G PROTEIN REAGENTS

ADP-RIBOSYLATION

ADP-RIBOSYLATION AGENTS

Heterotrimeric GTP-binding proteins (G proteins) play a key role in signal transduction by coupling cell surface receptors to effector systems^1,2. Bacterial toxins have proven to be extremely useful tools for identifying and studying the role of G proteins³. Both cholera toxin and pertussis toxin covalently modify the a subunits of numerous G proteins by ADP-ribosylating specific amino acid residues. Pertussis toxin uncouples the G protein from the receptor while cholera toxin reduces intrinsic GTPase activity leading to activation of the A subunit.

G-115
Cholera toxin (from Vibrio cholerae)
Lyophilized, MW=84.7 kDa [9012-63-9] Storage: 4°C
Cholera toxin consists of a single A subunit surrounded by five B subunits. The B subunits are responsible for the attachment of the native toxin to ganglioside GM1 on mammalian cell surfaces, and facilitates translocation of the A subunit. The A subunit catalyzes the ADP-ribosylation of an arginine residue on the a subunit of G proteins, reducing intrinsic GTPase activity and activating the a subunit3^3,4. ADP-ribosylation of other proteins such as human red cell Ca-ATPase has also been reported⁵. Cholera toxin must interact with ADP-ribosylation factor (ARF) for maximal activity⁶. When reconstituted to 1 ml with distilled water, each vial of cholera toxin contains 1.0 mg of protein in 0.05 M Tris, 0.2 M NaCl, 1 mM Na₂EDTA and 3 mM NaN₃ at pH 7.5. For detailed experimental procedures see reference 7.
1 mg
5 x 1 mg

G-117
Cholera toxin
Lyophilized solid, Storage: 4°C
Same as G-115 but azide free.
1 mg
5 x 1 mg

G-120
Cholera toxin A subunit (from Vibrio cholerae)
Lyophilized solid, MW=27.2 kDa, Storage: 4°C
The A subunit of cholera toxin possesses ADP-ribosyltransferase activity but is unable to penetrate cells in the absence of the B subunit. It is however, as effective as the native toxin in catalyzing ADP-ribosylation in broken cell preparations⁷. When reconstituted to 1 ml with distilled water, each vial of cholera toxin contains 250 µg of protein in 0.05 M Tris, 0.2 M NaCl, 1 mM Na₂EDTA and 3 mM NaN₃ at pH 7.5. For detailed experimental procedures see reference 7.
250 µg
5 x 250 µg

G-125
Cholera toxin B subunit (from Vibrio cholerae)
Lyophilized solid, MW=11.5 kDa, Storage: 4°C
The B subunit of cholera toxin attaches the native toxin to eukaryotic cell surfaces and facilitates the translocation of the A subunit. It does not possess any intrinsic ADP-ribosyltransferase activity¹⁷. The high affinity and specificity of the B subunit for ganglioside G_M1 makes it a novel tool for probing the involvement of G_M1 on growth and differentiation of neuronal and other cells⁸.
500 µg
5 x 500 µg

G-130
C3 Exoenzyme (from Clostridium botulinum)
98%, lyophilized, MW=25 kDa, Storage: -20°C
C3 Exoenzyme selectively ADP-ribosylates low molecular weight G proteins of the Rho subfamily at an asparagine residue within the putative effector domain⁹. It has been used as an effective tool to analyze the roles of Rho and related proteins in the activation of phospholipase D¹⁰ and other diverse processes such as lymphocyte-mediated cytotoxicity¹¹, cell motility¹² and thrombin-induced platelet aggregation¹³.
10 µg
50 µg

G-135
Diphtheria toxin, unnicked (from Corynebacterium diphtheriae)
Lyophilized, MW=63 kDa, Storage: 4°C
Elongation factor 2 (EF-2) catalyzes the GTP hydrolysis-dependent translocation reaction that is responsible for the movement of the ribosome along mRNA during protein synthesis¹⁴. Diphtheria toxin catalyzed ADP-ribosylation of EF-2 inhibits the translocation reaction which halts protein synthesis and ultimately results in cell death¹⁵. Diphtheria toxin is cell permeable and can translocate across endosomal membranes in response to low pH¹⁶.
1 mg
5 x 1 mg

G-100
Pertussis toxin (from Bordetella pertussis)
Islet-activating protein
Lyophilized MW=105 kDa [82248-93-9] Storage: 4°C
Pertussis toxin consists of an enzymatically active A protomer subunit (S-1) which possesses both NAD⁺ glycohydrolase and ADP-ribosyltransferase activities and a B oligomer subunit (S-2, S-3, 2 x S-4, and S-5) which is responsible for attachment of the native toxin to eukaryotic cell surfaces¹⁷. Pertussis toxin uncouples G proteins from receptors by ADP ribosylating a cysteine near the carboxy-terminus of the A subunit¹⁸. When reconstituted with 0.5 ml of distilled water, each vial contains 50 µg of protein in 0.01 M sodium phosphate buffer, pH 7.0, with 0.05 M sodium chloride. For detailed experimental procedures see reference ³.
50 µg
5 x 50 µg

G-105
Pertussis toxin A protomer (from Bordetella pertussi)
99%, MW=26.2 kDa, lyophilized, Storage: 4°C
The A protomer (S-1) of pertussis toxin possesses both NAD⁺ glycohydrolase and ADP-ribosyltransferase activities but is unable to penetrate cells in the absence of B oligomer¹⁷. It is however, as effective as native pertussis toxin in catalyzing ADP-ribosylation in broken cell preparations¹⁹. When reconstituted with 0.5 ml of distilled water, each vial contains 10 µg of protein in 0.01 M Tris, 0.1 mM Na₂EDTA and 0.04% CHAPS, pH 8.0. For detailed experimental procedures see reference ¹⁹.
10 µg
5 x 10 µg

