Product: Phospho-Blooms Syndrome Protein Blm (Thr99) Antibody
Catalog: AF3949
Description: Rabbit polyclonal antibody to Phospho-Blooms Syndrome Protein Blm (Thr99)
Application: ELISA(peptide)
Reactivity: Human
Mol.Wt.: 159kD(Calculated).
Uniprot: P54132
RRID: AB_2847672

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 100ul $350 In stock
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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:
Phospho-Blooms Syndrome Protein Blm (Thr99) Antibody detects endogenous levels of Blooms Syndrome Protein Blm only when phosphorylated at Thr99.
RRID:
AB_2847672
Cite Format: Affinity Biosciences Cat# AF3949, RRID:AB_2847672.
Conjugate:
Unconjugated.
Purification:
The antibody is from purified rabbit serum by affinity purification via sequential chromatography on phospho-peptide and non-phospho-peptide affinity columns.
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

Blm; BLM_HUMAN; Bloom syndrome; Bloom syndrome protein; Bloom syndrome RecQ helicase like; BS; DNA helicase; DNA helicase RecQ like type 2; MGC126616; MGC131618; MGC131620; RECQ 2; RECQ like; RecQ like type 2; RecQ protein like 3; RecQ protein-like 3; RecQ-like type 2; RecQ2; RECQL 2; RECQL 3; RECQL2; RECQL3; type 2;

Immunogens

Immunogen:

A synthesized peptide derived from human Blooms Syndrome Protein Blm around the phosphorylation site of Thr99.

Uniprot:
Gene(ID):
Sequence:
MAAVPQNNLQEQLERHSARTLNNKLSLSKPKFSGFTFKKKTSSDNNVSVTNVSVAKTPVLRNKDVNVTEDFSFSEPLPNTTNQQRVKDFFKNAPAGQETQRGGSKSLLPDFLQTPKEVVCTTQNTPTVKKSRDTALKKLEFSSSPDSLSTINDWDDMDDFDTSETSKSFVTPPQSHFVRVSTAQKSKKGKRNFFKAQLYTTNTVKTDLPPPSSESEQIDLTEEQKDDSEWLSSDVICIDDGPIAEVHINEDAQESDSLKTHLEDERDNSEKKKNLEEAELHSTEKVPCIEFDDDDYDTDFVPPSPEEIISASSSSSKCLSTLKDLDTSDRKEDVLSTSKDLLSKPEKMSMQELNPETSTDCDARQISLQQQLIHVMEHICKLIDTIPDDKLKLLDCGNELLQQRNIRRKLLTEVDFNKSDASLLGSLWRYRPDSLDGPMEGDSCPTGNSMKELNFSHLPSNSVSPGDCLLTTTLGKTGFSATRKNLFERPLFNTHLQKSFVSSNWAETPRLGKKNESSYFPGNVLTSTAVKDQNKHTASINDLERETQPSYDIDNFDIDDFDDDDDWEDIMHNLAASKSSTAAYQPIKEGRPIKSVSERLSSAKTDCLPVSSTAQNINFSESIQNYTDKSAQNLASRNLKHERFQSLSFPHTKEMMKIFHKKFGLHNFRTNQLEAINAALLGEDCFILMPTGGGKSLCYQLPACVSPGVTVVISPLRSLIVDQVQKLTSLDIPATYLTGDKTDSEATNIYLQLSKKDPIIKLLYVTPEKICASNRLISTLENLYERKLLARFVIDEAHCVSQWGHDFRQDYKRMNMLRQKFPSVPVMALTATANPRVQKDILTQLKILRPQVFSMSFNRHNLKYYVLPKKPKKVAFDCLEWIRKHHPYDSGIIYCLSRRECDTMADTLQRDGLAALAYHAGLSDSARDEVQQKWINQDGCQVICATIAFGMGIDKPDVRFVIHASLPKSVEGYYQESGRAGRDGEISHCLLFYTYHDVTRLKRLIMMEKDGNHHTRETHFNNLYSMVHYCENITECRRIQLLAYFGENGFNPDFCKKHPDVSCDNCCKTKDYKTRDVTDDVKSIVRFVQEHSSSQGMRNIKHVGPSGRFTMNMLVDIFLGSKSAKIQSGIFGKGSAYSRHNAERLFKKLILDKILDEDLYINANDQAIAYVMLGNKAQTVLNGNLKVDFMETENSSSVKKQKALVAKVSQREEMVKKCLGELTEVCKSLGKVFGVHYFNIFNTVTLKKLAESLSSDPEVLLQIDGVTEDKLEKYGAEVISVLQKYSEWTSPAEDSSPGISLSSSRGPGRSAAEELDEEIPVSSHYFASKTRNERKRKKMPASQRSKRRKTASSGSKAKGGSATCRKISSKTKSSSIIGSSSASHTSQATSGANSKLGIMAPPKPINRPFLKPSYAFS

