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  • Product Name
    HIF1A Antibody
  • Catalog No.
    AF1009
  • Source
    Rabbit
  • Application
    WB,IHC,IF/ICC,ELISA
  • Reactivity:
    Human, Mouse, Rat
  • Prediction:
    Pig(100%), Bovine(100%), Horse(100%), Rabbit(100%)
  • UniProt
  • Mol.Wt.
    120kDa
  • Concentration
    1mg/ml
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Product Information

Alternative Names:Expand▼

ARNT interacting protein; ARNT-interacting protein; Basic helix loop helix PAS protein MOP1; Basic-helix-loop-helix-PAS protein MOP1; bHLHe78; Class E basic helix-loop-helix protein 78; HIF 1A; HIF 1alpha; HIF-1-alpha; HIF1 A; HIF1 Alpha; HIF1; HIF1-alpha; HIF1A; HIF1A_HUMAN; Hypoxia inducible factor 1 alpha; Hypoxia inducible factor 1 alpha isoform I.3; Hypoxia inducible factor 1 alpha subunit; Hypoxia inducible factor 1 alpha subunit basic helix loop helix transcription factor; Hypoxia inducible factor 1, alpha subunit (basic helix loop helix transcription factor); Hypoxia inducible factor1alpha; Hypoxia-inducible factor 1-alpha; Member of PAS protein 1; Member of PAS superfamily 1; Member of the PAS Superfamily 1; MOP 1; MOP1; PAS domain-containing protein 8; PASD 8; PASD8;

Applications:

WB 1:500-1:2000, IHC 1:50-1:200, IF 1:200, ELISA(peptide) 1:20000-1:40000

Reactivity:

Human, Mouse, Rat

Predicted Reactivity:

Pig(100%), Bovine(100%), Horse(100%), Rabbit(100%)

Source:

Rabbit

Clonality:

Polyclonal

Purification:

The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).

Specificity:

HIF1a antibody detects endogenous levels of HIF1a.

Format:

Liquid

Concentration:

1mg/ml

Storage Condition and Buffer:

Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.Store at -20 °C.Stable for 15 months from date of receipt.

Immunogen Information

Immunogen:

A synthesized peptide derived from human HIF1A, corresponding to a region within the internal amino acids.

Uniprot:



>>Visit The Human Protein Atlas

Gene id:

Molecular Weight:

Observed Mol.Wt.: 120kDa.
Predicted Mol.Wt.: 93kDa.

Subcellular Location:

Cytoplasm. Nucleus. Cytoplasmic in normoxia, nuclear translocation in response to hypoxia. Colocalizes with SUMO1 in the nucleus, under hypoxia.

Tissue Specificity:

Expressed in most tissues with highest levels in kidney and heart. Overexpressed in the majority of common human cancers and their metastases, due to the presence of intratumoral hypoxia and as a result of mutations in genes encoding oncoproteins and tumor suppressors. A higher level expression seen in pituitary tumors as compared to the pituitary gland.

Description:

Cell growth and viability is compromised by oxygen deprivation (hypoxia). Hypoxia-inducible factors, including HIF-1α, Arnt 1 (also designated HIF-1β), EPAS-1 (also designated HIF-2α) and HIF-3α, induce glycolysis, erythropoiesis and angiogenesis in order to restore oxygen homeostasis. Hypoxia-inducible factors are members of the Per-Arnt-Sim (PAS) domain transcription factor family.

