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chicken anti-myc tag polyclonal antibody 5762

$100.00$2,600.00

Antibody summary

  • Chicken polyclonal to myc tag
  • Suitable for: ELISA
  • Reacts with: tagged fusion proteins
  • Isotype: IgY
  • 100 µg, 25 µg, 1 mg
SKU: 5762parent Categories: , Tags: , ,
Weight1 lbs
Dimensions9 × 5 × 2 in
host

chicken

isotype

IgY

clonality

polyclonal

concentration

1 mg/mL

applications

ELISA

reactivity

tagged fusion proteins

available sizes

1 mg, 100 µg, 25 µg

chicken anti-myc tag polyclonal antibody 5762

antibody
Database link:
Sequence -Glu-Gln-Lys-Leu-Ile-Ser-Glu-Glu-Asp-Leu
Derived from c-myc 425-434 P01106
Tested applications
ELISA
Recommended dilutions
user optimized
Immunogen
Highly purified EQKLISEEDL (C-MYC) conjugated with KLH
Size and concentration
25, 100, 1000µg and 1 mg/mL
Form
liquid
Storage Instructions
highly purified EQKLISEEDL (C-MYC) conjugated with KLH
Storage buffer
PBS, pH 7.2, 0.09% NaN3
Purity
affinity purified
Clonality
polyclonal
Isotype
IgY
Compatible secondaries
goat anti-chicken IgY, H&L chain specific, peroxidase conjugated polyclonal antibody 1688
goat anti-chicken IgY, H&L chain specific, biotin conjugated polyclonal antibody 8036
goat anti-chicken IgY, H&L chain specific, FITC conjugated, Conjugated polyclonal antibody 4317
goat anti-chicken IgY, H&L chain specific, peroxidase conjugated polyclonal antibody, crossabsorbed 1708
goat anti-chicken IgY, H&L chain specific, biotin conjugated polyclonal antibody, crossabsorbed 1718
goat anti-chicken IgY, H&L chain specific, FITC conjugated polyclonal antibody, crossabsorbed 1723
Isotype control
Chicken polyclonal - Isotype Control
target relevance
Myc tag is a small protein tag that minimally impacts protein structure. This antibody can be used to confirm expression and quantify Myc tag recombinant proteins in Western blotting and for their purification/copurification. When imaging in situ, Myc tag proteins can be identified by this antibody when used in conjunction with a suitable secondary antibody.