PTMs - P54132 As Substrate

Site PTM Type Enzyme
Phosphorylation
S17 Phosphorylation
T20 Phosphorylation
K24 Sumoylation
K24 Ubiquitination
S26 Phosphorylation
S28 Phosphorylation
K31 Sumoylation
S33 Phosphorylation
T36 Phosphorylation
K38 Methylation
K39 Methylation
K40 Sumoylation
S43 Phosphorylation
S48 Phosphorylation
T50 Phosphorylation
S53 Phosphorylation
K56 Sumoylation
T57 Phosphorylation
T68 Phosphorylation
S72 Phosphorylation
S74 Phosphorylation
K91 Sumoylation
K91 Ubiquitination
T99 Phosphorylation Q13535 (ATR) , Q13315 (ATM)
K105 Sumoylation
K105 Ubiquitination
T114 Phosphorylation
T122 Phosphorylation Q13535 (ATR) , Q13315 (ATM)
T125 Phosphorylation
T127 Phosphorylation
K129 Sumoylation
K129 Ubiquitination
S131 Phosphorylation
S142 Phosphorylation
S143 Phosphorylation
S144 Phosphorylation P33981 (TTK)
K167 Ubiquitination
S168 Phosphorylation
T171 Phosphorylation P49841 (GSK3B)
S175 Phosphorylation P24941 (CDK2)
T182 Phosphorylation O96017 (CHEK2) , O14757 (CHEK1)
K195 Methylation
K195 Sumoylation
Y199 Phosphorylation
T201 Phosphorylation
K225 Ubiquitination
K259 Ubiquitination
S269 Phosphorylation
S282 Phosphorylation
Y296 Phosphorylation
S304 Phosphorylation
K317 Sumoylation
K323 Ubiquitination
T327 Phosphorylation
S328 Phosphorylation
K331 Sumoylation
K331 Ubiquitination
S336 Phosphorylation
T337 Phosphorylation
S338 Phosphorylation Q8NG66 (NEK11)
K339 Ubiquitination
S343 Phosphorylation
K344 Sumoylation
K344 Ubiquitination
K347 Sumoylation
S349 Phosphorylation
S358 Phosphorylation
T359 Phosphorylation
S367 Phosphorylation
K390 Ubiquitination
K392 Sumoylation
K409 Sumoylation
K409 Ubiquitination
T412 Phosphorylation
K418 Sumoylation
K418 Ubiquitination
S419 Phosphorylation
S422 Phosphorylation
S426 Phosphorylation
S434 Phosphorylation
S443 Phosphorylation
S449 Phosphorylation
S456 Phosphorylation
S462 Phosphorylation
S464 Phosphorylation
T473 Phosphorylation
K476 Ubiquitination
S480 Phosphorylation
K484 Sumoylation
K484 Ubiquitination
K498 Sumoylation
S499 Phosphorylation
S502 Phosphorylation
T508 Phosphorylation
K514 Sumoylation
K514 Ubiquitination
K531 Ubiquitination
K535 Ubiquitination
T537 Phosphorylation
S539 Phosphorylation O14757 (CHEK1)
S550 Phosphorylation
Y551 Phosphorylation
K578 Ubiquitination
S579 Phosphorylation
K588 Sumoylation
K588 Ubiquitination
K594 Sumoylation
K594 Ubiquitination
S601 Phosphorylation
K604 Ubiquitination
K629 Ubiquitination
S646 Phosphorylation O14757 (CHEK1) , PR:O14757 (hCHEK1)
K653 Ubiquitination
K657 Acetylation
K661 Acetylation
K662 Acetylation
K662 Sumoylation
K662 Ubiquitination
Y699 Phosphorylation
S714 Phosphorylation P06493 (CDK1)
Y736 Phosphorylation
K741 Ubiquitination
K755 Ubiquitination
T766 Phosphorylation P06493 (CDK1)
K769 Ubiquitination
S773 Phosphorylation
K820 Sumoylation
K820 Ubiquitination
T830 Phosphorylation
T832 Phosphorylation
K839 Sumoylation
K839 Ubiquitination
K863 Acetylation
K863 Ubiquitination
K873 Sumoylation
K873 Ubiquitination
T903 Phosphorylation
T907 Phosphorylation
K1057 Ubiquitination
K1082 Sumoylation
K1082 Ubiquitination
S1083 Phosphorylation
K1125 Sumoylation
K1125 Ubiquitination
K1133 Ubiquitination
S1197 Phosphorylation
K1199 Sumoylation
K1199 Ubiquitination
K1207 Ubiquitination
K1217 Ubiquitination
K1273 Sumoylation
K1273 Ubiquitination
S1280 Phosphorylation
S1290 Phosphorylation P33981 (TTK)
S1295 Phosphorylation
S1296 Phosphorylation P33981 (TTK)
S1303 Phosphorylation
S1304 Phosphorylation
S1310 Phosphorylation
K1329 Ubiquitination
K1372 Sumoylation
K1372 Ubiquitination
S1375 Phosphorylation
S1383 Phosphorylation
K1411 Acetylation
S1417 Phosphorylation