Sequence:
        10         20         30         40         50
MEGAGGANDK KKISSERRKE KSRDAARSRR SKESEVFYEL AHQLPLPHNV
60 70 80 90 100
SSHLDKASVM RLTISYLRVR KLLDAGDLDI EDDMKAQMNC FYLKALDGFV
110 120 130 140 150
MVLTDDGDMI YISDNVNKYM GLTQFELTGH SVFDFTHPCD HEEMREMLTH
160 170 180 190 200
RNGLVKKGKE QNTQRSFFLR MKCTLTSRGR TMNIKSATWK VLHCTGHIHV
210 220 230 240 250
YDTNSNQPQC GYKKPPMTCL VLICEPIPHP SNIEIPLDSK TFLSRHSLDM
260 270 280 290 300
KFSYCDERIT ELMGYEPEEL LGRSIYEYYH ALDSDHLTKT HHDMFTKGQV
310 320 330 340 350
TTGQYRMLAK RGGYVWVETQ ATVIYNTKNS QPQCIVCVNY VVSGIIQHDL
360 370 380 390 400
IFSLQQTECV LKPVESSDMK MTQLFTKVES EDTSSLFDKL KKEPDALTLL
410 420 430 440 450
APAAGDTIIS LDFGSNDTET DDQQLEEVPL YNDVMLPSPN EKLQNINLAM
460 470 480 490 500
SPLPTAETPK PLRSSADPAL NQEVALKLEP NPESLELSFT MPQIQDQTPS
510 520 530 540 550
PSDGSTRQSS PEPNSPSEYC FYVDSDMVNE FKLELVEKLF AEDTEAKNPF
560 570 580 590 600
STQDTDLDLE MLAPYIPMDD DFQLRSFDQL SPLESSSASP ESASPQSTVT
610 620 630 640 650
VFQQTQIQEP TANATTTTAT TDELKTVTKD RMEDIKILIA SPSPTHIHKE
660 670 680 690 700
TTSATSSPYR DTQSRTASPN RAGKGVIEQT EKSHPRSPNV LSVALSQRTT
710 720 730 740 750
VPEEELNPKI LALQNAQRKR KMEHDGSLFQ AVGIGTLLQQ PDDHAATTSL
760 770 780 790 800
SWKRVKGCKS SEQNGMEQKT IILIPSDLAC RLLGQSMDES GLPQLTSYDC
810 820
EVNAPIQGSR NLLQGEELLR ALDQVN

Background

Function:

Functions as a master transcriptional regulator of the adaptive response to hypoxia. Under hypoxic conditions, activates the transcription of over 40 genes, including erythropoietin, glucose transporters, glycolytic enzymes, vascular endothelial growth factor, HILPDA, and other genes whose protein products increase oxygen delivery or facilitate metabolic adaptation to hypoxia. Plays an essential role in embryonic vascularization, tumor angiogenesis and pathophysiology of ischemic disease. Binds to core DNA sequence 5'-[AG]CGTG-3' within the hypoxia response element (HRE) of target gene promoters. Activation requires recruitment of transcriptional coactivators such as CREBBP and EP300. Activity is enhanced by interaction with both, NCOA1 or NCOA2. Interaction with redox regulatory protein APEX seems to activate CTAD and potentiates activation by NCOA1 and CREBBP. Involved in the axonal distribution and transport of mitochondria in neurons during hypoxia.

Post-translational Modifications:

S-nitrosylation of Cys-800 may be responsible for increased recruitment of p300 coactivator necessary for transcriptional activity of HIF-1 complex.Requires phosphorylation for DNA-binding. Phosphorylation at Ser-247 by CSNK1D/CK1 represses kinase activity and impairs ARNT binding. Phosphorylation by GSK3-beta and PLK3 promote degradation by the proteasome.Sumoylated; with SUMO1 under hypoxia. Sumoylation is enhanced through interaction with RWDD3. Both sumoylation and desumoylation seem to be involved in the regulation of its stability during hypoxia. Sumoylation can promote either its stabilization or its VHL-dependent degradation by promoting hydroxyproline-independent HIF1A-VHL complex binding, thus leading to HIF1A ubiquitination and proteasomal degradation. Desumoylation by SENP1 increases its stability amd transcriptional activity. There is a disaccord between various publications on the effect of sumoylation and desumoylation on its stability and transcriptional activity.Acetylation of Lys-532 by ARD1 increases interaction with VHL and stimulates subsequent proteasomal degradation (PubMed:12464182). Deacetylation of Lys-709 by SIRT2 increases its interaction with and hydroxylation by EGLN1 thereby inactivating HIF1A activity by inducing its proteasomal degradation (PubMed:24681946).Polyubiquitinated; in normoxia, following hydroxylation and interaction with VHL. Lys-532 appears to be the principal site of ubiquitination. Clioquinol, the Cu/Zn-chelator, inhibits ubiquitination through preventing hydroxylation at Asn-803. Ubiquitinated by a CUL2-based E3 ligase.In normoxia, is hydroxylated on Pro-402 and Pro-564 in the oxygen-dependent degradation domain (ODD) by EGLN1/PHD2 and EGLN2/PHD1 (PubMed:11292861, PubMed:11566883, PubMed:12351678, PubMed:15776016, PubMed:25974097). EGLN3/PHD3 has also been shown to hydroxylate Pro-564 (PubMed:11292861, PubMed:11566883, PubMed:12351678, PubMed:15776016, PubMed:25974097). The hydroxylated prolines promote interaction with VHL, initiating rapid ubiquitination and subsequent proteasomal degradation (PubMed:11292861, PubMed:11566883, PubMed:12351678, PubMed:15776016, PubMed:25974097). Deubiquitinated by USP20 (PubMed:11292861, PubMed:11566883, PubMed:12351678, PubMed:15776016, PubMed:25974097). Under hypoxia, proline hydroxylation is impaired and ubiquitination is attenuated, resulting in stabilization (PubMed:11292861, PubMed:11566883, PubMed:12351678, PubMed:15776016, PubMed:25974097). In normoxia, is hydroxylated on Asn-803 by HIF1AN, thus abrogating interaction with CREBBP and EP300 and preventing transcriptional activation (PubMed:12080085). This hydroxylation is inhibited by the Cu/Zn-chelator, Clioquinol (PubMed:12080085). Repressed by iron ion, via Fe2+ prolyl hydroxylase (PHD) enzymes-mediated hydroxylation and subsequent proteasomal degradation (PubMed:28296633).The iron and 2-oxoglutarate dependent 3-hydroxylation of asparagine is (S) stereospecific within HIF CTAD domains.

