, p85-alpha
Product Description
The PI3K contains a 110 kDa catalytic subunit and a
85 kDa regulatory subunit. A number of isoforms of the
110 kDa catalytic subunit and the 85 kDa regulatory
subunit
6Ckine.1-3
Human and mouse 6Ckine are highly conserved and
show 86% amino acid homology.1 Mouse 6Ckine cDNA
encodes a 133 amino acid precursor protein, a
23 amino acid signal peptide, and a 110 amino
unstable in the presence of water (see list below). 6
pH half-life [min.]
7.0 110
7.5 55
8.0 35
References:
1. D.E. Fahrney, A.M. Grold, Specific trypsin and chymotrypsin inhibitor, J. Am. Chem
region EU 50 1
IPI00382480 Ig heavy chain V-III region BRO 76 1 113 1 110 1 110 1 55 1
IPI00003111 Ig kappa chain V-I region AU 53 1
IPI00387025 Ig kappa chain V-I region DEE
B
ulletin A
L-110
PRODUCT NO.
revised 4 / 96 4 pages
Oxalyl Chloride
For many years we have supplied much of the world's needs
for research quantities of oxalylchloride.1 Now, we are also
p85α: PIK3R1, GRB1
Product Description
PI3K contains a 110 kDa catalytic subunit and a 85 kDa
regulatory subunit. A number of isoforms of the
110 kDa catalytic subunit and the 85 kDa regulatory
subunit
dependence of
CO2 hydration catalyzed by human carbonic
anhydrase I. Biochim. Biophys. Acta, 1120(1),
81-86 (1992).
11. Engstrand, C., et al., Proton transfer roles of lysine
64 and glutamic acid 64
solutions
at 25 °C have been reported as follows:27
• pH 7.0: 110 minutes
• pH 7.5: 55 minutes
• pH 8.0: 35 minutes
References
1. Fahrney, D.E., and Gold
dependence of
CO2 hydration catalyzed by human carbonic
anhydrase I. Biochim. Biophys. Acta, 1120(1),
81-86 (1992).
11. Engstrand, C., et al., Proton transfer roles of lysine
64 and glutamic acid
other human C-C chemokines.1 Comparatively, mouse
6Ckine cDNA encodes a 133 amino acid precursor
protein, a 23 amino acid signal peptide and a 110
amino acid mature protein.1
The human 6Ckine gene
mass of the reduced protein is approximately
86 kDa, but as a result of glycosylation, the recombinant
EphA3/Fc chimera migrates as an approximately 110
kDa protein on reducing SDS-PAGE.
The Eph