Product Description
Size: 100µg
Mouse Monoclonal Granzyme K antibody. Carrier free. Suitable for Flow Cyt (Intra), ELISA and reacts with Transfected cell line, Human samples. Cited in 4 publications.
Key facts
Host species:Mouse,
Clonality:Monoclonal,
Clone number:GM-24C3,
Isotype:IgG2b,
Carrier free:Yes,
Applications:ELISA, Flow Cyt (Intra)See reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:The exact immunogen used to generate this antibody is proprietary information.,
Specificity:This antibody recognises Granzyme K transiently expressed on the cell surface of transfected BOSC cells as well as the native protein in peripheral blood mononuclear cells. It does not cross react with Granzyme A. Specificity is routinely tested by flow cytometry on BOSC cells transiently transfected with a Granzyme K expression vector.
Product details:
Granzymes are exogenous serine proteases that are stored in the cytotoxic granules of activated T cells and NK cells. Upon target cell contact, the contents of these granules are directionally exocytosed and, with the assistance of perforin, the granzymes enter the cytosol of the target cell. To date, five human granzymes (A, B, H, K,M) have been described at the molecular genetic level. Human granzyme K (GZMK) is a 28 kD aserine protease whose gene is located on chromosome 5q11-12 close to the granzyme A-encoding gene. Like granzyme A, it has a trypsin-like specifity cleaving at the basic residues arginine and lysine. To which extent human granzyme K plays a role in the induction of apoptosis in the target cells remains to be evaluated. However, granzyme K purified from a rat large granular lymphoma cell line (RNK-16)has been shown to induce apoptosis in vitro. High mRNA levels of granzyme K are detected inactivated T cells and NK cells but are absent in normal tissues that do not contain high numbers of these cells. Antibodies produced from cDNA: Conventional technologies usually either generate antibodies against purified proteins, or against synthetic peptides based on amino acid sequences derived from DNA sequence data. Genetic immunization involves introducing the gene in the form of a cDNA directly into an animal which translates this cDNA into protein thus stimulating an immune response against the foreign protein. Although the synthetic peptide approach is comparable in speed, the quality of antibodies generated by genetic immunization is far superior. This is because the protein is made by the immunized animal, utilzing complex cellular mechanisms that allow it to gain a native conformation. Antibodies are then generated against a native protein, such as is found in the blood or tissues of its host species. Membrane-bound or secreted proteins often create problems for conventional antibody technology because in their native form, they are often modified by glycosylation, or in some cases exist as multiple membrane-spanning proteins that are not soluble following isolation or synthesis in recombinant systems. All of these problems are avoided if the immunized animal makes the protein itself. Antibodies generated by genetic immunization have been shown to have binding affinities to the protein in the sub-nanomolar range, which are approximately 100x higher than conventionally developed antibodies and much higher than single chain antibodies. Results confirm published data for much higher avidity of sera generated by genetic immunization as compared with that gained by immunization with a corresponding recombinant protein.
Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein G, Storage buffer-pH: 7.2Constituents: PBS, Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Granzyme K also known as protein K or 24c3 is a serine protease with a mass of approximately 27 kilodaltons. It belongs to the granzyme family of proteins which are mainly found within the cytotoxic granules of natural killer (NK) cells and cytotoxic T lymphocytes (CTLs). These immune cells store granzyme K in their granules which they release to induce apoptosis in target cells. Researchers have identified granzyme K expression in various tissues and immune cells highlighting its widespread role in modulating immune responses.
Biological function summary
Granzyme K serves as a potent mediator in the immune system by inducing apoptosis in target cells. It does not act alone but rather in concert with other granzymes and proteins to effectively execute cell death. Granzyme K can degrade cellular proteins once introduced into a target cell's cytoplasm leading to apoptosis. The protease functions independently and does not require a complex for its activity contributing to the immune system's ability to eliminate infected or transformed cells.
Pathways
The granzyme K protein exists within essential immune regulatory pathways such as the cytotoxic T lymphocyte-induced apoptosis pathway and the natural killer cell-mediated cytotoxicity pathway. Granzyme K acts alongside granzymes A and B to promote programmed cell death and finely tune host immune responses. While granzymes A and B have more defined roles granzyme K complements their activity offering redundancy and ensuring efficient elimination of harmful target cells.
Granzyme K shows significant connections to inflammatory conditions and autoimmune diseases such as rheumatoid arthritis. Elevated granzyme K levels in these diseases may result from dysregulated immune responses leading to excessive tissue damage. In autoimmune disorders granzyme K works in combination with proteins like perforin which facilitates entry of granzymes into the cell to stimulate apoptosis. Understanding granzyme K's role in these conditions may help develop therapeutic approaches to modulate immune activity and minimize tissue damage.
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Collaboration
Tony Tang
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