Subcellular Location:

Nucleus;

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte

Subunit Structure:

Interacts with the HIF1A beta/ARNT subunit; heterodimerization is required for DNA binding. Interacts with COPS5; the interaction increases the transcriptional activity of HIF1A through increased stability (By similarity). Interacts with EP300 (via TAZ-type 1 domains); the interaction is stimulated in response to hypoxia and inhibited by CITED2. Interacts with CREBBP (via TAZ-type 1 domains). Interacts with NCOA1, NCOA2, APEX and HSP90. Interacts (hydroxylated within the ODD domain) with VHLL (via beta domain); the interaction, leads to polyubiquitination and subsequent HIF1A proteasomal degradation. During hypoxia, sumoylated HIF1A also binds VHL; the interaction promotes the ubiquitination of HIF1A. Interacts with SENP1; the interaction desumoylates HIF1A resulting in stabilization and activation of transcription. Interacts (Via the ODD domain) with ARD1A; the interaction appears not to acetylate HIF1A nor have any affect on protein stability, during hypoxia. Interacts with RWDD3; the interaction enhances HIF1A sumoylation. Interacts with TSGA10 (By similarity). Interacts with HIF3A (By similarity). Interacts with RORA (via the DNA binding domain); the interaction enhances HIF1A transcription under hypoxia through increasing protein stability. Interaction with PSMA7 inhibits the transactivation activity of HIF1A under both normoxic and hypoxia-mimicking conditions. Interacts with USP20. Interacts with RACK1; promotes HIF1A ubiquitination and proteasome-mediated degradation. Interacts (via N-terminus) with USP19. Interacts with SIRT2. Interacts (deacetylated form) with EGLN1. Interacts with CBFA2T3. Interacts with HSP90AA1 and HSP90AB1 (PubMed:26517842).

Similarity:

Contains two independent C-terminal transactivation domains, NTAD and CTAD, which function synergistically. Their transcriptional activity is repressed by an intervening inhibitory domain (ID).

Research Fields

Research Fields:

· Cellular Processes > Transport and catabolism > Autophagy - animal.(View pathway)
· Environmental Information Processing > Signal transduction > HIF-1 signaling pathway.(View pathway)
· Human Diseases > Cancers: Specific types > Renal cell carcinoma.(View pathway)
· Human Diseases > Cancers: Overview > Pathways in cancer.(View pathway)
· Human Diseases > Cancers: Overview > Proteoglycans in cancer.
· Human Diseases > Cancers: Overview > Central carbon metabolism in cancer.(View pathway)
· Human Diseases > Cancers: Overview > Choline metabolism in cancer.(View pathway)
· Organismal Systems > Endocrine system > Thyroid hormone signaling pathway.(View pathway)
· Organismal Systems > Immune system > Th17 cell differentiation.(View pathway)

