This protein protein interaction antibody pair set comes with two antibodies to detect the protein-protein interaction, one against the HSPA1L protein, and the other against the MAP3K1 protein for use in in situ Proximity Ligation Assay. See Publication Reference below.
Reactivity:
Human
Quality Control Testing:
Protein protein interaction immunofluorescence result.
Representative image of Proximity Ligation Assay of protein-protein interactions between HSPA1L and MAP3K1. HeLa cells were stained with anti-HSPA1L rabbit purified polyclonal antibody 1:1200 and anti-MAP3K1 mouse monoclonal antibody 1:50. Each red dot represents the detection of protein-protein interaction complex. The images were analyzed using an optimized freeware (BlobFinder) download from The Centre for Image Analysis at Uppsala University.
Supplied Product:
Antibody pair set content: 1. HSPA1L rabbit purified polyclonal antibody (100 ug) 2. MAP3K1 mouse monoclonal antibody (40 ug) *Reagents are sufficient for at least 30-50 assays using recommended protocols.
Storage Instruction:
Store reagents of the antibody pair set at -20°C or lower. Please aliquot to avoid repeated freeze thaw cycle. Reagents should be returned to -20°C storage immediately after use.
This gene encodes a 70kDa heat shock protein. In conjunction with other heat shock proteins, this protein stabilizes existing proteins against aggregation and mediates the folding of newly translated proteins in the cytosol and in organelles. The gene is located in the major histocompatibility complex class III region, in a cluster with two closely related genes which also encode isoforms of the 70kDa heat shock protein. [provided by RefSeq
Other Designations:
OTTHUMP00000029295,heat shock 10kDa protein 1-like,heat shock 70kD protein-like 1
MAP3K, or MEK kinase, is a serine/threonine kinase that occupies a pivotal role in a network of phosphorylating enzymes integrating cellular responses to a number of mitogenic and metabolic stimuli, including insulin (MIM 176730) and many growth factors.[supplied by OMIM