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208670 Calmodulin, His•Tag® Human, Recombinant

Calmodulin, His•Tag® Human, Recombinant, is a full-length, recombinant human calmodulin fused to a His•Tag® sequence at the N-terminus. Contains four functional Ca2+-binding sites.

Ficha de datos de seguridad (MSDS o SDS), certificado de análisis y de calidad (CoA y CoQ), expedientes, folletos y otros documentos disponibles.

Sinónimos: Calmodulin, Human, Recombinant

208670
Purchase on Sigma-Aldrich

Descripción

Replacement Information

Products

Número de referenciaEmbalaje Cant./Env.
208670-50UG Ampolla de plást. 50 μg
Description
OverviewFull-length, recombinant human calmodulin fused to a His•Tag® sequence at the N-terminus. Contains four functional Ca2+-binding sites (aa 20-31; aa 56-67; aa 93-104; aa 129-140) with EF-hands (aa 7-42; aa 43-78; aa 80-115; aa 116-148); and a ubiquitination site at Lys21. This preparation is qualified for use as a substrate for protein tyrosine kinases in in vitro assays. Through its interaction with Ca2+, calmodulin mediates the control of a large number of enzymes, including protein kinases and phosphatases. It is expected to be phosphorylated at Thr44 by CaMK4. In addition, it serves as a substrate for various protein tyrosine kinases.
Catalogue Number208670
Brand Family Calbiochem®
SynonymsCalmodulin, Human, Recombinant
Application Data
References
ReferencesChou, J.J., et al. 2001.Nat. Struct. Biol.8, 990.
Lennon, G., et al. 1996.Genomics33, 151.
Product Information
FormLiquid
FormulationIn PBS, 0.2% Protease Inhibitor Cocktail Set VII (Cat. No. 539138).
Quality LevelMQ100
Applications
Biological Information
Purity>90% by SDS-PAGE
Concentration Label Please refer to vial label for lot-specific concentration
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Dry Ice Only
Toxicity Standard Handling
Storage ≤ -70°C
Avoid freeze/thaw Avoid freeze/thaw
Do not freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
Packaging Information
Transport Information
Supplemental Information
Specifications
Global Trade Item Number
Número de referencia GTIN
208670-50UG 04055977203295

Documentation

Calmodulin, His•Tag® Human, Recombinant Ficha datos de seguridad (MSDS)

Título

Ficha técnica de seguridad del material (MSDS) 

Calmodulin, His•Tag® Human, Recombinant Certificados de análisis

CargoNúmero de lote
208670

Referencias bibliográficas

Visión general referencias
Chou, J.J., et al. 2001.Nat. Struct. Biol.8, 990.
Lennon, G., et al. 1996.Genomics33, 151.
Ficha técnica

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.

Revision28-May-2008 RFH
SynonymsCalmodulin, Human, Recombinant
Application Data
DescriptionFull-length, recombinant human calmodulin fused to a His•Tag® sequence at the N-terminus. Contains four functional Ca2+-binding sites (aa 20-31; aa 56-67; aa 93-104; aa 129-140) with EF-hands (aa 7-42; aa 43-78; aa 80-115; aa 116-148); and a ubiquitination site at Lys21. This preparation is qualified for use as a substrate for protein tyrosine kinases in in vitro assays. Through its interaction with Ca2+, calmodulin mediates the control of a large number of enzymes, including protein kinases and phosphatases. It is expected to be phosphorylated at Thr44 by CaMK4. In addition, it serves as a substrate for various protein tyrosine kinases.
FormLiquid
FormulationIn PBS, 0.2% Protease Inhibitor Cocktail Set VII (Cat. No. 539138).
Concentration Label Please refer to vial label for lot-specific concentration
Purity>90% by SDS-PAGE
Storage Avoid freeze/thaw
≤ -70°C
Do Not Freeze Ok to freeze
Special InstructionsFollowing initial thaw, aliquot and freeze (-70°C).
Toxicity Standard Handling
ReferencesChou, J.J., et al. 2001.Nat. Struct. Biol.8, 990.
Lennon, G., et al. 1996.Genomics33, 151.