Cell Signaling Technology

Product Pathways - MAPK Signaling

Phospho-TAB2 (Ser372) (D5A4) Rabbit mAb #8155

No. Size Price
8155S 100 µl ( 10 western blots ) ¥4,050.00 现货查询 购买询价 防伪查询
8155 carrier free & custom formulation / quantityemail request
Applications Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W 1:1000 Human,Mouse,Rat,Monkey, Endogenous 80-84 Rabbit IgG
IP 1:100

Species cross-reactivity is determined by western blot.

Applications Key: W=Western Blotting, IP=Immunoprecipitation,

Specificity / Sensitivity

Phospho-TAB2 (Ser372) (D5A4) Rabbit mAb recognizes endogenous levels of TAB2 protein only when phosphorylated at Ser372.

Phospho-TAB2 (Ser372) (D5A4) Rabbit mAb兔单抗能够识别内源性Ser372位点磷酸化的TAB2蛋白水平。

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser372 of human TAB2 protein.


Western Blotting

Western Blotting

Western blot analysis of extracts from 293T cells, untreated or treated with Human Interleukin-1β (hIL-1β) #8900 (50 ng/ml) and Calyculin A (Serine/Threonine Phosphatase Inhibitor) #9902 (CalA) (100 nM, 20 min), using Phospho-TAB2 (Ser372) (D5A4) Rabbit mAb (upper) or total TAB2 (C88H10) Rabbit mAb #3745 (lower). Lysates were then treated with a combination of calf intestinal phosphatase (CIP) and λ-phosphatase to show phospho-specificity.western blot方法检测细胞提取物:用和未用人源Interleukin-1β (hIL-1β) #8900 (50 ng/ml) 、Calyculin A (Serine/Threonine Phosphatase Inhibitor) #9902 (CalA) (100 nM, 20 min)处理的293T细胞。使用的抗体是Phospho-TAB2 (Ser372) (D5A4) Rabbit mAb (上图) 和 total TAB2 (C88H10) Rabbit mAb #3745 (下图)。裂解物用牛小肠磷酸酶 (CIP)和λ-磷酸酶的混合物处理,以显示磷酸化特异性。


TAK1 is a mitogen-activated protein kinase kinase kinase activated by TGF-β and various pro-inflammatory signals (1,2). In vivo, TAK1 activation requires its association with TAK1 binding protein 1 (TAB1), which triggers TAK1 autophosphorylation at Thr184 and Thr187 (3,4). The TAB2 adaptor protein links TAK1 with TRAF6 to mediate TAK1 activation following IL-1 stimulation (5). Once activated, TAK1 phosphorylates the MAPK kinases MKK4 and MKK3/6, which activate JNK and p38 MAPK, respectively. TAK1 and TRAF6 also activate the NF-κB pathway by phosphorylating the NF-κB inducing kinase (NIK) to trigger subsequent activation of IKK (2,6). In addition to TAK1, TAB1 interacts with and activates p38α MAPK (7). Targeted disruption of the TAB1 gene in mice causes a drastic reduction in TAK1 activity and leads to embryonic lethality (8).

TAK1是MAPKKK家族中的成员,由TGF-β和许多促炎性反应信号分子激活(1,2)。在体内,TAK1的活化需要它与TAK1结合蛋白1 (TAB1)的结合,这种结合能够触发TAK1蛋白Thr184和Thr187位点的自磷酸化(3,4)。TAB2接头蛋白能够将TAK1与TRAF6连接起来,调节IL-1刺激引起的TAK1的活化(5)。一经激活,TAK1能够磷酸化MAPK激酶MKK4和MKK3/6,MKK4和MKK3/6再分别激活JNK和p38 MAPK。TAK1和TRAF6也能激活NF-κB通路,这是通过磷酸化NF-κB诱导激酶(NIK)从而激活后续的IKK实现的(2,6)。除了TAK1,TAB1还能与与p38α MAPK相互作用,并使其活化 (7)。对小鼠中TAB1基因的靶向断裂能够引起TAK1活性的急剧下降,导致胚胎期死亡(8)。

TAK1 is associated with TAB1 as well as either TAB2 or TAB3 (9). Activation of TAK1 is triggered by K63-ubiquitination of TRAF6, resulting in binding to TAB2 and TAB3 and autophosphorylation of TAK1 (10-12). Multiple phosphorylation sites have been identified in all three TAB family members that are triggered by IL-1 (13,14). TAB2 phosphorylation was identified at Ser372 and Ser524 (14).

TAK1能够与TAB1以及TAB2、TAB3相互作用(9)。TAK1能够被TRAF6的K63-泛素化所激活,使其能够与TAB2、TAB3相结合,引起TAK1的自磷酸化(10-12)。许多磷酸化位点被证明存在于IL-1刺激激活的所有3个TAB家族成员中。 (13,14)。TAB2的磷酸化位点是Ser372和Ser524位点(14)。

  1. Yamaguchi, K. et al. (1995) Science 270, 2008-11.
  2. Ninomiya-Tsuji, J. et al. (1999) Nature 398, 252-6.
  3. Shibuya, H. et al. (1996) Science 272, 1179-82.
  4. Sakurai, H. et al. (2000) FEBS Lett 474, 141-5.
  5. Takaesu, G. et al. (2000) Mol Cell 5, 649-58.
  6. Wang, C. et al. (2001) Nature 412, 346-51.
  7. Ge, B. et al. (2002) Science 295, 1291-4.
  8. Komatsu, Y. et al. (2002) Mech Dev 119, 239-49.
  9. Cheung, P.C. et al. (2004) Biochem J 378, 27-34.
  10. Kishida, S. et al. (2005) Genes Cells 10, 447-54.
  11. Sato, Y. et al. (2009) EMBO J 28, 3903-9.
  12. Kanayama, A. et al. (2004) Mol Cell 15, 535-48.
  13. Cheung, P.C. et al. (2003) EMBO J 22, 5793-805.
  14. Mendoza, H. et al. (2008) Biochem J 409, 711-22.

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