Western blot analysis of extracts from various sample,using hif1a antibody. lane1:mouse muscle, lane2:mouse brain, lane3:mouse muscle with blocking peptide, lane4:mouse brain with blocking peptide,
Colon tissue HIF1A antibody used at 1/200 on formalin-fixed paraffin embedded rat colon tissue.
AF1009 staining HeLa cells by IF/ICC. The sample were fixed with PFA and permeabilized in 0.1% Triton X-100,then blocked in 10% serum for 45 minutes at 25°C. The primary antibody was diluted at 1/200 and incubated with the sample for 1 hour at 37°C. An Alexa Fluor 594 conjugated goat anti-rabbit IgG (H+L) antibody(Red), diluted at 1/600, was used as secondary antibody.

Reference Citations:

1). Xiong Y et al. Hypoxia-inducible factor 1α-induced epithelial-mesenchymal transition of endometrial epithelial cells may contribute to the development of endometriosis. Hum Reprod 2016 Jun;31(6):1327-38 (PubMed: 27094478) [IF=5.506]

Application: WB    Species:human;    Sample:Not available

Figure 2 The expression of epithelial –mesenchymal transition (EMT) markers and b-catenin was detected at each time point. (A) Immunoblotting analysis of human primary cultured endometrial epithelial cell extracts using the corresponding antibodies. The ratios of each protein relative to non-treated cells were normalized to GAPDH. (B) The relative expression of HIF-1a, N-cadherin, E-cadherin, b-catenin, vimentin and snail proteins in human endometrial epithelial glands under hypoxic conditions at each time point was investigated by western blot. Data are represented as mean+SD and are representative of the relative expression of protein normalized by GAPDH. All experiments were repeated four times. Data were evaluated by one-way ANOVA analysis (*P , 0.05, **P , 0.01 compared with untreated group). (C) The changed cellular morphologies of human endometrial epithelial glands in hypoxia compared with cells in normoxia, the hypoxic time was 48 h. Red arrows indicate the spindle-shaped and fibroblast-like cells.

Application: IHC    Species:human;    Sample:Not available

Figure 1 EMT occurs in endometrial epithelial cells of ovarian endometriosis samples. Representative photomicrographs of HIF-1a (A–C), b-catenin (D–F), E-cadherin (G–I), N-cadherin (J–L) and vimentin (M–O) in normal endometrium (A, D, G, J, M), eutopic endometrium (B, E, H, K, N) and ovarian endometriosis (C, F, I, L,O). (P)Colon cancer tissue that was positive for HIF-1a. (Q) Healthy liver tissue that was negative for HIF-1a. (R) Peptide-blocking reagent without antibody was applied as the negative controls. Photographs were taken at magnifications of ×200 (left panels) and ×400 (right panels). N, normal endometrium; U, eutopic endometrium; E, ovarian endometriosis.


2). Zhang L et al. Estrogen stabilizes hypoxia-inducible factor 1α through G protein-coupled estrogen receptor 1 in eutopic endometrium of endometriosis. Fertil Steril 2017 Feb;107(2):439-447 (PubMed: 27939762) [IF=5.411]

Application: WB    Species:human;    Sample:Not available

17b-Estradiol and G1 regulate GPER and HIF-1a expression in ESCs. (A–D) Time course of GPER and HIF-1a mRNA levels in ESCs treated with 10 nM E2 or 100 nM G1 for 0, 5, 10, 15, 30, 60, and 120 minutes. (E, I) Time course of GPER and HIF-1a mRNA levels in ESCs treated with 10 nM E2 or 100 nM G1 for 0, 5, 10, 15, 30, 60, and 120 minutes. (F, G, J, K) Quantitative comparison of the fold difference in the expression of GPER and HIF- 1a proteins (*P<.05, ** P<.01, *** P<.001, R ¼ 0.7014) or G1 (P<.001, R ¼ 0.6386). (M–P) Time course of VEGF and MMP9 secretion after treatment with 10 nM E2 or 100 nM G1 for 0, 5, 10, 15, 30, 60, and 120 minutes.