G-110
Pertussis toxin B oligomer (from Bordetella pertussis)
Lyophilized, MW=78.7 kDa, Storage: 4°C
The B oligomer (S-2, S-3, 2 x S-4, and S-5) of pertussis toxin attaches the native toxin to eukaryotic cell surfaces and facilitates the translocation of the A protomer¹⁷. It does not possess any intrinsic ADP-ribosyltransferase activity. It does elicit several physiologic responses including human T cell mitogenesis²⁰, human platelet aggregation²¹ and insulin-like action in rat adipocytes²².
40 µg
5 x 40 µg

ARF REAGENTS

G-445
ARF inhibitory peptide (P-13)
Gly-Asn-Ile-Phe-Ala-Asn-Leu-Phe-Lys-Gly-Leu-Phe-Gly-Lys-Lys-Glu
>97%, MW=1782.0, Storage: -20°C
Sequence is ADP-ribosylation factor (ARF) mARF1p (2-17) N-terminal peptide²³. Peptide inhibits ARF-dependent ADP-ribosylation by cholera toxin, endoplasmic reticulum to Golgi transport, intra-Golgi transport and endosome-endosome fusion in vitro at IC₅₀=10-40 µM^23,24,25,26.
1 mg
5 x 1 mg

G-405
Brefeldin A (BFA)
98%, MW=280.4 [20350-15-6] Storage: -20°C
BFA inhibits binding of the cytosolic coat protein, b-COP and ARF to Golgi membranes^27,28,29. It induces a rapid redistribution of Golgi into the ER and blocks transport of proteins into post-Golgi compartments³⁰. BFA blocks the action of ARF activating protein^31,32,33.
5 mg
25 mg NEW LOWER PRICE

G-435
Ilimaquinone
99%, MW=358.5 [71678-03-0] Storage: -20°C
Induces complete and reversible Golgi membrane breakdown. Inhibits the association of b-COP and ARF to Golgi membranes, but unlike BFA, does not induce a retrograde transport of Golgi enzymes into ER or cause random fusion of successive Golgi cisternae^34,35.
100 µg
5 x 100µg

ADP-RIBOSYLATION INHIBITORS

G-400
3-Aminobenzamide
97%, MW=136.2 [3544-24-9] Storage: RT
Inhibits endogenous poly-ADP-ribosyltransferases often present in membrane preparations with minimal effect on bacterial toxin mediated ADP-ribosylation^36,37.
1 g
5 g

G-440
m-Iodobenzylguanidine·½H₂SO₄
98%, MW=324.1 [80663-95-2] Storage: -20°C
Competitive inhibitor of arginine specific mono-ADP-ribosyltransferase. IC₅₀~100 µM^38,39. Blocks ADP-ribosylation-dependent signal transduction pathways⁴⁰.
10 mg
50 mg

GDP and GTP ANALOGS AND REAGENTS

A-230
Decoyinine (U-7984)
99%, MW=279.2, Storage: 0°C
An adenine-ketose antibiotic which is a specific inhibitor of GMP synthase⁴¹. It may be used to decrease intracellular GTP levels^42,43.
10 mg
50 mg

G-300
Guanosine-5'-O-(2-thiodiphosphate), trilithium salt (GDPbS)
>85%, MW=477.0 [97952-36-8] Storage: -20°C
A nonhydrolyzable GDP analog. Competitively inhibits G protein activation by GTP and GTP analogs^44,45,46.
5 mg
5 x 5 mg

G-305
Guanosine-5'-O-(3-thiotriphosphate), tetralithium salt (GTPgS)
>85%, MW=563.0 [94825-44-2] Storage: -20°C
A nonhydrolyzable, G protein activating, GTP analog^45,46.
10 mg
5 x 10 mg

G-310
Guanylyl-imidodiphosphate, tetralithium salt (Gpp(NH)p)
>85%, MW=545.9 [74812-64-9] Storage: -20°C
A nonhydrolyzable GTP analog. Gpp(NH)p is the preferred GTP analog for activation of ADP-ribosylation factor (ARF)^7,47.
5 mg
25 mg

POSTTRANSLATIONAL MODIFICATION REAGENTS

FARNESYLATION AND GERANYLGERANYLATION

Numerous G proteins are posttranslationally modified by isoprenylation of cysteine residues via a thioether linkage. Two types of isoprenyl groups can be utilized, a C₁₅ farnesyl group and a C₂₀ geranylgeranyl group. Proteins which are farnesylated include Ras, lamin B and several proteins involved in visual signal transduction. Targets which are geranylgeranylated include most g-subunits of heterotrimeric G proteins as well as members of the Ras, Rac/Rho and Rab families (for reviews, see references 48,49,50,51,52). Isoprenylation is required for G protein activity and anchoring in the plasma membrane as well as other protein-protein interactions⁵³. Efforts to design selective farnesyltransferase inhibitors have resulted in several new research tools for studying protein isoprenylation and have raised the possibility of developing new, effective therapeutic agents for cancer^54,55.

