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MOCS3 Antibody (N-term)

Affinity Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - MOCS3 Antibody (N-term) AP19278a
    MOCS3 Antibody (N-term)(Cat. #AP19278a) western blot analysis in mouse heart tissue lysates (35ug/lane).This demonstrates the MOCS3 antibody detected the MOCS3 protein (arrow).
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
WB, E
Primary Accession O95396
Other Accession A2BDX3, NP_055299.1
Reactivity Human, Mouse
Host Rabbit
Clonality Polyclonal
Isotype Rabbit IgG
Calculated MW 49669 Da
Antigen Region 40-66 aa
Additional Information
Gene ID 27304
Other Names Adenylyltransferase and sulfurtransferase MOCS3 {ECO:0000255|HAMAP-Rule:MF_03049}, Molybdenum cofactor synthesis protein 3 {ECO:0000255|HAMAP-Rule:MF_03049}, Molybdopterin synthase sulfurylase, MPT synthase sulfurylase, Molybdopterin-synthase adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_03049}, 27780 {ECO:0000255|HAMAP-Rule:MF_03049}, Adenylyltransferase MOCS3 {ECO:0000255|HAMAP-Rule:MF_03049}, Sulfur carrier protein MOCS2A adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_03049}, Molybdopterin-synthase sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_03049}, 28111 {ECO:0000255|HAMAP-Rule:MF_03049}, Sulfur carrier protein MOCS2A sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_03049}, Sulfurtransferase MOCS3 {ECO:0000255|HAMAP-Rule:MF_03049}, MOCS3 {ECO:0000255|HAMAP-Rule:MF_03049}
Target/Specificity This MOCS3 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 40-66 amino acids from the N-terminal region of human MOCS3.
Dilution WB~~1:1000
E~~Use at an assay dependent concentration.
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsMOCS3 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name MOCS3 {ECO:0000255|HAMAP-Rule:MF_03049}
Function Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln) (PubMed:19017811, PubMed:22453920, PubMed:30817134). Also essential during biosynthesis of the molybdenum cofactor (PubMed:15073332, PubMed:22453920, PubMed:30817134). Acts by mediating the C-terminal thiocarboxylation of sulfur carriers URM1 and MOCS2A (PubMed:15073332, PubMed:19017811, PubMed:22453920). Its N-terminus first activates URM1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus (PubMed:19017811, PubMed:22453920). The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as a nucleophile towards URM1 and MOCS2A (PubMed:15073332, PubMed:22453920). Subsequently, a transient disulfide bond is formed (PubMed:15073332, PubMed:22453920). Does not use thiosulfate as sulfur donor; NFS1 acting as a sulfur donor for thiocarboxylation reactions (PubMed:18650437, PubMed:22453920).
Cellular Location Cytoplasm, cytosol
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

Molybdenum cofactor (MoCo) is necessary for the function of all molybdoenzymes. One of the enzymes required for the biosynthesis of MoCo is molybdopterin synthase (MPT synthase). The protein encoded by this gene adenylates and activates MPT synthase. This gene contains no introns. A pseudogene of this gene is present on chromosome 14.

REFERENCES

Schlieker, C.D., et al. Proc. Natl. Acad. Sci. U.S.A. 105(47):18255-18260(2008)
Marelja, Z., et al. J. Biol. Chem. 283(37):25178-25185(2008)
Schmitz, J., et al. Biochemistry 47(24):6479-6489(2008)
Krepinsky, K., et al. FEBS J. 274(11):2778-2787(2007)
Matthies, A., et al. Biochemistry 44(21):7912-7920(2005)

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