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Rabbit anti-TRM6 Antibody

Bethyl Laboratories®

Bethyl Laboratories® Catalog #

Validated
Target:
TRM6
Reactivity:
Human
Host:
Rabbit
Clonality:
Polyclonal
Format:
Whole IgG
Immunogen:
between 447 and 497
IsoType:
IgG
Purity:
Antigen Affinity Purified
100 µl (1000 µg/ml)

100 µl (10 blots)

20 µl (2 blots)

For ordering information, see our International Distributors

Product Details

Specifications
Verified Reactivity
Human
Presumed Reactivity
Bovine
Antigen Species
Human
Stock Concentration
100 µg/ml
1000 µg/ml
Storage
2 - 8 °C
Shelf Life
1 year from date of receipt
Physical State
Liquid
Buffer
Tris-buffered Saline containing 0.1% BSA and 0.09% Sodium Azide
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Tris-citrate/phosphate buffer, pH 7 to 8 containing 0.09% Sodium Azide
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Prod Procedures
Antibody was affinity purified using an epitope specific to TRM6 immobilized on solid support.

The epitope recognized by A303-008A-T maps to a region between residue 447 and 497 of human tRNA Methyltransferase 6 using the numbering given in entry NP_057023.2 (GeneID 51605).

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Gene & Protein Information

tRNA (adenine-N(1)-)-methyltransferase non-catalytic subunit TRM6 is a substrate-binding subunit of tRNA (adenine-N(1)-)-methyltransferase, which catalyzes the formation of N(1)-methyladenine at position 58 (m1A58) in initiator methionyl-tRNA [taken from the Universal Protein Resource (UniProt) www.uniprot.org/uniprot/ Q9UJA5].

51605

TRMT6

tRNA methyltransferase 6

Q9UJA5

tRNA (adenine(58)-N(1))-methyltransferase non-cata

Alternate Names

CGI-09, GCD10, Gcd10p, mRNA methyladenosine-N(1)-methyltransferase non-catalytic subunit TRM6, tRNA (adenine(58)-N(1))-methyltransferase non-catalytic subunit TRM6, tRNA methyltransferase 6 homolog, tRNA(m1A58)-methyltransferase subunit TRM6, tRNA(m1A58)MTase subunit TRM6

Applications

Western blot of immunoprecipitates performed using Normal Pig Serum (Cat. No. S100-020), Goat anti-Rabbit Light Chain HRP Conjugate (Cat. No. A120-113P) and 4-20% SDS-PAGE. Western blot of lysates performed using standard western blot reagents and 4-20% SDS-PAGE.

Citations (4)