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MOB1B/MOBKL1A Monoclonal Antibody - 1
  • MOB1B/MOBKL1A Monoclonal Antibody - 1
  • MOB1B/MOBKL1A Monoclonal Antibody - 2
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100μL $ 320.00
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For research use only.

Verified Samples Verified Samples in IF: Hela
Dilution ICC/IF 1:20-1:100
Isotype IgG2a
Host Mouse
Reactivity Human
Applications ICC/IF
Clonality Monoclonal
Immunogen Recombinant Human MOB1B/MOBKL1A Protein
Abbre MOB1B
Synonyms MOB4A,  MOBKL1A,  MOB1B
Swissprot
Tissue Specificity Adrenal gland, bone marrow, brain, lung, placenta, prostate, salivary gland, skeletal muscle, testis, thymus, thyroid gland, uterus, colon with mucosa, fetal brain and fetal liver.
Concentration 1 mg/mL
Buffer 0.2 μm filtered solution in PBS
Purification Method Protein A
Research Areas Signal Transduction
Clone No. 2D8
Conjugation Unconjugated
Storage This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free. Avoid repeated freeze-thaw cycles.
Shipping Ice bag
background MST1 and MST2 are the mammalian Ste2-related protein kinases most closely related to Drosophila Hippo, a major regulator of cell proliferation and survival during development. Overexpression of MST1 or MST2 in mammalian cells is proapoptotic. MST1 and MST2 activity increase during mitosis, especially in nocodazole-arrested mitotic cells, where these kinases exhibit an increase in both abundance and activation. MST1 and MST2 also can be activated nonphysiologically by okadaic acid or H2O2. The MOB1B and MOBKL1B polypeptides, homologs of the Drosophila MATS polypeptide, are identified as preferred MST1/MST2 substrates in vitro and are phosphorylated in cells in an MST1/MST2-dependent manner in mitosis and response to okadaic acid or H2O2. MST1/MST2-catalyzed MOB1B/MOBKL1B phosphorylation alters the ability of MOB1B/MOBKL1B to bind and regulate downstream targets such as the NDR-family protein kinases. Thus, MOB1B/MOBKL1B phosphorylation in cells promotes MOB1B/MOBKL1B binding to the LATS1 kinase and enables H2O2-stimulated LATS1 activation loop phosphorylation. Most importantly, the replacement of endogenous MOB1B/MOBKL1B by a non-phosphorylatable mutant is sufficient to accelerate cell proliferation substantially by speeding progression through G1/S as well as mitotic exit.
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Unconjugated

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