Research Backgrounds

Function:

ATP-dependent DNA helicase that unwinds single- and double-stranded DNA in a 3'-5' direction. Participates in DNA replication and repair. Involved in 5'-end resection of DNA during double-strand break (DSB) repair: unwinds DNA and recruits DNA2 which mediates the cleavage of 5'-ssDNA. Negatively regulates sister chromatid exchange (SCE). Stimulates DNA 4-way junction branch migration and DNA Holliday junction dissolution. Binds single-stranded DNA (ssDNA), forked duplex DNA and DNA Holliday junction.

PTMs:

Phosphorylated in response to DNA damage. Phosphorylation requires the FANCA-FANCC-FANCE-FANCF-FANCG protein complex, as well as the presence of RMI1.

Subcellular Location:

Nucleus.
Note: Together with SPIDR, is redistributed in discrete nuclear DNA damage-induced foci following hydroxyurea (HU) or camptothecin (CPT) treatment. Accumulated at sites of DNA damage in a RMI complex- and SPIDR-dependent manner.

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

Monomer. Homodimer (via N-terminus). Homotetramer (via N-terminus); dimer of dimers. Homohexamer (via N-terminus). Self-association negatively regulates DNA unwinding amplitude and rate. Oligomeric complexes dissociate into monomer in presence of ATP. Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBS1 protein complex. This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains. Interacts with ubiquitinated FANCD2. Interacts with RMI complex. Interacts directly with RMI1 (via N-terminal region) component of RMI complex. Interacts with SUPV3L1. Found in a complex, at least composed of BLM, RAD51 and SPIDR; the complex formation is mediated by SPIDR. Interacts with TOP3A (via N-terminal region). Interacts with SPIDR (via C-terminal region); the interaction is direct and required to target BLM to sites of DNA damage.

Family&Domains:

The N-terminal region mediates dimerization and homooligomerization (PubMed:28228481). Both the helicase ATP-binding domain and the helicase C-terminal domain form intramolecular interactions with the HRDC domain in a ATP-dependent manner (PubMed:25901030). The HRDC domain is required for single-stranded DNA (ssDNA) and DNA Holliday junction binding (PubMed:20639533).

Belongs to the helicase family. RecQ subfamily.

Research Fields

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

· Genetic Information Processing > Replication and repair > Fanconi anemia pathway.

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