G-200
N-Acetyl-S-farnesyl-L-cysteine (AFC)
98%, MW=367.5 [135304-07-3] Storage: -20°C
Members of the Ras superfamily of G proteins⁵⁶, g-subunits of heterotrimeric G proteins⁵⁷ and the a-subunit of cGMP phosphodiesterase from retinal rods⁵⁸ are all carboxyl methylated at carboxy-terminal S-farnesylcysteine residues. AFC specifically inhibits the S-farnesylcysteine methyl transferase (K_m=20µM) in cell free extracts and in whole cells⁵⁹. It inhibits carboxyl methylation of p21^ras17 platelet Rap1⁶⁰ and the g-subunit of transducin⁶¹. It blocks receptor-mediated signal transduction in platelets⁶² and neutrophils (IC₅₀~15 µM)^63,64 not by inhibiting the methyltransferase⁶⁵. but possibly by inhibiting capacitative Ca²⁺ entry⁶⁶.
5 mg
25 mg

G-221
N-Acetyl-S-geranyl-L-cysteine (AGC)
98%, MW=299.4, Storage: -20°C
AGC is a close structural analog of AFC and AGGC but is biologically inactive. It may be used as a negative control for either AFC⁶² or AGGC⁶³.
5 mg
25 mg

G-220
N-Acetyl-S-geranylgeranyl-L-cysteine (AGGC)
98%, MW=435.7 [139332-94-8] Storage: -20°C
AGGC specifically blocks methyl esterification of geranylgeranylated proteins such as Rab proteins⁶⁷. AGGC blocks receptor-mediated signal transduction in human neutrophils (IC₅₀=4 µM)⁶³. Induces insulin release from HIT-T15 cells by mimicking the action of Rab3A⁶⁸ and inhibits b2-integrin-induced actin polymerization (IC₅₀~45nM) in neutrophils⁶⁹.
5 mg
25 mg

G-235
B581
N-(2(S)-(2(R)-Amino-3-mercaptopropylamino)-3-methylbutyl)-Phe-Met-OH
>96%, MW=470.7 [149759-96-6] Storage: -20°C
A potent and selective, cell-permeable farnesyl transferase inhibitor IC₅₀=21 nM, 30-fold selective over geranylgeranyl transferase^70,71.
1 mg
5 mg

G-229
Chaetomellic Acid A·Na₂
99%, MW=370.4, Storage: -20°C
Chaetomellic acid A is a potent inhibitor of farnesyltransferase in isolated enzyme assays⁷² (IC₅₀=55 nM) but is inactive in whole cells. Inhibition of farnesyltransferase is selective over geranylgeranyltransferase I and II (IC₅₀=92 µM and 34 µM respectively)⁷².
5 mg
25 mg

G-223
Ebelactone B
99%, MW=352.5 [76808-15-6] Storage: -20°C
Isoprenylated proteins are reversibly methylated and demethylated and thus are potentially subject to regulation^61,73. Demethylation is carried out by specific esterases including rod outer segment (ROS) membrane methyl esterase. Ebelactone B inhibits ROS membrane methyl esterase (K_i=42 µM) and thus is a useful tool to explore regulation of isoprenylated proteins⁷⁴.
1 mg
5 x 1mg

G-201
S-Farnesyl-L-cysteine methyl ester
97%, MW=339.5, Storage: -70°C
Stimulates the multidrug resistance transporter ATPase activity (4-5-fold at 10-20 µM) and competes for drug binding⁷⁵.
5 mg
25 mg

G-224
Farnesylpyrophosphate
98%, MW=433.5 [13058-04-3] Storage: -20°C
Farnesylpyrophosphate is a farnesyl-donor which is utilized by farnesyltransferase for farnesylation of target proteins^76,77.
200 µg 1 mg
5 x 200 µg

G-222
Farnesylthioacetic acid (FTA)
98%, MW=296.5 [135784-48-4] Storage: -20°C
FTA potently and specifically inhibits methyl esterification of farnesylated proteins such as the g subunit of transducin (70% at 10 µM)⁷⁸. It does not act as a substrate for methyl transferase.
5 mg
25 mg

G-225
Geranylgeranylpyrophosphate
98%, MW=501.5 [6699-20-3] Storage: -20°C
Geranylgeranylpyrophosphate is a geranylgeranyl-donor molecule which is utilized by geranylgeranyltransferase⁷⁹ for isoprenylation of target proteins.
200 µg 1 mg
5 x 200 µg

G-228
a-Hydroxyfarnesylphosphonic acid
96%, MW=302.4 [140633-12-1] Storage: -20°C
a-Hydroxyfarnesylphosphonic acid is a potent inhibitor of farnesyltransferase in isolated enzyme assays^72,77(IC₅₀=30 nM) and in whole cells. Inhibition of farnesyltransferase is selective over geranylgeranyltransferase I and II (IC₅₀=35.8 µM and 67.0 µM respectively)⁷². a-Hydroxyfarnesylphosphonic acid inhibited (1 µM) Ras processing in Ha-ras-transformed NIH 3T3 fibroblasts⁷².
1 mg
5 x 1 mg

G-236
Manumycin A
98%, MW=550.7 [52665-74-4] Storage: -20°C
Inhibits farnesyltransferase (IC₅₀=5 µM) selectively over geranylgeranyltransferase (IC₅₀=180 µM)⁸⁰.
1 mg
5 mg

G-233
Mevastatin (Compactin)
95%, MW=390.5 [73573-88-3] Storage: -20°C
Mevastatin inhibits isoprenoid biosynthesis by inhibition of HMG-CoA reductase (Ki for acid form is 1 nM)⁸³ and therefore blocks protein isoprenylation and reduces plasma cholesterol levels in humans⁸³. It causes cells to arrest early in the G1 phase^81,82. Mevastatin is a close structural analog of lovastatin and both agents have the same biochemical and pharmacological activities⁸³. Mevastatin is inactive in cell-free assays. In cells however, it is hydrolyzed to the active free acid form by intracellular esterases.
10 mg
50 mg
NEW LOWER PRICE

G-238
Mevastatin sodium
95%, MW=414.5, Storage: -20°C
This is the active carboxylate form of mevastatin. It is active in whole cells as well as in cell free assays.
Inquire

