DATASHEET
Host:
Rabbit
Target Protein:
INPPL1 Tyr1135
Modification Site:
Tyr1135
Clonality:
Polyclonal
Isotype:
IgG
Entrez Gene:
3636
Source:
KLH conjugated synthetic phosphopeptide derived from human SHIP2 around the phosphorylation site of Tyr1135
Purification:
Purified by Protein A.
Storage Buffer:
0.01M TBS(pH7.4) with 1% BSA, 0.02% Proclin300 and 50% Glycerol.
Storage:
Shipped at 4°C. Store at -20°C for one year. Avoid repeated freeze/thaw cycles.
Background:
The steady state of protein tyrosyl phosphorylation in cells is regulated by the opposing action of tyrosine kinases and protein tyrosine phosphatases (PTPs). Several groups have independently identified a non transmembrane PTP, designated SHPTP1 (also known as PTP1C, HCP and SHP), which is primarily expressed in hematopoietic cells and characterized by the presence of two SH2 domains N terminal to the PTP domain. A second and much more widely expressed PTP with SH2 domains, SHPTP2 (also designated PTP1D and Syp), has been identified. SHP2 is a protein tyrosine phosphatase that is widely expressed and plays a regulatory role in various cell signaling events that are important for many cell functions, such as mitogenic activation, metabolic control, transcription regulation, and cell migration.
VALIDATION IMAGES
Paraformaldehyde-fixed, paraffin embedded mouse brain; Antigen retrieval by boiling in sodium citrate buffer (pH6) for 15min; Block endogenous peroxidase by 3% hydrogen peroxide for 30 minutes; Blocking buffer (normal goat serum) at 37°C for 20min; Antibody incubation with INPPL1(Tyr1135) Polyclonal Antibody (bs-3399R) at 1:400 overnight at 4°C, followed by a conjugated secondary and DAB staining.
Paraformaldehyde-fixed, paraffin embedded human glioma; Antigen retrieval by boiling in sodium citrate buffer (pH6) for 15min; Block endogenous peroxidase by 3% hydrogen peroxide for 30 minutes; Blocking buffer (normal goat serum) at 37°C for 20min; Antibody incubation with INPPL1(Tyr1135) Polyclonal Antibody (bs-3399R) at 1:400 overnight at 4°C, followed by a conjugated secondary and DAB staining.