Anti-Granzyme A / GZMA

0.5mg/ml if reconstituted with 0.2ml sterile DI water. GRB7, growth factor receptor-bound protein 7, is a protein which in humans is encoded by the GRB7 gene. The product of this gene belongs to a small family of adaptor proteins that are known to interact with a number of receptor tyrosine kinases and signaling molecules. This gene encodes a growth factor receptor-binding protein that interacts with epidermal growth factor receptor(EGFR) and ephrin receptors. The protein plays a role in the integrin signaling pathway and cell migration by binding with focal adhesion kinase(FAK). Alternative splicing results in multiple transcript variants encoding different isoforms, although the full-length natures of only two of the variants have been determined to date. GRB7 is an SH2-domain adaptor protein that binds to receptor tyrosine kinases and provides the intra-cellular direct link to the Ras proto-oncogene. Human GRB7 is located on the long arm of chromosome 17, next to the ERBB2(alias HER2/neu) proto-oncogene. These two genes are commonly co-amplified(present in excess copies) in breast cancers. GRB7 though to be involved in migration, is well known to be over-expressed in testicular germ cell tumors, esophageal cancers, and gastric cancers. Protein function: Abundant protease in the cytosolic granules of cytotoxic T- cells and NK-cells which activates caspase-independent pyroptosis when delivered into the target cell through the immunological synapse (PubMed:3257574, PubMed:3262682, PubMed:3263427, PubMed:32299851, PubMed:12819770). It cleaves after Lys or Arg (PubMed:32299851, PubMed:12819770). Once delivered into the target cell, acts by catalyzing cleavage of gasdermin-B (GSDMB), releasing the pore-forming moiety of GSDMB, thereby triggering pyroptosis and target cell death (PubMed:32299851). Cleaves APEX1 after 'Lys-31' and destroys its oxidative repair activity (PubMed:12524539). Cleaves the nucleosome assembly protein SET after 'Lys-189', which disrupts its nucleosome assembly activity and allows the SET complex to translocate into the nucleus to nick and degrade the DNA (PubMed:11555662, PubMed:12628186, PubMed:16818237). [The UniProt Consortium]