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Merck
CN

G4915

Anti-Gαi1,2 antibody produced in rabbit

whole antiserum

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UNSPSC Code:
12352203
NACRES:
NA.41
MDL number:
Conjugate:
unconjugated
Clone:
polyclonal
Application:
WB
Citations:
10
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biological source

rabbit

conjugate

unconjugated

antibody form

whole antiserum

antibody product type

primary antibodies

clone

polyclonal

mol wt

antigen 40 kDa

contains

≤0.1% sodium azide

species reactivity

mammals

technique(s)

western blot: 1:100-1:200 using cell membranes

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Quality Level

Gene Information

human ... GNAI2(2771)
mouse ... Gnai2(14678)
rat ... Gnai2(81664)

General description

G-proteins are membrane associated heterotrimeric proteins that are comprised of α-, β-, and γ-subunits. These proteins play a key role in signal transduction pathways that regulate cell′s response to several hormones, neuromodulators and ligands. All α subunits appear to be palmitoylated near the N-terminus. Palmitate regulates GTPase activity by GTPase activating proteins.

Immunogen

Synthetic peptide corresponding to the C-terminal region of Gα i1,2.

Application

Anti-Gαi1,2 antibody produced in rabbit is suitable for use as a primary antibody at a working dilution of 1:1000 in immunocytochemical staining of oocytes of the starfish Asterias amurensis after induction of maturation.

Biochem/physiol Actions

The gene GNAI2 (guanine nucleotide binding protein (G protein), α inhibiting activity polypeptide 2) encodes an α subunit of guanine nucleotide binding proteins. The α-subunit contains a guanine-binding domain that is in its inactive state when it is occupied by GDP. Upon activation, GDP is replaced with GTP, causing the dissociation of the α-subunit from the βγ-subunit complex. This enables the Gα-GTP complex to bind to and regulate specific signaling pathways. GTP is then hydrolyzed, allowing for re-association of the α-subunit with the βγ-subunit complex. This subunit has the binding site for guanine nucleotide and regulates adenylate cyclase. G αi-2 is localized to the basolateral plasma membrane.Carboxy-terminal end plays a key role in the specificity of membrane targeting in Gα i proteins. When coupled to phospholipase C, the α subunits may have a role in pertussis toxin-insensitive pathways.

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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存储类别

10 - Combustible liquids

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分析证书(COA)

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J B de Almeida et al.
Journal of cell science, 107 ( Pt 3), 507-515 (1994-03-01)
Heterotrimeric guanine nucleotide-regulatory (G) proteins are associated with a variety of intracellular membranes and specific plasma membrane domains. In polarized epithelial LLC-PK1 cells we have shown previously that endogenous G alpha i-2 is localized on the basolateral plasma membrane, whereas
Jessica E Smotrys et al.
Annual review of biochemistry, 73, 559-587 (2004-06-11)
Protein S-palmitoylation is the thioester linkage of long-chain fatty acids to cysteine residues in proteins. Addition of palmitate to proteins facilitates their membrane interactions and trafficking, and it modulates protein-protein interactions and enzyme activity. The reversibility of palmitoylation makes it
N E Lamash et al.
Ontogenez, 37(4), 273-278 (2006-10-07)
We studied the actin cytoskeleton state in Asterias amurensis oocytes within 30 min after the 1-methyladenine-induced maturation until the germinal vesicle breakdown. The total amount of actin remained unchanged during oocyte maturation. In immature oocytes, the major part of actin
The many faces of G protein signaling.
H E Hamm
The Journal of biological chemistry, 273(2), 669-672 (1998-02-14)
M E Linder et al.
Proceedings of the National Academy of Sciences of the United States of America, 90(8), 3675-3679 (1993-04-15)
A small number of membrane-associated proteins are reversibly and covalently modified with palmitic acid. Palmitoylation of G-protein alpha and beta subunits was assessed by metabolic labeling of subunits expressed in simian COS cells or insect Sf9 cells. The fatty acid

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