVCANEMRKVSKSSTHPQHNPNENEILVADTYDQSQSPMAKAHGTSSYTPDKSSFNLATVVAETLGLGVQEESETQGPMSPLGDELYHCLEGNHKKQPFEESTRNTEDSLRFSDSTSKTPPQEELPTRVSSPVFGATSSIKSGLDLNTSLSPSLLQPGKKKHLKTLPFSNTCISRLEKTRSKSEDSALFTHHSLGSEVNKIIIQSSNKQILINKNISESLGEQNRTEYGKDSNTDKHLEPLKSLGGRTSKRKKTEEESEHEVSCPQASFDKENAFPFPMDNQFSMNGDCVMDKPLDLSDRFSAIQRQEKSQGSETSKNKFRQVTLYEALKTIPKGFSSSRKASDGNCTLPKDSPGEPCSQECIILQPLNKCSPDNKPSLQIKEENAVFKIPLRPRESLETENVLDDIKSAGSHEPIKIQTRSDHGGCELASVLQLNPCRTGKIKSLQNNQDVSFENIQWSIDPGADLSQYKMDVTVIDTKDGSQSKLGGETVDMDCTLVSETVLLKMKKQEQKGEKSSNEERKMNDSLEDMFDRTTHEEYESCLADSFSQAADEEEELSTATKKLHTHGDKQDKVKQKAFVEPYFKGDERETSLQNFPHIEVVRKKEERRKLLGHTCKECEIYYADMPAEEREKKLASCSRHRFRYIPPNTPENFWEVGFPSTQTCMERGYIKEDLDPCPRPKRRQPYNAIFSPKGKEQKT

PTMs - Q99708 As Substrate

Site PTM Type Enzyme
S4 Phosphorylation
S10 Phosphorylation
S17 Phosphorylation
S18 Phosphorylation
K62 Ubiquitination
K115 Sumoylation
S163 Phosphorylation
S231 Phosphorylation
S233 Phosphorylation
T245 Phosphorylation
S276 Phosphorylation
S309 Phosphorylation
K314 Ubiquitination
T315 Phosphorylation P24941 (CDK2)
T323 Phosphorylation
S326 Phosphorylation
S327 Phosphorylation
S345 Phosphorylation
S347 Phosphorylation
S349 Phosphorylation
K360 Ubiquitination
T361 Phosphorylation
K378 Sumoylation
K378 Ubiquitination
S379 Phosphorylation
K410 Ubiquitination
T422 Phosphorylation
Y424 Phosphorylation
S428 Phosphorylation
K432 Acetylation
K438 Sumoylation
K438 Ubiquitination
S439 Phosphorylation
K449 Sumoylation
T450 Phosphorylation
K513 Acetylation
K515 Acetylation
Y522 Phosphorylation
K526 Acetylation
K526 Ubiquitination
K530 Ubiquitination
S539 Phosphorylation
S549 Phosphorylation
S555 Phosphorylation
S568 Phosphorylation
K578 Sumoylation
K585 Ubiquitination
S593 Phosphorylation
K604 Acetylation
K604 Sumoylation
K604 Ubiquitination
K613 Ubiquitination
K640 Ubiquitination
S649 Phosphorylation
S664 Phosphorylation Q13315 (ATM)
S679 Phosphorylation
S723 Phosphorylation
S745 Phosphorylation Q13315 (ATM)
K760 Ubiquitination
K774 Sumoylation
K782 Ubiquitination
S836 Phosphorylation
T847 Phosphorylation P24941 (CDK2)
T859 Phosphorylation Q13535 (ATR)
K869 Sumoylation
S889 Phosphorylation

Research Backgrounds

Function:

Endonuclease that cooperates with the MRE11-RAD50-NBN (MRN) complex in DNA-end resection, the first step of double-strand break (DSB) repair through the homologous recombination (HR) pathway. HR is restricted to S and G2 phases of the cell cycle and preferentially repairs DSBs resulting from replication fork collapse. Key determinant of DSB repair pathway choice, as it commits cells to HR by preventing classical non-homologous end-joining (NHEJ). Functions downstream of the MRN complex and ATM, promotes ATR activation and its recruitment to DSBs in the S/G2 phase facilitating the generation of ssDNA. Component of the BRCA1-RBBP8 complex that regulates CHEK1 activation and controls cell cycle G2/M checkpoints on DNA damage. During immunoglobulin heavy chain class-switch recombination, promotes microhomology-mediated alternative end joining (A-NHEJ) and plays an essential role in chromosomal translocations (By similarity).

