DUSP4 is a member of the dual specificity protein phosphatase subfamily.
These phosphatases inactivate their target kinases by dephosphorylating both the phosphoserine/threonine and phosphotyrosine residues.
They negatively regulate members of the mitogen-activated protein (MAP) kinase superfamily (MAPK/ERK, SAPK/JNK, p38), which are associated with cellular proliferation and differentiation.
Different members of the family of dual specificity phosphatases show distinct substrate specificities for various MAP kinases, different tissue distribution and subcellular localization, and different modes of inducibility of their expression by extracellular stimuli.
DUSP4 inactivates ERK1, ERK2 and JNK, is expressed in a variety of tissues, and is localized in the nucleus.
Applications:Suitable for use in ELISA, Western Blot, and Immunohistochemistry.
Other applications not tested.
Recommended Dilutions:Immunohistochemistry: Formalin fixed and paraffin embedded tissuesOptimal dilutions to be determined by the researcher.
Storage and Stability:Store product at 4°C if to be used immediately within two weeks.
For long-term storage, aliquot to avoid repeated freezing and thawing and store at -20°C.
Aliquots are stable at -20°C for 12 months after receipt.
Dilute required amount only prior to immediate use.
Further dilutions can be made in assay buffer.
For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Note: Applications are based on unconjugated antibody.
仕様
Size：200ul
Host：rabbit
Source Antibody：human
Grade：Affinity Purified
Purity：Purified by Protein A/G affinity chromatography.
Form：Supplied as a liquid in PBS, pH 7.2. No preservative added. Labeled with Biotin.
Specificity：Recognizes human DUSP4. Species Crossreactivity: mouse
Isotype：IgG
Calc Applications Abbrev：E IHC WB
Calc Crossreactivity：Hu Mo
Immunogen：KLH-conjugated synthetic peptide mapping to a fragment of residues within amino acids 331-361 in the C-terminal region of human DUSP4, UniProt Accession #Q13115.
