P8984
Monoclonal Anti-Protein Tyrosine Phosphatase μ antibody produced in mouse
clone SBK10, purified immunoglobulin, buffered aqueous solution
Synonym(s):
Anti-PTPμ
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About This Item
Conjugate:
unconjugated
Clone:
SBK10, monoclonal
Application:
IP, WB CL
Citations:
6
biological source
mouse
conjugate
unconjugated
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
SBK10, monoclonal
form
buffered aqueous solution
mol wt
antigen 200 kDa
species reactivity
rat, mouse, human, bovine
technique(s)
immunoprecipitation (IP): suitable, western blot (chemiluminescent): 1-10 μg/mL
isotype
IgG1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... PTPRM(5797)
mouse ... Ptprm(19274)
rat ... Ptprm(29616)
General description
Among the post-translational modifications, phosphorylation is a vital regulatory mechanism of key proteins involved in specific pathways. Reverse phosphorylation has become recognized as the key process of regulation of gene expression, cellular proliferation, differentiation in Eukaryotes. The protein phosphatases can be divided into two main groups: protein tyrosine phosphatases (PTPs) and protein serine/threonine phosphatases (PPs) which remove phosphate from proteins/peptides containing phosphotyrosine (pTyr) or phosphoserine/phosphothreonine (pSer/pThr), respectively. Several of the PTPs are known to control the function of growth factor receptors, many of which are tyrosine kinases encoded by oncogenes. PTPmu participates in homophilic binding of extracellular surface of adjacent cells. PTPmu is reported to be downregulated in glioblastoma in which it regulates cell migration and growth factor-independent survival
Monoclonal Anti-Protein Tyrosine Phosphatase mu recognizes PTPmu isoforms in all mammalian species.
Monoclonal Anti-Protein Tyrosine Phosphatase mu recognizes PTPmu isoforms in all mammalian species.
Immunogen
peptide corresponding to amino acid residues 42-60 of PTPμ.
Application
Anti-protein tyrosine phosphatase mu may be used for detection by immunoblotting at a working concentration of 1 to 10 μg/mL. The antibody is suitable for immunoprecipitation.
Physical form
Solution in phosphate buffered saline with 0.08% sodium azide.
Preparation Note
Purified from tissue culture supernatant using Protein G.
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Storage Class
10 - Combustible liquids
Regulatory Information
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M F Gebbink et al.
The Journal of biological chemistry, 268(22), 16101-16104 (1993-08-05)
Receptor-like protein tyrosine phosphatases (receptor-PTPs) represent a novel family of transmembrane proteins that are thought to play important roles in cellular regulation. They consist of a cytoplasmic catalytic region, a single transmembrane segment and an extracellular, putative ligand-binding domain, but
A Gjörloff-Wingren et al.
European journal of immunology, 30(8), 2412-2421 (2000-08-15)
A high protein tyrosine phosphatase (PTPase) activity is required to maintain circulating T lymphocytes in a resting phenotype, and to limit the initiation of T cell activation. We report that 15 of the currently known 24 intracellular PTPases are expressed
S M Brady-Kalnay et al.
The Journal of biological chemistry, 269(45), 28472-28477 (1994-11-11)
The receptor-type protein tyrosine phosphatase PTP mu comprises an extracellular segment containing a MAM domain, an immunoglobulin domain and four fibronectin type III repeats, a transmembrane segment, and two intracellular PTP domains. We have previously shown that PTP mu binds
Adam M Burgoyne et al.
Neuro-oncology, 11(6), 767-778 (2009-03-24)
The cell-surface receptor protein tyrosine phosphatase mu (PTPmu) is a homophilic cell adhesion molecule expressed in CNS neurons and glia. Glioblastomas (GBMs) are the highest grade of primary brain tumors with astrocytic similarity and are characterized by marked dispersal of
Adam M Burgoyne et al.
Cancer research, 69(17), 6960-6968 (2009-08-20)
Glioblastoma multiforme (GBM), the most common malignant primary brain tumor, represents a significant disease burden. GBM tumor cells disperse extensively throughout the brain parenchyma, and the need for tumor-specific drug targets and pharmacologic agents to inhibit cell migration and dispersal
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