400060
Anti-Glucose Transporter-1 Rabbit pAb
Synonym(s):
Anti-Glut-1
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About This Item
antibody form
affinity isolated antibody
Quality Level
clone
polyclonal
form
liquid
species reactivity
mouse, human, rabbit, rat
isotype
IgG
General description
Glucose transporter-1 (Glut-1) is a transmembrane protein that facilitates transport of glucose in the cell in an energy-independent fashion. Glut-1 is expressed in many tissues and is the only isoform of the glucose transporter family expressed in mammary gland.
Immunoaffinity purified rabbit polyclonal antibody. Recognizes the ~42-45 kDa Glut-1 protein.
Recognizes the ~42-45 kDa GLUT-1 protein. Also recognizes the HepG2-type transporter.
Immunogen
a synthetic peptide corresponding to amino acids near the C-terminus of mouse GLUT-1, conjugated to KLH
Application
ELISA (0.5-1 μg/ml)
Immunoblotting (1-10 μg/ml)
Immunofluorescence (see comments)
Frozen Sections (2-10 μg/ml)
Immunoprecipitation (see comments)
Immunoblotting (1-10 μg/ml)
Immunofluorescence (see comments)
Frozen Sections (2-10 μg/ml)
Immunoprecipitation (see comments)
Physical form
In PBS, 0.1% BSA, pH 7.4.
Reconstitution
Following initial thaw, aliquot and freeze (-20°C).
Analysis Note
Positive Control
Rat brain
Rat brain
Other Notes
The antigen used is 100% homologous to mouse, rabbit, human, bovine, pig, and chicken Glut-1. Also recognizes the Hep G2-type transporter. This antibody is also reported to work for immunofluorescence and immunoprecipitation. Variables associated with ass
Storage Class
10-13 - German Storage Class 10 to 13
Certificates of Analysis (COA)
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M Mueckler
European journal of biochemistry, 219(3), 713-725 (1994-02-01)
Facilitative glucose transport is mediated by members of the Glut protein family that belong to a much larger superfamily of 12 transmembrane segment transporters. Six members of the Glut family have been described thus far. These proteins are expressed in
H C Haspel et al.
The Journal of biological chemistry, 263(1), 398-403 (1988-01-05)
Peptides corresponding to amino acid residues 1-12 of the amino terminal and 480-492 of the carboxyl terminal of the deduced sequence of the glucose transporter were synthesized and used to produce site-specific polyclonal antipeptide sera. In a solid-phase radioimmunoassay, antiserum
D S Harris et al.
Proceedings of the National Academy of Sciences of the United States of America, 89(16), 7556-7560 (1992-08-15)
We have examined the expression and cellular location of facilitated glucose transporter proteins (GLUT1, -3, and -5) in a human colonic epithelial cell line (Caco-2) by using peptide-specific antibodies. A differential cellular distribution of these transporters was observed in differentiated
M J Birnbaum et al.
Proceedings of the National Academy of Sciences of the United States of America, 83(16), 5784-5788 (1986-08-01)
Antibody raised against the human erythrocyte glucose transporter identified a recombinant lambda gt11 bacteriophage in a cDNA library prepared from immunoselected polysomal RNA from adult rat brain. The cDNA predicts a 492-amino acid protein that demonstrates 97.6% identity to the
Karen Gertz et al.
BMC neurology, 16(1), 144-144 (2016-08-20)
VE-cadherin is the chief constituent of endothelial adherens junctions. However, the role of VE-cadherin in the pathogenesis of cerebrovascular diseases including brain ischemia has not yet been investigated. VE-cadherin heterozygous (VEC(+/-)) mice and wildtype controls were subjected to transient brain
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