MEK5 Antibody

Product Specifications

Background

A family of protein kinases located upstream of the MAP kinases andresponsible for their activation has been identified. The prototype member ofthis family, designated MAP kinase kinase, or MEK-1, specifically phospho-rylates the MAP kinase regulatory threonine and tyrosine residues present inthe Thr-Glu-Tyr motif of ERK. A second MEK family member, MEK-2, resem-bles MEK-1 in its substrate specificity. MEK-3 (or MKK-3) functions to acti-vate p38 MAP kinase, and MEK-4 (also called SEK1 or MKK-4) activatesboth p38 and JNK MAP kinases. MEK-5 appears to specifically phosphory-late ERK5, whereas MEK-6 phosphorylates p38 and p38b. MEK-7 (or MKK-7) phosphorylates and activates the JNK signal transduction pathway.

NCBI Gene ID

29568

Swiss Prot

Q62862

Accession Number

NP_001029159.1

Host

Rabbit

Reactivity

Human, Mouse, Rat

Immunogen

MEK5 antibody was raised against a peptide sequence around aa. 311-315 (K-T-Y-V-G) derived from Rat MEK5.

Clonality

Polyclonal

Conjugation

Unconjugated

Type

Primary Antibodies

Field of Research

Other

Purification

Antibodies were purified by affinity-chromatography using epitope-specific peptide

Concentration

1 mg/mL

Buffer

Antibody supplied in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.

Modification

None

Shipping Conditions

Blue Ice

Storage Conditions

Store antibody at -20˚ C for up to one year.

Calculated Molecular Weight

49 kDa

Specificity

This antibody detects endogenous level of total MEK5 protein.

Applications Notes

Western Blot: 1:500

Symbol

Map2k5

NCBI Official Name

Mitogen activated protein kinase kinase 5

NCBI Organism

This antibody was raised against a peptide sequence around aa. 311-315 (K-T-Y-V-G) derived from Rat MEK5.

Background Reference 01

Han, J., et al. 1996. J. Biol. Chem. 271: 2886-2891. Jiang, Y., et al. 1996. J. Biol. Chem. 271: 17920-17926. Tournier, C., et al. 1997. Proc. Natl. Acad. Sci. USA94: 7337-7442. Holland, P. M., et al. 1997. J. Biol. Chem. 272: 24994-24998.