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钙调蛋白1(CALM1)重组蛋白The target protein is fused with a His-tag and its sequence is listed below. The first Met is an initiator amino acid. Moreover, Gly and Ser are added to improve the flexibility of N-terminus at both ends of the His-tag, which will increas
YB93315Ra01
Calmodulin 1 (CALM1)
Organism: Rattus norvegicus (Rat)
Instruction manual
FOR IN VITRO USE AND RESEARCH USE ONLY
NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES
3th Edition (Revised in February, 2012)
[ DESCRIPTION ]
Protein Names: Calmodulin 1
Gene Names: CALM1
Size: 100µg
Source: Recombinant
Expression Host: E.coli
Function: Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca2+, AND MASS SPECTROMETRY. Among the enzymes to be stimulated by the calmodulin-Ca2+ complex are a number of protein kinases and phosphatases.
Subcellular Location: Cytoplasm; cytoskeleton; spindle.
[ PROPERTIES ]
Residues: Met1~Lys149 (Accession # P62161), with a N-terminal His-tag.
Grade & Purity: >97%, 18.08 kDa as determined by SDS-PAGE reducing conditions.
Form & Buffer: Supplied as lyophilized form in PBS, pH 7.4.
Endotoxin Level: <1.0 EU per 1μg (determined by the LAL method).
Applications: SDS-PAGE; WB; ELISA; IP.
(May be suitable for use in other assays to be determined by the end user.)
Predicted Molecular Mass: 18.08 kDa
[ PREPARATION ]
Reconstitute in PBS.
[ STORAGE AND STABILITY ]
Storage: Store at 4oC for short time storage (1-2 weeks). Aliquot and store at -20oC or -80oC for long term storage. Avoid repeated freeze/thaw cycles.
Valid period: 12 months stored at -80oC.
[ BACKGROUND]
The target protein is fused with a His-tag and its sequence is listed below. The first Met is an initiator amino acid. Moreover, Gly and Ser are added to improve the flexibility of N-terminus at both ends of the His-tag, which will increase the chelating ability of the tag to Ni-Sepharose during purification.
MGHHHHHHSGS-MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE
EVDEMIREAD IDGDGQVNYE EFVQMMTAK
[ REFERENCES ]
1.Giaccone G., et al. (2005) Ann Onc. 16: 538-48.
2.Schlessinger J., et al. (2000) Cell. 103: 211-25.
3.Yarden Y., et al. (2001) Nat Rev Mol Cell Biol. 2: 127-37.
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