G-227
Patulin
98%, MW=154.1 [149-29-1] Storage: -20°C
Patulin is a mycotoxin which inhibits protein farnesylation in a cell free assay (IC₅₀=290 µM). It inhibits [³H] mevalonate incorporation into proteins in whole cells (IC₅₀=7 µM)⁸⁴.
2 mg
10 mg

G-210
Perillic acid
95%, MW=166.2 [7694-45-3] Storage: 0°C
Perillic acid is a limonene derivative which dose-dependently inhibits the isoprenylation of p21^ras and other small G proteins in NIH 3T3 cells and human mammary epithelial cells⁸⁵.
100 mg
500 mg

MYRISTOYLATION AND PALMITOYLATION

G-237
Cerulenin
2,3-Epoxy-4-oxo-7,10-dodecadienamide
98%, MW=223.3 [17397-89-6] Storage: -20°C
Inhibits protein palmitoylation at concentrations in the range of 45-134 µM⁸⁶.
5 mg
25 mg

G-230
2-Hydroxymyristic acid
98%, MW=244.4 [2507-55-3] Storage: 0°C
p56^lck and other members of the Src family of protein-tyrosine⁹⁸ kinases98 as well as the ao, ai and az subfamilies of G protein A subunits⁸⁷ are covalently modified by N-myristoylation of their amino-terminal glycine residues. Myristoylation aids in membrane anchoring and is a requirement for full activity. 2-Hydroxymyristic acid inhibits protein myristoylation following metabolic activation in cultured cells (0.5 mM)⁸⁸. Its selectivity for myristoylation makes it a useful tool to distinguish between protein myristoylation and palmitoylation⁸⁹. It blocks p56^lck mediated signal transduction⁹⁰ and inhibits Varicella-zoster virus replication⁹¹.
50 mg
250 mg

G-234
12-Methoxydodecanoic acid
99%, MW=230.4 [92169-28-3] Storage: RT
A myristate analog which has similar chain length but reduced hydrophobicity compared to myristate. Inhibits replication of HIV-1. Its specific mechanism of action is not clear but it is believed to either inhibit the activity of N-myristoyltransferase or modulate the function of target acylated proteins⁹².
10 mg
50 mg

G-232
4-Oxatetradecanoic acid
99%, MW=230.4, Storage: 0°C
4-Oxatetradecanoic acid is a myristate analog which has similar chain length but reduced hydrophobicity compared to myristate.It inhibits replication of human immunodeficiency virus I and is fungicidal for Cryptococcus neoformans. Its specific mechanism of action is not clear but it is believed to either inhibit the activity of N-myristoyltransferase or modulate the function of target acylated proteins⁹³.
10 mg
50 mg

G-231
2-Fluoropalmitic acid
98%, MW=274.4 [16518-94-8] Storage: 0°C
G protein a subunits including a₀, a_s, a_q, a_i1, a_i2, a_i3, a_z^94,95,96, low molecular weight G proteins such as ras and the protein-tyrosine kinase⁹⁸84 p56^lck are all posttranslationally palmitoylated, a modification that regulates localization and function. 2-Fluoropalmitic acid inhibits the biosynthesis of palmityl-CoA⁹⁹ thereby blocking protein palmitoylation.
5 mg
25 mg

G PROTEIN EFFECTORS AND ANTAGONISTS

G PROTEIN EFFECTORS

EI-179
Compound 48/80
Average MW=630 [94724-12-6] Storage: 0°C
Compound 48/80 is an oligomeric mixture of condensation products of N-methyl-p-methoxyphenethylamine and formaldehyde. It activates G proteins by a mechanism analogous to that of mastoparan^100,101. It inhibits calmodulin^102,103 and human platelet PLC and exhibits a concentration dependent biphasic modulation of human platelet PLA₂¹⁰⁴.
100 mg
500 mg

G-410
Mastoparan, (Vespula lewisii)
Ile-Asn-Leu-Lys-Ala-Leu-Ala-Ala-Leu-Ala-Lys-Lys-Ile-Leu-NH2
98%, MW=1478.9 [72093-21-1] Storage: -20°C
Mastoparan is an amphiphilic wasp venum, tetradecapeptide capable of directly activating G proteins by a mechanism analogous to that of G protein-coupled receptors. It is cell permeable (EC₅₀=14 µM in Swiss 3T3 cells) and acts preferentially on G_i and G_O rather than G_s^105,106,107. It stimulates exocytosis and phosphoinositide breakdown in a variety of cells^108,109,110. It inhibits calmodulin^111,112 and activates PLA2¹¹³. In Swiss 3T3 cells it acts as a mitogen and stimulates pertussis toxin-sensitive arachidonate release without phosphoinositide breakdown¹¹⁴.
1 mg
5 x 1 mg

G-415
Mastoparan X, (Vespa xanthoptera)
Ile-Asn-Trp-Lys-Gly-Ile-Ala-Ala-Met-Ala-Lys-Lys-Leu-Leu-NH2
98%, MW=1555.9, Storage: -20°C
Mastoparan X^115,116 has similar activity to mastoparan¹⁰⁰.
1 mg
5 x 1 mg

G-420
Mas 7
Ile-Asn-Leu-Lys-Ala-Leu-Ala-Ala-Leu-Ala-Lys-Ala-Leu-Leu-NH2
98%, MW=1420.9, Storage: -20°C
A mastoparan analog with 5-fold greater potency than mastoparan¹⁰⁰.
1 mg
5 x 1 mg