Application: IHC    Species:human;    Sample:Not available

G protein-coupled estrogen receptor (GPER) and HIF-1a expression and localization in EuEM of endometriosis and CoEM. (A–D) Immunohistochemical analysis of GPER and HIF-1a protein expression and localization in CoEM. (E–H) Immunohistochemical analysis of GPER and HIF-1a protein in EuEM. Photographs were taken at original magnifications of 200 (left) and 400 (right), respectively. (I–L) Quantitative comparison of the fold difference in the expression of GPER and HIF-1a protein. The data are presented as means  SEM (*P<.05, ** P<.01, *** P


3). Wang X et al. Curcumin pretreatment protects against hypoxia/reoxgenation injury via improvement of mitochondrial function, destabilization of HIF-1α and activation of Epac1-Akt pathway in rat bone marrow mesenchymal stem cells. Biomed Pharmacother 2019 Jan;109:1268-1275 (PubMed: 30551377) [IF=3.743]

4). Sun Z et al. Long non-coding RNA and mRNA profile analysis of metformin to reverse the pulmonary hypertension vascular remodeling induced by monocrotaline. Biomed Pharmacother 2019 May 3;115:108933 (PubMed: 31060005) [IF=3.743]

5). Dong J et al. A novel HDAC6 inhibitor exerts an anti-cancer effect by triggering cell cycle arrest and apoptosis in gastric cancer. Eur J Pharmacol 2018 Jun 5;828:67-79 (PubMed: 29563065) [IF=3.170]

6). Liu H et al. Hypoxia-inducible factor-1α promotes endometrial stromal cells migration and invasion by upregulating autophagy in endometriosis. Reproduction 2017 Jun;153(6):809-820 (PubMed: 28348069) [IF=3.125]

Application: WB    Species:human;    Sample:Not available

FIGURE 4. Knockdown of HIF-1α interferes with hypoxia-induced autophagy in HESCs. (A) Representative western blots of HIF-1α, Beclin1 and LC3 protein in HESCs transfected with scrambled control siRNA or HIF- 1α specific siRNA in the presence or absence of hypoxia. (B) The protein expression levels were quantified by Image J software and normalized to GAPDH protein levels. The data are presented as the means ± SD from at least three independent experiments (*p<0.05;**p<0.01; ***p


7). Liu H et al. Autophagy contributes to hypoxia-induced epithelial to mesenchymal transition of endometrial epithelial cells in endometriosis. Biol Reprod 2018 May 31 (PubMed: 29860279)

8). An S et al. Administration of CoCl2 Improves Functional Recovery in a Rat Model of Sciatic Nerve Transection Injury. Int J Med Sci 2018 Sep 7;15(13):1423-1432 (PubMed: 30443161)

9). An S et al. Administration of CoCl2 Improves Functional Recovery in a Rat Model of Sciatic Nerve Transection Injury. Int J Med Sci 2018 Sep 7;15(13):1423-1432 (PubMed: 30443161)

10). Chen J et al. Aspirin inhibits hypoxia-mediated lung cancer cell stemness and exosome function. Pathol Res Pract 2019 Mar 11 (PubMed: 30878308)

11). Li J et al. HIF1A and VEGF regulate each other by competing endogenous RNA mechanism and involve in the pathogenesis of peritoneal fibrosis. Pathol Res Pract 2018 Dec 26 (PubMed: 30598338)

12). Liu H et al. Long non-coding RNA MALAT1 mediates hypoxia-induced pro-survival autophagy of endometrial stromal cells in endometriosis. J Cell Mol Med 2018 Oct 15 (PubMed: 30324652)

13). Liu X et al. MicroRNA-370 inhibits the growth and metastasis of lung cancer by down-regulating epidermal growth factor receptor expression. Oncotarget 2017 Oct 4;8(50):88139-88151 (PubMed: 29152147)

Application: WB    Species:human;    Sample:Not available

Figure 4: Induction of miR-370 over-expression reduces EGFR and HIF-1α expression and inhibits the ERK and AKT phosphorylation in XWLC-05 and H157 cells. XWLC-05 and H157 cells were transfected with miR-370 mimics, miR-370 inhibitor or corresponding controls for 24 h. The relative levels of EGFR, HIF-1α, ERK, AKT expression, ERK and AKT phosphorylation were determined by Western blot assays. Data are representative images or expressed as the means ± SEM of each group of cells from three separate experiments. *P<0.05, **P<0.01, ***P<0.001, ****P<0.0001.

