Description

Background:

SRF is a transcription factor that binds to the serum response element (SRE), a short sequence of dyad symmetry located 300 bp to the 5′ of the site of transcription initiation of some genes (such as FOS). Required for cardiac differentiation and maturation.

Product datasheet:

Overview

Product Description  
Species ReactivitiesHuman,Mouse,Rat
ImmunogenSynthesized peptide derived from human SRF around the phosphorylation site of S103.

Properties

FormLiquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Storage Instructions-20°C/1 year
ClonalityPolyclonal

References:

  1. Isolation and properties of cDNA clones encoding SRF, a transcription factor that binds to the c-fos serum response element.
    Norman C., Runswick M., Pollock R., Treisman R.
    Cell 55:989-1003(1988) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
  2. The DNA sequence and analysis of human chromosome 6.
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC]

    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

  3. Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R.
    , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases

    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

  4. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung and Lymph.
  5. C-terminal phosphorylation of the serum-response factor.
    Janknecht R., Ernst W.H., Houthaeve T., Nordheim A.
    Eur. J. Biochem. 216:469-475(1993) [PubMed] [Europe PMC] Cited for: PROTEIN SEQUENCE OF 210-221 AND 253-264, PHOSPHORYLATION AT SER-253.
  6. Identification of multiple SRF N-terminal phosphorylation sites affecting DNA binding properties.
    Janknecht R., Hipskind R.A., Houthaeve T., Nordheim A., Stunnenberg H.G.
    EMBO J. 11:1045-1054(1992) [PubMed] [Europe PMC] Cited for: PHOSPHORYLATION AT SER-77; SER-79; SER-83; SER-85 AND SER-103.
  7. Localization of O-GlcNAc modification on the serum response transcription factor.
    Reason A.J., Morris H.R., Panico M., Marais R., Treisman R.H., Haltiwanger R.S., Hart G.W., Kelly W.G., Dell A.
    J. Biol. Chem. 267:16911-16921(1992) [PubMed] [Europe PMC] Cited for: GLYCOSYLATION AT SER-277; SER-307; SER-309; SER-316 AND SER-383.
  8. The carboxyl-terminal transactivation domain of human serum response factor contains DNA-activated protein kinase phosphorylation sites.
    Liu S.-H., Ma J.-T., Yueh A.Y., Lees-Miller S.P., Anderson C.W., Ng S.-Y.
    J. Biol. Chem. 268:21147-21154(1993) [PubMed] [Europe PMC] Cited for: PHOSPHORYLATION AT SER-435 AND SER-446.
  9. Phenotypic modulation of smooth muscle cells through interaction of Foxo4 and myocardin.
    Liu Z.-P., Wang Z., Yanagisawa H., Olson E.N.
    Dev. Cell 9:261-270(2005) [PubMed] [Europe PMC] Cited for: INTERACTION WITH MLLT7.
  10. Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
external
sizechest(in.)waist(in.)hips(in.)
XS34-3627-2934.5-36.5
S36-3829-3136.5-38.5
M38-4031-3338.5-40.5
L40-4233-3640.5-43.5
XL42-4536-4043.5-47.5
XXL45-4840-4447.5-51.5

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