G-421
Mas 17
Ile-Asn-Leu-Lys-Ala-Lys-Ala-Ala-Leu-Ala-Lys-Lys-Leu-Leu-NH2
98%, MW=1493.0, Storage: -20°C
Inactive analog of mastoparan. May be used as a negative control¹⁰⁶.
1 mg
5 x 1 mg

G-425
Mastoparan, Polistes, (Polistes jadwagae)
Val-Asp-Trp-Lys-Lys-Ile-Gly-Gln-His-Ile-Leu-Ser-Val-Leu-NH2
98%, MW=1635.9 [74129-19-4] Storage: -20°C
Polistes mastoparan has similar activity to mastoparan¹¹⁶.
1 mg
5 x 1 mg

G-505
Melittin
>95%, MW=2846.5 [37231-28-0] Storage: -20°C
Gly-Ile-Gly-Ala-Val-Leu-Lys-Val-Leu-Thr-Thr-Gly-Leu-Pro-Ala-Leu-Ile-Ser-Trp-Ile-Lys-Arg-Lys-Arg-Gln-Gln-NH2
Melittin is a PLA2 stimulatory, 26-residue bee venum peptide with sequence similarity to PLAP¹¹⁷. It activates phospholipase A₂ (5-fold at 10 µg/ml) in BC3H₁ cell sonicates¹¹⁷.
250 µg
5 x 250 µg

G-500
PLAP Peptide
>98%, MW=2330.8, Storage: -20°C
Glu-Ser-Pro-Leu-Ile-Ala-Lys-Val-Leu-Thr-Thr-Glu-Pro-Pro-Ile-Ile-Thr-Pro-Val-Arg-Arg
PLAP peptide is a 21-residue PLAP (PLA₂ Activating Protein) fragment which spans the PLAP-melittin homology sequence. PLAP peptide activates phospholipase A₂ (10-fold at 1 µg/ml) in BC3H₁ cell sonicates¹¹⁷. PLAP was recently recognized as a member of the b-transducin (G_b) superfamily¹¹⁸.
250 µg
5 x 250 µg

G PROTEIN ANTAGONISTS

G-510
GP Antagonist-2
99%, MW=1093.6, Storage: -20°C
Pyr-Gln-D-Trp-Phe-D-Trp-D-Trp-Met-NH2
A G protein antagonist which inhibits the activation of G_i or G_O by M2 muscarinic cholinergic receptors and G_s by b-adrenergic receptors. Inhibition is reversible and competitive with respect to receptor binding to G proteins¹¹⁹.
1 mg
5 x 1 mg

G-515
GP Antagonist-2A
99%, MW=1589.3, Storage: -20°C
Arg-Pro-Lys-Pro-Gln-Gln-D-Trp-Phe-D-Trp-D-Trp-Met-NH2
A G protein antagonist which selectively inhibits the activation of G_q by M1 muscarinic cholinergic receptors. Inhibition is reversible and competitive with respect to receptor binding to G proteins¹¹⁹. Also inhibits activation by cholecystokinin receptor in pancreatic acini at 10 µM¹²⁰.
1 mg
5 x 1 mg

G-520
Isotetrandrine
98%, MW=622.8 [477-57-6] Storage: -20°C
Isotetrandrine is a biscoclaurine alkaloid which inhibits G protein activation of PLA₂ but not PLC or PLD^121,122.
1 mg
5 mg

G-430
Suramin sodium
98%, MW=1429.2 [129-46-4] Storage: RT
Suramin uncouples G proteins from receptors presumably by blocking their interaction with intracellular receptor domains¹²³. It also inhibits the cell surface binding of various growth factors including PDGF, EGF and TGF-b^{124,125,126,127}. It is a potent competitive inhibitor of reverse transcriptase^128,129 and protects T lymphocytes against in vitro human immunodeficiency virus infection¹³⁰. It is a potent inhibitor of melanoma heparanase and tumor cell metastasis¹³¹.
50 mg
250 mg

G PROTEIN ANTIBODIES

SA-280
Anti-Ga₀ subunit
Mouse monoclonal antibody. Clone 2A.3. Immunogen: Partially purified bovine brain Ga₀ protein. Supplied as purified IgG1, 0.2 mg/ml. Recognizes human, bovine, guinea pig, rat and mouse Ga₀. No crossreactivity with transducin, Ga_i1, Ga_i2, Ga_i3 or Ga_s. ADP-ribosylation of Ga₀ does not alter the immunoreactivity. Applications: WB 1 µg/ml.
100 µg

SA-281
Anti-Ga_i1 subunit
Mouse monoclonal antibody. Clone R4.5. Immunogen: Partially purified rat brain G_ai1 protein. Supplied as purified IgG2b, 0.2 mg/ml. Recognizes human, bovine, guinea pig, rat and mouse Ga_i1. No crossreactivity with transducin, Ga₀, Ga_i2, Ga_i3 or Ga_s. ADP-ribosylation of Ga_i1 does not alter the immunoreactivity. Applications: WB 1 µg/ml.
100 µg

SA-127
Anti-Ga_il subunit
Rabbit polyclonal antibody. Immunogen: Ga_il (159-168) peptide^132,133. Supplied as purified IgG. Denature protein to expose epitope. Applications: WB 1/1000, IP.
50 µl

SA-128
Anti- Ga_i1 and Ga_i2 subunits
Rabbit polyclonal antibody. Immunogen: Ga_i1,2 subunits C-terminal (345-354) peptide conserved sequence^132,133. Supplied as purified IgG. Applications: WB 1/1000, IH.
50 µl

