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208780 Calmodulin, Biotinylated, Porcine Brain

208780
  
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Přehled

Replacement Information
Description
Overview

This product has been discontinued.



Calmodulin (CaM) purified from porcine brain and biotinylated using NHS ester-activated biotin with an 8 atom spacer arm. A ubiquitous, calcium-binding protein that interacts with and regulates a wide variety of proteins, thus affecting different cellular functions and calcium-calmodulin-dependent signaling pathways. CaM mediates several biological processes, such as inflammation, apoptosis, muscle contraction, intracellular movement, short-term and long-term memory, nerve growth, and the immune response. Useful for enzyme activation, CaM binding studies, and general assessment of CaM-dependent signaling pathways. Biotin/Protein Ratio: 0.5-1.0 as determined by HABA assay.

Catalogue Number208780
Brand Family Calbiochem®
References
ReferencesBillingsley, M.L., et al. 1985. Proc. Natl. Acad. Sci. USA 82, 7585.
Product Information
Unit of DefinitionOne unit is defined as the amount of calmodulin that will stimulate 0.01 unit of 3'5'-cyclic nucleotide phosphodiesterase to 50% of the maximum activity of the enzyme when saturated with CaM in the presence of 100 µM Ca<sup>2+</sup> in a 3 ml reaction volume at 30°C, pH 7.5.
FormLyophilized
FormulationLyophilized from 10 mM sodium phosphate buffer, 5% sucrose, pH 7.0.
Quality LevelMQ100
Applications
Biological Information
Purity>98% by SDS-PAGE
Specific Activity≥ 35,000 U/mg protein
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Blue Ice Only
Toxicity Standard Handling
Storage -20°C
Avoid freeze/thaw Avoid freeze/thaw
Do not freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Katalogové číslo GTIN
208780 0

Documentation

Calmodulin, Biotinylated, Porcine Brain MSDS

Title

Safety Data Sheet (SDS) 

Calmodulin, Biotinylated, Porcine Brain Certificates of Analysis

TitleLot Number
208780

References

Přehled odkazů
Billingsley, M.L., et al. 1985. Proc. Natl. Acad. Sci. USA 82, 7585.
Data Sheet

Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

Revision25-September-2007 JSW
DescriptionCalmodulin (CaM) purified from porcine brain and biotinylated using NHS ester-activated biotin with an 8 atom spacer arm. A ubiquitous, calcium-binding protein that interacts with and regulates a wide variety of proteins, thus affecting different cellular functions and calcium-calmodulin-dependent signaling pathways. CaM mediates several biological processes, such as inflammation, apoptosis, muscle contraction, intracellular movement, short-term and long-term memory, nerve growth, and the immune response. Useful for enzyme activation, CaM binding studies, and general assessment of CaM-dependent signaling pathways. Biotin/Protein Ratio: 0.5-1.0 as determined by HABA assay.
FormLyophilized
FormulationLyophilized from 10 mM sodium phosphate buffer, 5% sucrose, pH 7.0.
Purity>98% by SDS-PAGE
Specific activity≥ 35,000 U/mg protein
Unit definitionOne unit is defined as the amount of calmodulin that will stimulate 0.01 unit of 3'5'-cyclic nucleotide phosphodiesterase to 50% of the maximum activity of the enzyme when saturated with CaM in the presence of 100 µM Ca2+ in a 3 ml reaction volume at 30°C, pH 7.5.
SolubilityH₂O (1 mg/ml)
Storage Avoid freeze/thaw
-20°C
Do Not Freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 6 months at -20°C.
Toxicity Standard Handling
ReferencesBillingsley, M.L., et al. 1985. Proc. Natl. Acad. Sci. USA 82, 7585.