Lane 1: Zebrafish tissue lysate
Lane 2: MCF-7 cell lysate
Lane 3: HepG2 cell lysate
Lane 4: A431 cell lysate
Recombinant Rabbit monoclonal primary
PTP1B Recombinant Rabbit Monoclonal Antibody [JJ0935] (ET1701-90)
Synthetic peptide within human ptp1b aa 374-400 / 435.
A431, MCF-7, Hela, HepG2, human tonsil tissue, Zebrafish.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*TBS (pH7.4), 0.05% BSA, 40% Glycerol. Preservative: 0.05% Sodium Azide.
Protein A purified.
PTP1B antibody; Non receptor tyrosine phosphatase 1 antibody; Protein phosphotyrosylphosphatase 1B antibody; Protein tyrosine phosphatase 1B antibody; Protein tyrosine phosphatase non receptor type 1 antibody; Protein tyrosine phosphatase placental antibody; Protein-tyrosine phosphatase 1B antibody; PTN1_HUMAN antibody; PTP 1B antibody; PTP-1B antibody; PTPN 1 antibody; PTPN1 antibody; Tyrosine protein phosphatase non receptor type 1 antibody; Tyrosine-protein phosphatase non-receptor type 1 antibody
Belongs to the protein-tyrosine phosphatase family. Non-receptor class 1 subfamily.
Expressed in keratinocytes (at protein level).
Oxidized on Cys-215; the Cys-SOH formed in response to redox signaling reacts with the alpha-amido of the following residue to form a sulfenamide cross-link, triggering a conformational change that inhibits substrate binding and activity. The active site can be restored by reduction.; Ser-50 is the major site of phosphorylation as compared to Ser-242 and Ser-243. Activated by phosphorylation at Ser-50.; S-nitrosylation of Cys-215 inactivates the enzyme activity.; Sulfhydration at Cys-215 following endoplasmic reticulum stress inactivates the enzyme activity, promoting EIF2AK3/PERK activity.
Endoplasmic reticulum membrane.
The phosphorylation of proteins at tyrosine residues has long been recognized as an important regulatory component of signal transduction. This is a reversible process, involving both enzymes that phosphorylate proteins on tyrosine residues as well as a rapidly expanding family of protein tyrosine phosphatases. These latter enzymes bear little resemblance to either the protein serine and protein threonine phosphatases or to the acid and alkaline phosphatases. In most tissues, the major PTPase is a vanadate- and molybdate-sensitive protein. On the basis of sequence analysis, PTP1B (PTPase 1B) expressed in human placenta exhibits similarities both with the common leukocyte antigen (CD45) and with LAR, a homolog of the neural adhesion molecule (NCAM). PTP1B is synthesized as a 435 amino acid precursor protein which is cleaved to generate the active 321 amino acid enzyme.