O5003
OPI Media Supplement
Hybri-Max™, γ-irradiated, powder, suitable for hybridoma
Synonym(s):
OPI Media for cell culture
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About This Item
NACRES:
NA.75
UNSPSC Code:
12352207
Product Name
OPI Media Supplement, Hybri-Max™, γ-irradiated, powder, suitable for hybridoma
grade
Hybri-Max™
sterility
γ-irradiated
form
powder
concentration
18-40 mg/vial
technique(s)
cell culture | hybridoma: suitable
impurities
endotoxin, tested
storage temp.
−20°C
Quality Level
Application
OPI Media Supplement has been used to grow hybridoma cell lines from XenoMouse strains and BALB/c female mice.
Other Notes
Formulated with: 0.15 g oxaloacetate, 0.05 g pyruvate, and 0.0082 g insulin.
Preparation Note
Reconstitute contents of vial with 10 mL sterile water. Do not use cell culture medium for initial reconstitution. Each vial sufficient to prepare 1 liter of medium. Final working concentration: 1 mM oxaloacetate, 0.45 mM pyruvate, 0.2 U/ml insulin.
Legal Information
Hybri-Max is a trademark of Sigma-Aldrich Co. LLC
signalword
Danger
hcodes
Hazard Classifications
Eye Dam. 1 - Skin Corr. 1 - Skin Sens. 1
Storage Class
8A - Combustible corrosive hazardous materials
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Andrew W Drake et al.
Analytical biochemistry, 328(1), 35-43 (2004-04-15)
Two biophysical methods, Biacore and KinExA, were used to kinetically and thermodynamically characterize high-affinity antigen/antibody complexes. Three to five independent experiments were performed on each platform with three different antigen/antibody complexes possessing nanomolar to picomolar equilibrium dissociation constants. By monitoring
Gabriela A Canziani et al.
Analytical biochemistry, 325(2), 301-307 (2004-01-31)
Experimental and data analysis protocols were developed to screen antibodies from hybridoma culture supernatants using Biacore surface plasmon resonance biosensor platforms. The screening methods involved capturing antibodies from crude supernatants using Fc-specific antibody surfaces and monitoring antigen binding at a
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Andrew W Drake et al.
Analytical biochemistry, 328(1), 35-43 (2004-04-15)
Two biophysical methods, Biacore and KinExA, were used to kinetically and thermodynamically characterize high-affinity antigen/antibody complexes. Three to five independent experiments were performed on each platform with three different antigen/antibody complexes possessing nanomolar to picomolar equilibrium dissociation constants. By monitoring
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