371723
Anti-Giα-1 and Giα-2-Subunits, C-Terminal (345-354 and 346-355) Rabbit pAb
liquid, Calbiochem®
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关于此项目
UNSPSC Code:
12352203
Clone:
polyclonal
Species reactivity:
-
Application:
—
Citations:
11
biological source
rabbit
antibody form
purified antibody
antibody product type
primary antibodies
clone
polyclonal
form
liquid
does not contain
preservative
species reactivity (predicted by homology)
mammals
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze, avoid repeated freeze/thaw cycles
isotype
IgG
shipped in
wet ice
storage temp.
−70°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... GNAI1(2770)
General description
Anti-Giα-1 and Giα-2-Subunits, C-Terminal (345-354 and 346-355), rabbit polyclonal, recognizes Giα-1 and Giα-2 subunits. It is validated for use in Western blotting.
Protein A purified rabbit polyclonal antibody. Recognizes Giα-1 and Giα-2 subunit proteins.
Recognizes Giα-1 and Giα-2 subunits. Does not cross-react with G3α-3 or Goα subunits.
Immunogen
a synthetic peptide [(C)KNNLKDCGLF] corresponding to amino acids at the C-terminus of mammalian Giα-1 and Giα-2, conjugated to KLH
Application
Immunoblotting (1:1000)
Physical form
In 140 mM NaCl, 100 mM potassium phosphate, pH 7.5.
Preparation Note
Following initial thaw, aliquot and freeze (-70°C).
Other Notes
Does not cross-react with Giα-3 and Goα. The specificity and cross-reactivity were confirmed with lysates from separate cultures of bacteria transfected with the genes for Giα-1, Giα-2, Giα-3, and Goα. Variables associated with assay conditions will dictate the proper working dilution.
Mumby, S.M., and Gilman, A.G. 1991. Methods Enzymol.195, 215.
Goldsmith, P.P., et al. 1987. J. Biol. Chem.262, 14683.
Goldsmith, P.P., et al. 1987. J. Biol. Chem.262, 14683.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Toxicity: Standard Handling (A)
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存储类别
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
C Puma et al.
Journal of neurochemistry, 78(5), 960-971 (2001-09-13)
The chemokine IL-8 is known to be synthesized by glial cells in the brain. It has traditionally been shown to have an important role in neuroinflammation but recent evidence indicates that it may also be involved in rapid signaling in
K Takano et al.
Endocrinology, 138(6), 2405-2409 (1997-06-01)
SRIF activates an inwardly rectifying K+ current in human GH-secreting adenoma cells. Activation of this K+ current induces hyperpolarization of the membrane and abolishment of action potential firing. This mechanism is an essential mechanism for SRIF-induced decrease in intracellular Ca2+
Y Xu et al.
Infection and immunity, 64(2), 593-599 (1996-02-01)
In previous studies, an in vitro ADP-ribosylation assay was developed to quantitatively evaluate the in vivo ADP-ribosylation of eukaryotic target proteins in intact Chinese hamster ovary (CHO) cells by pertussis toxin (PT). Immunoblot analysis identified the two PT-sensitive target proteins
Jennifer S Ignatious Raja et al.
The European journal of neuroscience, 39(8), 1245-1255 (2014-01-22)
Intracellular signaling in insect olfactory receptor neurons remains unclear, with both metabotropic and ionotropic components being discussed. Here, we investigated the role of heterotrimeric Go and Gi proteins using a combined behavioral, in vivo and in vitro approach. Specifically, we
Suzy D Carvalho-Bianco et al.
Molecular endocrinology (Baltimore, Md.), 18(7), 1840-1849 (2004-05-08)
Whereas many cardiac symptoms of thyrotoxicosis resemble those of the hyperadrenergic state, circulating catecholamines are reduced or normal in this condition. To test the hypothesis that the thyrotoxic heart is hypersensitive to catechol-amines, we studied beta-adrenergic signaling in a transgenic
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