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NSJ Bioreagents

SKU:V9719-100UG

PRMT7 Antibody, 100 ug

PRMT7 Antibody, 100 ug

Regular price $559.00 USD
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Arginine methylation is an irreversible protein modification catalyzed by Arginine methyltransferases, such as PRMT7, which uses S-adenosylmethionine (AdoMet) as the methyl donor. Arginine methylation is implicated in signal transduction, RNA transport and RNA splicing. PRMT7 has two methyltransferase domains, each containing a putative AdoMet-binding motif. The N-terminal methyltransferase domain closely resembles the catalytic core of PRMT5, and the C-terminal domain is most similar to that of PRMT1. Three PRMT7 splice variants have been identified by database analysis. PRMT7 is localized to the nucleus and cytoplasm and moderate expression is observed in adult brain and lung tissues.

Specifications

Catalog No V9719-100UG
Family Primary antibody
Qty 100 ug
Formulation 0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced), 0.05% sodium azide
Format Purified
Clone PCRP-PRMT7-1A7
Host Animal Mouse
Clonality Monoclonal (mouse origin)
Isotype Mouse IgG1
Species Reactivity Human
Application FACS, IF
Application Details Immunofluorescence: 1-2ug/ml,Flow cytometry: 1-2ug/million cells
Application Note Optimal dilution of the PRMT7 antibody should be determined by the researcher.
Localization Nucleus, Cytoplasm
Immunogen Recombinant full-length human PRMT7 protein was used as the immunogen for the PRMT7 antibody.
Purity Protein A/G affinity
Storage Aliquot the PRMT7 antibody and store frozen at -20oC or colder. Avoid repeated freeze-thaw cycles.
Limitation This PRMT7 antibody is available for research use only.
Uniprot # Q9NVM4
Status Available
PDF Link https://www.nsjbio.com/tds-pdf/prmt7-antibody-pcrp-prmt7-1a7-v9719
Title PRMT7 Antibody
Description Arginine methylation is an irreversible protein modification catalyzed by Arginine methyltransferases, such as PRMT7, which uses S-adenosylmethionine (AdoMet) as the methyl donor. Arginine methylation is implicated in signal transduction, RNA transport and RNA splicing. PRMT7 has two methyltransferase domains, each containing a putative AdoMet-binding motif. The N-terminal methyltransferase domain closely resembles the catalytic core of PRMT5, and the C-terminal domain is most similar to that of PRMT1. Three PRMT7 splice variants have been identified by database analysis. PRMT7 is localized to the nucleus and cytoplasm and moderate expression is observed in adult brain and lung tissues.
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