Application: IHC    Species:human;    Sample:Not available

Figure 5: Induction of miR-370 over-expression inhibits the growth and angiogenesis of NSCLC xenograft tumors in vivo. (H) Histological and immunohistochemistry analysis.


14). Gong Q et al. Enhanced ROBO4 is mediated by up-regulation of HIF-1α/SP1 or reduction in miR-125b-5p/miR-146a-5p in diabetic retinopathy. J Cell Mol Med 2019 May 15 (PubMed: 31094072)

15). Chen C et al. A multifunctional-targeted nanoagent for dual-mode image-guided therapeutic effects on ovarian cancer cells. Int J Nanomedicine 2019 Jan 21;14:753-769 (PubMed: 30718954)

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Catalog Number :

AF1009-BP
(Blocking peptide available as AF1009-BP)

Price/Size :

$200/1mg.
Tips: For phospho antibody, we provide phospho peptide(0.5mg) and non-phospho peptide(0.5mg).

Function :

Blocking peptides are peptides that bind specifically to the target antibody and block antibody binding. These peptide usually contains the epitope recognized by the antibody. Antibodies bound to the blocking peptide no longer bind to the epitope on the target protein. This mechanism is useful when non-specific binding is an issue, for example, in Western blotting (immunoblot) and immunohistochemistry (IHC). By comparing the staining from the blocked antibody versus the antibody alone, one can see which staining is specific; Specific binding will be absent from the western blot or immunostaining performed with the neutralized antibody.

Format and storage :

Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 10 mg/ml.The purity is >90%,tested by HPLC and MS.Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.

Precautions :

This product is for research use only. Not for use in diagnostic or therapeutic procedures.

Pig
100%
Rabbit
100%
Bovine
100%
Horse
100%
Chicken
55%
Zebrafish
0%
Dog
0%
Sheep
0%
Xenopus
0%
High similarity Medium similarity Low similarity No similarity
Q16665 as Substrate
Site PTM Type Enzyme
K10 Acetylation
K10 Sumoylation
K11 Acetylation
K12 Acetylation
K19 Acetylation
K21 Acetylation
S31 Phosphorylation
K32 Ubiquitination
T63 Phosphorylation
Y66 Phosphorylation
K71 Ubiquitination
K85 Ubiquitination
S113 Phosphorylation
K172 Ubiquitination
K185 Sumoylation
K185 Ubiquitination
S247 Phosphorylation P48730 (CSNK1D)
K251 Ubiquitination
Y276 Phosphorylation
K289 Ubiquitination
K297 Ubiquitination
K377 Ubiquitination
K389 Acetylation
K389 Ubiquitination
K391 Methylation
K391 Sumoylation
K391 Ubiquitination
S451 Phosphorylation
T455 Phosphorylation
T458 Phosphorylation
K460 Ubiquitination
S465 Phosphorylation
K477 Sumoylation
K477 Ubiquitination
C520 S-Nitrosylation
K532 Acetylation
K532 Ubiquitination
K538 Ubiquitination
K547 Ubiquitination
S551 Phosphorylation
T555 Phosphorylation
Y565 Phosphorylation
S576 Phosphorylation Q9H4B4 (PLK3)
S589 Phosphorylation
K636 Ubiquitination
S641 Phosphorylation P28482 (MAPK1) , P27361 (MAPK3)
S643 Phosphorylation P28482 (MAPK1) , P27361 (MAPK3)
K649 Ubiquitination
T651 Phosphorylation
T652 Phosphorylation
S653 Phosphorylation
S656 Phosphorylation
S657 Phosphorylation Q9H4B4 (PLK3)
S668 Phosphorylation P06493 (CDK1)
K674 Acetylation
K674 Ubiquitination
K682 Ubiquitination
S683 Phosphorylation
S687 Phosphorylation
S692 Phosphorylation
S696 Phosphorylation Q13315 (ATM)
T700 Phosphorylation
K709 Acetylation
K709 Ubiquitination
K721 Ubiquitination
S727 Phosphorylation
S760 Phosphorylation
S761 Phosphorylation
K769 Ubiquitination
T796 Phosphorylation
S797 Phosphorylation Q5S007 (LRRK2)
C800 S-Nitrosylation
S809 Phosphorylation
IMPORTANT: For western blots, incubate membrane with diluted antibody in 5% w/v milk , 1X TBS, 0.1% Tween®20 at 4°C with gentle shaking, overnight.