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Merck

GW10762

Sigma-Aldrich

Anti-SMS antibody produced in chicken

affinity isolated antibody, buffered aqueous solution

Sinónimos:

Anti-MRSR, Anti-Spermine synthase

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

chicken

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

rat, human, mouse

manufacturer/tradename

Genway 15-288-10762

technique(s)

western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SMS(6611)

Immunogen

Immunogen Sequence: GI # 4759152, sequence 206-335
Recombinant spermine synthase; SpS

Application

Anti-SMS antibody produced in chicken is suitable for western blotting at a working dilution of 1:500 and for cell staining at a working dilution of 1:200.

Biochem/physiol Actions

SMS (spermine synthase) encodes a member of the spermidine/spermin synthase family. It catalyzes the synthesis of spermine from spermidine and decarboxylated S-adenosylmethionine (dcSAM). Defects in this gene are linked to X-linked Snyder-Robinson mental retardation syndrome.

Physical form

Solution in phosphate buffered saline containing 0.02% sodium azide.

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Storage Class

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


Certificados de análisis (COA)

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Partial purification and characterization of spermine synthase from rat brain.
P Hannonen et al.
Biochimica et biophysica acta, 289(1), 225-231 (1972-11-10)
A Lauren Cason et al.
European journal of human genetics : EJHG, 11(12), 937-944 (2003-09-26)
Polyamines (putrescine, spermidine, spermine) are ubiquitous, simple molecules that interact with a variety of other molecules in the cell, including nucleic acids, phospholipids and proteins. Various studies indicate that polyamines are essential for normal cell growth and differentiation. Furthermore, these
Hong Wu et al.
The Journal of biological chemistry, 283(23), 16135-16146 (2008-03-28)
The crystal structures of two ternary complexes of human spermine synthase (EC 2.5.1.22), one with 5'-methylthioadenosine and spermidine and the other with 5'-methylthioadenosine and spermine, have been solved. They show that the enzyme is a dimer of two identical subunits.

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