SA-282
Anti-Ga_i2 subunit
Mouse monoclonal antibody. Clone L5.6. Immunogen: Recombinant rat Ga_i2 protein. Supplied as purified IgG2b, 0.2 mg/ml. Recognizes human, bovine, guinea pig, rat and mouse Ga_i2. No crossreactivity with transducin, Ga₀, Ga_i1, Ga_i3 or Ga_s. ADP-ribosylation of Ga_i1 does not alter the immunoreactivity. Applications: WB 1 µg/ml.
100 µg

SA-129
Anti-Ga_i3 subunit
Rabbit polyclonal antibody. Immunogen: Ga_i3 subunit, C-terminal (345-354) peptide^132,134. Supplied as purified IgG. Applications: WB 1/1000, IP.
50 µl

SA-130
Anti-Ga_i3 and Ga_O
Rabbit polyclonal antibody. Immunogen: Ga_i3and Ga_O subunits C-terminal (345-354) peptide. Supplied as dialysed serum. Applications: WB 1/1000, IP.
50 µl

SA-131
Anti-Ga_s subunit
Rabbit polyclonal antibody. Immunogen: Ga_s subunit C-terminal (385-394) peptide^132,134. Supplied as purified IgG. Recognizes 45 and 52 kDa forms. Denature protein to expose epitope. Applications: WB 1/1000, IP.
50 µl

SA-132
Anti-Ga_z subunit
Rabbit polyclonal antibody. Immunogen: Ga_z subunit N-terminal (3-18) peptide^132,133. Supplied as purified IgG. Denature protein to expose epitope. Applications: WB 1/1000, IP.
50 µl

SA-232
Anti-Ga_q/11 subunit
Rabbit polyclonal antibody. Immunogen: Mouse G-protein Ga_q/11 subunits C-terminal sequence peptide conjugated to KLH^132,133,135. Supplied as purified IgG. Recognizes specifically Ga_q and Ga₁₁ subunits from human, dog, hamster, rat and mouse. Applications: WB 1/1000, IH, IP.
50 µl

SA-126
Anti-G protein, a-subunit
Rabbit polyclonal antibody. Immunogen: Ga_z subunit (40-54) peptide, part of the GTP binding domain^132,133. Supplied as purified IgG. Cross-reacts with Ga_s, Ga_i1, Ga_i2, Ga_i3, Ga₀, Ga_z and Ga_t. Applications: WB 1/1000, IP denatured protein only.
50 µl

SA-125
Anti-G protein, b-subunit internal
Rabbit polyclonal antibody. Immunogen: Gb (127-139) peptide^136,137. Supplied as purified IgG. Specificity is G-protein 35 and 36 kDa b-subunits. Applications: WB 1/1000, IP.
50 µl

SA-182
G Protein Antibody set
Contains 10 µl of each of the following antibodies: SA-125, SA-127, SA-128, SA-129, SA-130 and SA-131.
1 ea

SA-181
Anti-GTPase activating protein (GAP)
Mouse monoclonal antibody. Clone B4F8. Immunogen: Full length recombinant human GAP¹³⁸. Supplied as purified IgG2a, lyophilized. Reacts with human, rat, mouse, bovine and simian 120 kDa ras GAP. Applications: WB 10 µg/ml, IF 5 µg/ml, IP (GAP related p190 kDa protein co-immunoprecipitates).
100 µg

SMALL G PROTEINS

PROTEINS

SE-131
H-Ras, Wild-Type (human, recombinant)
>95% by SDS-PAGE, MW=20 kDa, Storage: -70°C
A substrate for farnesyltransferase (>25%) with K_m~4 µM using rat brain FT^139,140,141. Possesses GDP binding at >1:4 GDP/H-ras.
100 µg
5 x 100 µg

SE-132
H-Ras, CVLL-Type (human, recombinant)
>95% by SDS-PAGE, MW=20 kDa, Storage: -70°C
This is H-ras with a C-terminal mutation to CVLL. It is a substrate for geranylgeranyltransferase rather than farnesyltransferase. Extent of geranylgeranylation is >25% with K_m~4 µM using bovine brain G-GT. Possesses GDP binding at >1:4 GDP/H-ras.
100 µg
5 x 100 µg

SE-136
Rab3a (human, recombinant)
>90% by SDS-PAGE, MW=21 kDa, Storage: -70°C
Human Rab3a expressed in E. coli. It is a physiological substrate for geranylgeranyltransferase type II^142,143>. Extent of geranylgeranylation is >1:4 GDP/Rab3a.
100 µg
5 x 100 µg

REAGENTS

G-130
C3 Exoenzyme (from Clostridium botulinum)
98%, MW=25 kDa, lyophilized, Storage: -20°C
C3 Exoenzyme selectively ADP-ribosylates low molecular weight G proteins of the Rho subfamily at an asparagine residue within the putative effector domain.

G-239
Farnesylthiosalicylic acid
98%, MW=358.5, Storage: -20°C
Inhibits the growth of Ha-ras-transformed cells and reverses their morphology in a dose-dependent fashion (0.1-10 µM). Inhibits protein carboxymethylation independent of its growth inhibitory activity¹⁴⁴.
10 mg
50 mg

GR-309
Trichostatin A
Induces reversion of ras-transformed cells to normal morphology¹⁴⁵.

