Recombinant Mouse Granzyme A Protein (His tag)

Beta LifeScience SKU/CAT #: BLA-9873P

Recombinant Mouse Granzyme A Protein (His tag)

Beta LifeScience SKU/CAT #: BLA-9873P
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Product Overview

Host Species Mouse
Accession P11032
Synonym CTL tryptase CTLA3 Cytolytic t cell and natural killer cell specific trypsin like serine protease Cytotoxic T lymphocyte associated serine esterase 3 Cytotoxic T lymphocyte proteinase 1 Cytotoxic T-lymphocyte proteinase 1 Fragmentin 1 Fragmentin-1 GRAA_HUMAN Granzyme 1 cytotoxic T lymphocyte associated serine esterase 3 Granzyme A Granzyme A (Cytotoxic T lymphocyte associated serine esterase 3; Hanukah factor serine protease) Granzyme A (granzyme 1, cytotoxic T lymphocyte associated serine esterase 3) Granzyme A precursor Granzyme-1 GZMA H factor Hanukah factor serine protease Hanukkah factor HF HFSP TSP1
Description Recombinant Mouse Granzyme A Protein (His tag) was expressed in E.coli. It is a Full length protein
Source E.coli
Molecular Weight 40 kDa including tags
Purity >90% SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Liquid Solution
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.

Target Details

Target 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. It cleaves after Lys or Arg. Cleaves APEX1 after 'Lys-31' and destroys its oxidative repair activity. 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.
Subcellular Location Secreted. Cytoplasmic granule.
Protein Families Peptidase S1 family, Granzyme subfamily
Database References
Tissue Specificity Found in cytotoxic lymphocytes and in normal lymphoid tissues such as thymus and spleen.; [Isoform HF1]: More abundant in lymphoid tissues than isoform HF2.

Gene Functions References

  1. GzmA and gzmB were predominantly expressed by natural killer cells, and during abdominal sepsis, the percentage of these cells expressing gzms in peritoneal lavage fluid decreased, while the amount of expression in the gzm(+) cells increased PMID: 28694562
  2. a novel endogenous trigger for autoimmune diabetes and an in vivo role for granzyme A in maintaining immune tolerance. PMID: 28733313
  3. this study shows that gzmA and gzmB partly regulate local inflammation during early pneumonia but eventually play an insignificant role during pneumosepsis by the common human pathogen Klebsiella pneumoniae PMID: 26894590
  4. Granzyme A does not have a crucial role in vivo in the protective response to tuberculosis. PMID: 27055232
  5. Data indicate N-terminomics on the human and mouse granzymes A and K by combined fractional diagonal chromatography (COFRADIC). PMID: 25383893
  6. The results, in susceptible B6 mice for GzmB and in resistant 129/Sv mice for GzmA and/or the GzmB cluster, point to granzyme-mediated host defense regulation in the liver in experimental visceral leishmaniasis. PMID: 25452549
  7. Estrogen increases the extracellular expression and interleukin (IL)-12-induced activity of a critical member of serine protease family granzyme A. PMID: 24840346
  8. functional divergence between human and mouse granzyme A PMID: 24505135
  9. We have demonstrated that cell death can be induced when mGzmA is delivered by primary natural killer cells via authentic Cytotoxic lymphocyte/target cell interactions. PMID: 23744295
  10. Regulated secretion of granzyme A and cytotoxic killing was enhanced and correlated with increased vesicle-associated membrane protein 7 availability. PMID: 23084031
  11. GzmA deficiency in filarial infection is linked with reduced inflammation and a trend toward increased alternatively activated macrophages. PMID: 21248253
  12. granzyme A- and B-cluster deficiency delays the acute progression of pneumovirus disease by reducing alveolar injury. PMID: 20018616
  13. the genes for perforin, the three major T cell granzymes (A-C) and IFN-gamma are differentially expressed during primary activation of naive CD8(+) T cells, kinetically and at the single-cell level PMID: 12039912
  14. granzyme A and granzyme B have a similar potential to induce rapid perf-mediated apoptosis but that their individual contribution to the underlying intracellular process is dictated by the quality of the target cell PMID: 12115618
  15. NK cell mediated tumor control is dependent on granzymes. PMID: 12355441
  16. some cytolytic T lymphocytes mature into perforin/granzyme-expressing effector cells in the mediastinal lymph node and are detectable when they accumulate in lung infection PMID: 12601154
  17. In all tumor models examined thus far, granzyme A is not necessary for tumor rejection mediated by the perforin pathway in vivo. PMID: 12847210
  18. gzmA and gzmB induce multiple independent cell death pathways; all gzm-induced apoptotic features analyzed depend critically on perf. PMID: 15534000
  19. polymorphonuclear leukocytes from mice and humans lack the 3 cytotoxic effector molecules, gzmA, granzyme B, and perforin, generally associated with natural killer and cytotoxic T lymphocytes PMID: 15998831
  20. IL-2 increased the expression of perforin and granzyme A, B, and C mRNA; induction of granzyme A, B, and C mRNA required exogenous IL-2, whereas induction of perforin and IFN-gamma expression did not. PMID: 16339537
  21. CTLs from granzyme AB(-/-) mice induce target cell death by a unique mechanism that is distinct from both perforin lysis and apoptosis. PMID: 16606695
  22. Mouse granzyme B is 30 times less cytotoxic than human granzyme B and does not require Bid for killing but regains cytotoxicity on engineering of its active site cleft. Mouse granzyme A is considerably more cytotoxic than human granzyme A. PMID: 17116752
  23. Skin-, but not lung-associated primary mast cells as well as in vitro-differentiated bone marrow-derived mast cells (BMMC) express granzyme (gzm) B, but not gzmA or perforin (perf). PMID: 17599099
  24. GzmA accesses the mitochondrial matrix to cleave the complex I protein NDUFS3, an iron-sulfur subunit of the NADH:ubiquinone oxidoreductase complex I. PMID: 18485875
  25. grzK plays an important role in CD8(+) T-cell cytotoxicity both in the presence and absence of grzA and B. PMID: 18788942
  26. the granule secretory pathway plays an unexpected role in inflammation, with GzmA acting as an endogenous modulator. PMID: 18951048
  27. Neither gzmA nor gzmB is required for rapid and efficient in vivo cytotoxicity by cytotoxic T (Tc) cells. PMID: 19525394


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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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