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CUL7/Fbxw8 (show FBXW8 Proteins) ubiquitin ligase-mediated HPK1 degradation revealed a direct link and novel role of CUL7/Fbxw8 (show FBXW8 Proteins) ubiquitin ligase in the MAPK (show MAPK1 Proteins) pathway, which plays a critical role in cell proliferation and differentiation.
HPK1 is critically involved in LFA-1 (show ITGAL Proteins)-mediated polymorphonuclear neutrophils trafficking during acute inflammation.
results indicate that uncleaved HPK1 is a positive regulator of vitamin D-induced differentiation in acute myeloid leukemia (show BCL11A Proteins) cells, but the cleaved HPK1 fragment inhibits differentiation
Pdcd4 (show PDCD4 Proteins) knockdown up-regulates MAP kinase (show MAPK1 Proteins) kinase kinase kinase 1 (MAP4K1) expression and increases phosphorylation of c-Jun (show JUN Proteins).
QVD and 1,25D-induced differentiation was accompanied by increased signaling by Hematopoietic Progenitor Kinase 1(HPK1), and the expression of transcription factors known to be involved in monocytic differentiation was increased.
HPK1 negatively regulates T cell activation by reducing the persistence of signaling microclusters.
The purpose of the study was to investigate the potential contribution of HPK1, MEKK1 (show MAP3K1 Proteins), TAK1 (show MAP3K7 Proteins), p-MKK4 (show MAP2K4 Proteins) to the development of extramammary Paget disease
The catalytic activity of a hematopoietic cell-restricted, Ste20-related S/TPK, HPK1, is positively regulated by exposure to physiological concentrations of PGE2. HPK1 is a negative regulator of PGE2-induced FOS gene transcription.
PP4 (show ANXA5 Proteins) is a positive regulator for HPK1 and the HPK1-JNK (show MAPK8 Proteins) signaling pathway
Full activation of HPK1 is dependent on autophosphorylation of threonine 165 and phosphorylation of serine 171, which is a target site for protein kinase D (PKD) in vitro.
Introduction of three 4-R-hydroxyproline residues stabilizes the SH3m-cortactin (show CTTN Proteins) binding of HPK1 peptide.
a novel negative feedback regulation of BCR (show BCR Proteins) signaling by HPK1-mediated phosphorylation, ubiquitination, and subsequent degradation of the activated BLNK (show BLNK Proteins)
HPK1 associates with SKAP1 (show SKAP1 Proteins) to negatively regulate Rap1 (show TERF2IP Proteins)-mediated B-lymphocyte (show AKAP17A Proteins) adhesion.
HPK1 competes with ADAP for SLP-76 binding and via Rap1 negatively affects T-cell adhesion.
Hpk1 supports apoptosis of T lymphocytes by inhibiting the antiapoptotic action of NF-kappaB (show NFKB1 Proteins) and inducing the proapoptotic activity of JNK (show MAPK8 Proteins).
Mona/Gads (show GRAP2 Proteins) SH3C binding to hematopoietic progenitor kinase 1 (HPK1) combines an atypical SH3 binding motif, R/KXXK, with a classical PXXP motif embedded in a polyproline type II (PPII) helix
suppression or activation of NFkappaB by HPK1 determines sensitivity to activation-induced cell death
HPK1-C as a suppressor of antiapoptotic Bcl-2 (show BCL2 Proteins) proteins and provide a molecular basis for our understanding of CD95L (show FASL Proteins)-independent activation-induced cell death of lymphocytes.
Our data reveal a novel role for HPK1 as a negative regulator of dendritic cell functions
May play a role in the response to environmental stress. Appears to act upstream of the JUN N-terminal pathway. May play a role in hematopoietic lineage decisions and growth regulation.
mitogen-activated protein kinase kinase kinase kinase 1
, MAPK/ERK kinase kinase kinase 1
, MEK kinase kinase 1
, MEKKK 1
, hematopoietic progenitor kinase 1
, mitogen activated protein kinase kinase kinase kinase 1