Skip to Content
Merck
All Photos(1)

Key Documents

07-482

Sigma-Aldrich

Anti-Calmodulin Binding Protein Epitope Tag Antibody

Upstate®, from rabbit

Sign Into View Organizational & Contract Pricing


About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

purified antibody

antibody product type

primary antibodies

clone

polyclonal

purified by

affinity chromatography

species reactivity

E. coli

manufacturer/tradename

Upstate®

technique(s)

western blot: suitable

isotype

IgG

shipped in

wet ice

target post-translational modification

unmodified

General description

Calmodulin (CaM), a small 17 kDa ubiquitous Ca2+-binding protein acts as an intracellular Ca2+ receptor and transduces Ca2+ transients, usually in response to growth factors. It mediates the activity of a number of Ca2+ regulating enzymes, including protein kinases, phosphatases, nitric oxide synthases, and phosphodiesterase.

Specificity

Recognizes recombinant proteins containing the calmodulin binding protein epitope tag.

Immunogen

KLH-conjugated, synthetic peptide (MKRRWKKNFIAVSAANRFKKISSSGAL) corresponding to the Calmodulin Binding Protein (CBP) epitope tag found in several E. coli expression vectors. The immunizing sequence is identical in rabbit, mouse, and rat.

Application

Anti-Calmodulin Binding Protein Epitope Tag Antibody detects level of Calmodulin Binding Protein Epitope Tag & has been published & validated for use in WB.

Quality

Routinely evaluated by Western Blot in lysates from transformed E. coli.

Western Blot Analysis:
A 1:2000-1:10000 dilution of this lot detected a recombinant protein containing the calmodulin binding protein epitope tag in lysates from transformed E. coli.

Target description

The molecular weight is related to the tagged protein.

Physical form

Purified rabbit IgG in buffer containing 0.1M Tris-Glycine, 0.15M NaCl, 0.05% Sodium Azide, pH7.4.

Analysis Note

Control
Lysates from transformed E. coli.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Legal Information

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

Not finding the right product?  

Try our Product Selector Tool.

Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Thomas Hubert et al.
Traffic (Copenhagen, Denmark), 10(9), 1257-1271 (2009-06-26)
Nucleoporin Nup62 localizes at the central channel of the nuclear pore complex and is essential for nucleocytoplasmic transport. Through its FG-repeat domain, Nup62 regulates nuclear pore permeability and binds nuclear transport receptors. Here, we report that Nup62 interacts directly with
Stephen M T Hoke et al.
Current genetics, 56(5), 447-465 (2010-07-17)
Tra1 is a component of the Saccharomyces cerevisiae SAGA and NuA4 complexes and a member of the PIKK family, which contain a C-terminal phosphatidylinositol 3-kinase-like (PI3K) domain followed by a 35-residue FATC domain. Single residue changes of L3733A and F3744A
Weijun Chen et al.
RNA (New York, N.Y.), 20(3), 308-320 (2014-01-21)
Excision of introns from pre-mRNAs is mediated by the spliceosome, a multi-megadalton complex consisting of U1, U2, U4/U6, and U5 snRNPs plus scores of associated proteins. Spliceosome assembly and disassembly are highly dynamic processes involving multiple stable intermediates. In this
Role of km23-1 in RhoA/actin-based cell migration.
Jin, Q; Pulipati, NR; Zhou, W; Staub, CM; Liotta, LA; Mulder, KM
Biochemical and biophysical research communications null
Physiological importance and identification of novel targets for the N-terminal acetyltransferase NatB.
Caesar, R; Warringer, J; Blomberg, A
Eukaryotic Cell null

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service