Click for more on: epitope tags and myc tag
Protein names
Myc proto-oncogene protein (Class E basic helix-loop-helix protein 39) (bHLHe39) (Proto-oncogene c-Myc) (Transcription factor p64)
Gene names
MYC,MYC BHLHE39
Mass
50565Da
Function
FUNCTION: Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3' (PubMed:24940000, PubMed:25956029). Activates the transcription of growth-related genes (PubMed:24940000, PubMed:25956029). Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis (PubMed:24940000, PubMed:25956029). Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells (By similarity). Functions with TAF6L to activate target gene expression through RNA polymerase II pause release (By similarity). Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (PubMed:20010808). {ECO:0000250|UniProtKB:P01108, ECO:0000269|PubMed:20010808, ECO:0000269|PubMed:24940000, ECO:0000269|PubMed:25956029}.
Subellular location
SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:17558397}. Nucleus, nucleolus {ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:25775507}.
Structure
SUBUNIT: Efficient DNA binding requires dimerization with another bHLH protein. Binds DNA as a heterodimer with MAX (PubMed:9680483). Interacts with TAF1C and SPAG9. Interacts with PARP10. Interacts with KDM5A and KDM5B. Interacts (when phosphorylated at Thr-73 and Ser-77) with FBXW7(PubMed:25775507, PubMed:17558397). Interacts with PIM2. Interacts with RIOX1. The heterodimer MYC:MAX interacts with ABI1; the interaction may enhance MYC:MAX transcriptional activity. Interacts with TRIM6 (By similarity). Interacts with NPM1; the binary complex is recruited to the promoter of MYC target genes and enhances their transcription (PubMed:25956029). Interacts with CIP2A; leading to the stabilization of MYC (PubMed:17632056). {ECO:0000250|UniProtKB:P01108, ECO:0000269|PubMed:15103331, ECO:0000269|PubMed:15674325, ECO:0000269|PubMed:15723054, ECO:0000269|PubMed:17308053, ECO:0000269|PubMed:17311883, ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:17632056, ECO:0000269|PubMed:17873522, ECO:0000269|PubMed:25775507, ECO:0000269|PubMed:25956029, ECO:0000269|PubMed:9680483}.
Post-translational modification
PTM: Phosphorylated by PRKDC (PubMed:1597196). Phosphorylation at Ser-344 by PIM2 leads to the stabilization of MYC (By similarity). Phosphorylation at Ser-77 by CDK2 prevents Ras-induced senescence (PubMed:19966300, PubMed:20713526). Phosphorylated at Ser-77 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-73 (PubMed:22307329). Phosphorylation at Thr-73 and Ser-77 by GSK3 is required for ubiquitination and degradation by the proteasome (PubMed:15103331, PubMed:17558397, PubMed:8386367). Dephosphorylation at Ser-77 by protein phosphatase 2A (PPP2CA) promotes its degradation; interaction with PPP2CA is enhanced by AMBRA1 (PubMed:25803737, PubMed:25438055). {ECO:0000250|UniProtKB:P01108, ECO:0000269|PubMed:15103331, ECO:0000269|PubMed:1597196, ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:19966300, ECO:0000269|PubMed:20713526, ECO:0000269|PubMed:22307329, ECO:0000269|PubMed:25438055, ECO:0000269|PubMed:25803737, ECO:0000269|PubMed:8386367}.; PTM: Ubiquitinated by the SCF(FBXW7) complex when phosphorylated at Thr-73 and Ser-77, leading to its degradation by the proteasome (PubMed:15103331, PubMed:17558397, PubMed:25775507). In the nucleoplasm, ubiquitination is counteracted by USP28, which interacts with isoform 1 of FBXW7 (FBW7alpha), leading to its deubiquitination and preventing degradation (PubMed:17873522, PubMed:17558397). In the nucleolus, however, ubiquitination is not counteracted by USP28 but by USP36, due to the lack of interaction between isoform 3 of FBXW7 (FBW7gamma) and USP28, explaining the selective MYC degradation in the nucleolus (PubMed:17558397, PubMed:25775507). Also polyubiquitinated by the DCX(TRPC4AP) complex (PubMed:20551172, PubMed:29779948). Ubiquitinated by TRIM6 in a phosphorylation-independent manner (By similarity). {ECO:0000250|UniProtKB:P01108, ECO:0000269|PubMed:15103331, ECO:0000269|PubMed:17558397, ECO:0000269|PubMed:17873522, ECO:0000269|PubMed:20551172, ECO:0000269|PubMed:25775507, ECO:0000269|PubMed:29779948}.
Biotechnology
BIOTECHNOLOGY: POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 are the four Yamanaka factors. When combined, these factors are sufficient to reprogram differentiated cells to an embryonic-like state designated iPS (induced pluripotent stem) cells. iPS cells exhibit the morphology and growth properties of ES cells and express ES cell marker genes. {ECO:0000269|PubMed:18035408}.
Target Relevance information above includes information from UniProt accession : P01106
The UniProt Consortium

Data

ELISA-image-chicken-anti-myc tag-polyclonal-antibody-5762

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.

There are 3 publications in our database for this antibody or clone. Here are the latest 5, for more click below.


pmidtitleauthorscitation
27998981Src Acts as an Effector for Ku70-dependent Suppression of Apoptosis through Phosphorylation of Ku70 at Tyr-530Morii M, Kubota S, Honda T, Yuki R, Morinaga T, Kuga T, Tomonaga T, Yamaguchi N, Yamaguchi N.J Biol Chem. 2017 Feb 3;292(5):1648-1665. doi: 10.1074/jbc.M116.753202. Epub 2016 Dec 20.
26822090Disulfide Mispairing During Proinsulin Folding in the Endoplasmic ReticulumHaataja L, Manickam N, Soliman A, Tsai B, Liu M, Arvan P.Diabetes. 2016 Apr;65(4):1050-60. doi: 10.2337/db15-1345. Epub 2016 Jan 28.
21043486Ca2+ homeostasis modulation enhances the amenability of L444P glucosylcerebrosidase to proteostasis regulation in patient-derived fibroblastsWang F, Agnello G, Sotolongo N, Segatori L.ACS Chem Biol. 2011 Feb 18;6(2):158-68. doi: 10.1021/cb100321m. Epub 2010 Nov 10.

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