400060
Anti-Glucose Transporter-1 Rabbit pAb
Sinónimos:
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
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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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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