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Key Documents

SAB4502804

Sigma-Aldrich

Anti-GLUT3, C-Terminal antibody produced in rabbit

affinity isolated antibody

Synonyma:

GLUT-3, GLUT3, Glucose transporter type 3 brain, SLC2A3, Solute carrier family 2 facilitated glucose transporter member 3

Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen


About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 53 kDa

species reactivity

human

concentration

~1 mg/mL

technique(s)

ELISA: 1:1000
immunohistochemistry: 1:50-1:100
western blot: 1:500-1:1000

NCBI accession no.

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SLC2A3(6515)

General description

Anti-GLUT3 Antibody detects endogenous levels of total GLUT3 protein.

Solute carrier family 2 member 3 (SLC2A3), also known as glucose transporter -3 (GLUT-3), is encoded by the gene mapped to human chromosome 12p13.3. The encoded protein belongs to the SLC2 family of GLUTs.

Immunogen

The antiserum was produced against synthesized peptide derived from human GLUT3.

Immunogen Range: 447-496

Application

Anti-GLUT3, C-Terminal antibody produced in rabbit has been used in immunocytochemistry.

Biochem/physiol Actions

Solute carrier family 2 member 3 (SLC2A3)/ glucose transporter -3 (GLUT-3) along with GLUT1, facilitates the transport of dehydroascorbic acid (DHA). It also plays a vital role in cerebral glucose metabolism, providing energy for the activity of neurons, which, in turn, moderates the excitatory-inhibitory balance impacting both brain development and activity-dependent neural plasticity. SLC2A3 is essential for or optimal preimplantation embryo development and survival. Mutation in the gene increases the risk of susceptibility to attention-deficit/hyperactivity disorder (ADHD).

Features and Benefits

Evaluate our antibodies with complete peace of mind. If the antibody does not perform in your application, we will issue a full credit or replacement antibody. Learn more.

Physical form

Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class

10 - Combustible liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


Osvědčení o analýze (COA)

Vyhledejte osvědčení Osvědčení o analýze (COA) zadáním čísla šarže/dávky těchto produktů. Čísla šarže a dávky lze nalézt na štítku produktu za slovy „Lot“ nebo „Batch“.

Již tento produkt vlastníte?

Dokumenty související s produkty, které jste v minulosti zakoupili, byly za účelem usnadnění shromážděny ve vaší Knihovně dokumentů.

Navštívit knihovnu dokumentů

slc2a3 single?nucleotide polymorphism and duplication influence cognitive processing and population?specific risk for attention?deficit/hyperactivity disorder.
Merker S, et al.
Journal of Child Psychology and Psychiatry, and Allied Disciplines, 58(7), 798-809 (2017)
Glucose transporter isoforms GLUT1 and GLUT3 transport dehydroascorbic acid.
Rumsey S C, et al.
The Journal of Biological Chemistry, 272(30), 18982-18989 (1997)
Energy requirements of odor transduction in the chemosensory cilia of olfactory sensory neurons rely on oxidative phosphorylation and glycolytic processing of extracellular glucose.
Villar P S, et al.
The Journal of Neuroscience, 37(23), 5736-5743 (2017)
The facilitative glucose transporter GLUT3: 20 years of distinction.
Simpson I A, et al.
American Journal of Physiology. Endocrinology and Metabolism, 295(2), E242-E253 (2008)
The human Hox-bearing chromosome regions did arise by block or chromosome (or even genome) duplications.
Larhammar D, et al.
Genome Research, 12(12), 1910-1920 (2002)

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