References

1. A.M. Spiegel Med. Res. Rev. 1992 12 55

2. Y. Kaziro et al. Annu. Rev. Biochem. 1991 60 349

3. M. Ui In ADP-ribosylating Toxins and G Proteins (J. Moss and M. Vaughn, eds.) American Society for Microbiology, Washington DC, 1990 p.64

4. J. Moss and M. Vaughn In Handbook of Natural Toxins (M.C. Hardegree and A.T. Tu, eds.) Marcel Dekker, New York, 1988 4 39

5. P.J. Romero and C. Weitzman et al. Biochem. Biophys. Res. Commun. 1991 181 208

6. O. Weiss et al. J. Biol. Chem. 1989 264 21066

7. D.M. Gill and M.J. Woolkalis Methods Enzymol. 1991 195 267

8. D. Masco et al. J. Neuroscience 1991 11 2443

9. A. Valencia et al. Biochemistry 1991 30 4637

10. M. Schmidt et al. J. Biol. Chem. 1996 271 2422

11. P. Lang et al. J. Biol. Chem. 1992 267 11677

12. K. Takaishi et al. Mol. Cell. Biol. 1993 13 72

13. N. Morii et al. J. Biol. Chem. 1992 267 20921

14. K. Moldave et al. Annu. Rev. Biochem. 1985 54 1109

15. L.D. Phan et al. J. Biol. Chem. 1993 268 8665

16. V.G. Johnson et al. J. Biol. Chem. 1993 268 3514

17. M. Tamura et al. Biochemistry 1982 21 5516

18. J. Moss and M. Vaughn Adv. Enzymol. 1988 61 303

19. G.S. Kopf and M.J. Woolkalis Methods Enzymol. 1991 195 257

20. C.F. Strand and R.A. Carchman FEBS Lett. 1987 225 16

21. S. Banga et al. J. Biol. Chem. 1987 262 14871

22. M. Tamura et al. J. Biol. Chem. 1983 258 6756

23. R.A. Kahn et al. J. Biol. Chem. 1992 267 13039

24. P.A. Randazzo et al. J. Biol. Chem. 1993 268 9555

25. J.M. Lenhard et al. J. Biol. Chem. 1992 267 13047

26. W.E. Balch et al. J. Biol. Chem. 1992 267 13053

27. J.G. Donaldson et al. Science 1991 254 1197

28. J.G. Donaldson et al. J. Cell Biol. 1991 112 579

29. L. Orci et al. Cell 1991 64 1183

30. J. Lippincott-Schwartz et al. Cell 1990 60 821

31. P.A. Randazzo et al. J. Biol. Chem. 1993 268 9555

32. J.G. Donaldson et al. Nature 1992 360 350

33. J.B. Helms et al. Nature 1992 360 352

34. P.A. Takizawa et al. Cell 1993 73 1

35. B. Veit et al. J. Cell Biol. 1993 122 1197

36. K.R. Kozak and I.A. Ross Biochem. Biophys. Res. Commun. 1991 179 1225

37. C.J. Skidmore et al. In ADP-Ribose Transfer Reactions, Mechanisms and Biological Significance (M.K. Jacobsen and E.L. Jacobsen, eds.) Springer-Verlag, New York, 1989 p.109