PTMs:

Acetylated. Deacetylation by SIRT6 upon DNA damage promotes DNA end resection.

Hyperphosphorylation upon ionizing radiation results in dissociation from BRCA1. Phosphorylation at Thr-847 by CDK1 is essential for the recruitment to DNA and the DNA repair function. Phosphorylated on Ser-327 as cells enter G2 phase. This phosphorylation is required for binding BRCA1 and for the G2/M DNA damage transition checkpoint control. Phosphorylation at Thr-315, probably catalyzed by CDK2, is required for PIN1-binding, while phosphorylation at Ser-276 serves as a PIN1 isomerization site. Phosphorylation at Thr-315 is cell-cycle dependent. It steadily increases during S phase, peaks at late S/G2 phase, and drops at G1.

Ubiquitinated. Ubiquitination at multiple sites by BRCA1 (via its N-terminal RING domain) does not lead to its proteasomal degradation but instead the ubiquitinated RBBP8 binds to chromatin following DNA damage and may play a role in G2/M checkpoint control. Ubiquitinated by RNF138 at its N-terminus. Ubiquitinated through 'Lys-48' by the E3 CUL3-KLHL15 complex; this modification leads to proteasomal degradation. Ubiquitinated by the E3 FZR1/APC/C complex; this modification leads to proteasomal degradation.

Subcellular Location:

Nucleus. Chromosome.
Note: Associates with sites of DNA damage in S/G2 phase (PubMed:10764811, PubMed:25349192). Ubiquitinated RBBP8 binds to chromatin following DNA damage (PubMed:16818604).

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

Expressed in ER-positive breast cancer lines, but tends to be down-regulated ER-negative cells (at protein level).

Subunit Structure:

Homodimer; dimerizes via the coiled coil domain. Interacts (via the PXDLS motif) with CTBP1; the interaction is disrupted via binding of the adenovirus E1A to CTBP1. Component of the BRCA1-RBBP8 complex. Interacts (the Ser-327 phosphorylated form) with BRCA1 (via the C-terminal BRCA1 domains): the interaction occurs in the G2 phase, ubiquitinates RBBP8 and involves RBBP8 in BRCA1-dependent G2/M checkpoint control on DNA damage. Interacts with RB1. Interacts with the MRN complex. Interacts directly with MRE11; the interaction is required for efficient homologous recombination (HR) and regulation of the MRN complex. Interacts directly with RAD50. Interacts directly with NBN. Interacts with SIRT6; the interaction deacetylates RBBP8 upon DNA damage. Interacts with LM04 (via the LIM zinc-binding 1 domain). Interacts with SIAH1. Interacts with RNF138. Interacts with EXD2. Interacts with CUL3 and KLHL15; this interaction leads to RBBP8 proteasomal degradation. Directly interacts with PIN1; this interaction depends upon RBBP8 phosphorylation, predominantly at Thr-315. Interacts with FZR1; this interaction leads to APC/C-mediated RBBP8 proteasomal degradation. Interacts with AUNIP; leading to recruit RBBP8 to sites of DNA damage. Interacts with SAMHD1.

Family&Domains:

The PXDLS motif binds to a cleft in CtBP proteins.

The damage-recruitment motif is required for DNA binding and translocation to sites of DNA damage.

Belongs to the COM1/SAE2/CtIP family.

Research Fields

· Genetic Information Processing > Replication and repair > Homologous recombination.

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