38. L.A. Smets et al. Biochim. Biophys. Acta 1990 1054 49

39. C. Loesberg et al. Biochim. Biophys. Acta 1990 1037 92

40. H. Halldorsson et al. FEBS Lett. 1992 314 322

41. R.J. Suhadolnick Nucleoside Antibiotics John Wiley and Sons, New York, 1970, pp.96-121

42. M.A. Glazebrook J. Gen. Microbiol. 1990 136 581

43. A. Fouet and A.L. Sonenshein J. Bacteriol. 1990 172 835

44. R.M. Burch and J Axelrod et al. Proc. Natl. Acad. Sci. USA 1987 84 6374

45. S.T. Silk et al. J. Biol. Chem. 1989 264 21466

46. A.G. Gilman Annu. Rev. Biochem. 1987 56 615

47. D.M. Gill and J. Coburn Biochemistry 1987 26 6364

48. C.A. Omer and J.B. Gibbs Mol. Microbiol. 1994 11 219

49. G.A. Caldwell et al. Microbiol. Rev. 1995 59 406

50. J.A. Glomset and C.C. Farnsworth Annu. Rev.Cell Biol. 1994 10 181

51. P.J. Casey and M.C. Seabra J. Biol. Chem. 1996 271 5289

52. F.L. Zhang and P.J. Casey Annu.. Rev. Biochem. 1996 65 241

53. C.J. Marshall Sc ience 1993 259 1865

54. J.E. Buss and J.C. Marsters, Jr. Chemistry Biology 1995 2 787

55. F. Tamanoi Trends Biochem. Sci. 1993 18 349

56. A. Hall Science 1990 249 635

57. H.K. Yamane et al. Proc. Natl. Acad. Sci. USA 1990 87 5868

58. O.C. Ong et al. Proc. Natl. Acad. Sci. USA 1989 86 9238

59. C. Volker et al. J. Biol. Chem. 1991 266 21515

60. Huzoor-Akbar et al. J. Biol. Chem. 1991 266 4387

61. D. Perez-Sala et al. Proc. Natl. Acad. Sci. USA 1991 88 3043

62. Huzoor-Akbar et al. Proc. Natl. Acad. Sci. USA 1993 90 868

63. M.R. Philips et al. Science 1993 259 977

64. J. Ding et al. J. Biol. Chem. 1994 269 16837

65. Y. Ma et al. Biochemistry 1994 33 5414

66. Y. Xu. et al. Mol. Pharmacol. 1996 50 1495

67. C. Volker et al. FEBS Lett. 1991 295 189

68. R. Regazzi et al. Biochim. Biophys. Acta 1995 1268 269

69. L. Malony et al. Biochem. Biophys.Res. Commun.. 1996 223 612

70. M.A. Garcia et al. J. Biol. Chem. 1993 268 18415

71. A.D. Cox et al. J. Biol. Chem. 1994 269 19203

72. J.B. Gibbs et al. J. Biol. Chem. 1993 268 7617

73. C.J. Marshall Science 1993 259 1865

74. E.W. Tan and R.R. Rando Biochemistry 1992 31 5572

75. L. Zhang et al. J. Biol. Chem. 1994 269 15973

76. Y. Reiss et al. J. Biol. Chem. 1992 267 6403

77. D.L. Pompliano et al. Biochemistry 1992 31 3800

78. E.W. Tan et al. J. Biol. Chem. 1991 266 10719

79. M. Seabra et al. J. Biol. Chem. 1992 267 14497

80. M. Hara et al. Proc. Natl. Acad. Sci. USA 1993 90 2281

81. V. Quesney-Huneeus et al.J. Biol. Chem. 1983 258 378

82. V. Quesney-Huneeus et al. Proc. Natl. Acad. Sci. USA 1979 76 5056

83. A. Endo J.Lipid Res. 1992 33 1569

84. S. Miura et al. FEBS Lett. 1993 318 88

85. P.L. Crowell et al. J. Biol. Chem. 1991 266 17679

86. S.A. Metz et al. Biochem.. J. 1993 295 31

87. A.M. Spiegel et al. Trends Biochem. Sci. 1991 16 338

88. L.A. Paige et al. Biochemistry 1990 29 10566

89. L.A. Paige et al. J. Biol. Chem. 1993 268 8669

90. M.J.S. Nadler et al. Biochemistry 1993 32 9250

91. D.R. Harper et al. J. Gen. Virol. 1993 74 1181

92. J.I. Gordon Clin. Res. 1990 38 517

93. C.A. Langner et al. J. Biol. Chem. 1992 267 17159

94. M.E. Linder et al. Proc. Natl. Acad. Sci. USA 1993 90 3675

95. M. Parenti et al. Biochem. J. 1993 291 349

96. M.Y. Degtyarev et al. Biochemistry 1993 32 8057

97. J.F. Hancock et al. Cell 1989 57 1167

98. N. Abraham and A. Veillette Mol. Cell. Biol. 1990 10 5197

99. R.M. Soltysiak et al. Biochim. Biophys. Acta 1984 792 214

100. T. Higashijima et al. J. Biol. Chem. 1990 265 14176

101. M. Mousli et al. FEBS Lett. 1990 259 260

102. K. Gietzen et al. Biochim. Biophys. Acta 1983 736 109

103. K. Gietzen Biochem. J. 1983 216 611

104. C. Bronner et al. Biochim. Biophys. Acta 1987 920 301

105. T. Higashijima et al. J. Biol. Chem. 1988 263 6491

106. T. Higashijima et al. J. Biol. Chem. 1990 265 14176

107. R. Weingarten et al. J. Biol. Chem. 1990 265 11044

108. M. Mousli et al. J. Pharmacol. Exp. Ther. 1989 250 329

109. N. Yokokawa et al. Biochem. Biophys. Res. Commun. 1989 158 712

110. J. Adolfo Garcia-Sainz et al. Biochem. Biophys. Res. Commun. 1991 179 852

111. M. Barnette et al. Biochem. Pharmacol. 1983 32 2929

112. D. Malencik and S. Anderson Biochem. Biophys. Res. Commun. 1983 114 50

113. A. Argiolas and J.J. Pisano J. Biol. Chem. 1983 258 13697

114. J. Gil et al. J. Cell Biol. 1991 113 943

115. T. Higashijima et al. FEBS Lett. 1983 152 227

116. T. Nakajima et al. Peptides 1985 6 425

117. M.A. Clark et al. Proc. Natl. Acad. Sci. USA 1991 88 5418

118. M.C. Peitsch et al. Trends Biochem. Sci. 1993 18 292

119. H. Mukai et al. J. Biol. Chem. 1992 267 16237

120. Y. Tsunoda and C. Owyang. Biochem. Biophys. Res. Commun. 1995 211 648

121. S. Akiba et al. Biochem. Pharmacol. 1992 44 45

122. T. Hashizume et al. Biochem. Pharmacol. 1991 41 419

123. R.-R.C. Huang et al. Mol. Pharmacol. 1990 37 304

124. M. Hosang J. Cell. Biochem. 1985 29 265

125. C. Betsholz et al. Proc. Natl. Acad. Sci. USA 1986 83 6440

126. J.R. Coffey et al. J. Cell. Physiol. 1987 132 143

127. R. Kopp and A. Pfeiffer Cancer Res. 1990 50 6490

128. E. De Clercq Cancer Lett. 1979 8 9

129. K. Jentsch et al. J. Gen. Physiol. 1987 68 2183

130. H. Mitsuya et al. Science 1984 226 172

131. M. Nakajima et al. J. Biol. Chem. 1991 266 9661

132. S.M. Mumby and A.G. Gilman, Methods Enzymol. 1991 195 215

133. P.P. Goldsmith et al. J. Biol. Chem. 1987 262 683

134. D.T. Jones and R.R. Reed J. Biol. Chem. 1987 262 241

135. S. Offermanns et al. J. Biol. Chem. 1987 262 683

136. M.A. Levine et al. J. Biol. Chem. 1990 265 3553

137. D.N. Posnett et al. J. Biol. Chem. 1988 263 1719

138. J. Settleman et al. Cell 1992 69 539

139. G.L. James et al. Science 1993 260 1937

140. M.C. Seabra et al. Cell 1991 65 429

141. Y. Reiss et al. Cell 1990 62 81

142. E.J. Tisdale et al. J. Cell Biol. 1992 119 749

143. R. Khosravi-Far et al. Proc. Natl. Acad. Sci. USA 1991 88 6264

144. M. Marom et al. J. Biol. Chem. 1995 270 22263

145. M. Futamora et al. Oncogene 1995 20 1119