Human Granzyme H protein (Recombinant) (His-Tag) (STJP019125)

SPECIFICATIONS
HostE.coli
ImmunogenHuman
STJP019125
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General Information

Short DescriptionRecombinant-Human Granzyme H-His-Tag protein was developed from e.coli and has a target region of His-Tag. For use in research applications.
ApplicationsSDS-PAGE/Denatured
HostE.coli
NoteSTRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.

Product Properties

Concentration0.25 mg/mL
FormulationLiquid in 20mM Tris-HCl buffer (pH 8.0) containing 10% Glycerol
Storage InstructionFor short term storage, keep at +2C to +8C for up to 1 week. For long term storage, aliquot and store at-20C, and avoid repeat freeze-thaw cycles.

Target Information

Gene SymbolGZMH
Gene ID2999
Uniprot IDGRAH_HUMAN
Accession NumberNP_219491
ImmunogenHuman
Immunogen Region20-246aa
Immunogen SequenceMGSSHHHHHH SSGLVPRGSH MEIIGGHEAK PHSRPYMAFV QFLQEKSRKR CGGILVRKDF VLTAAHCQGS SINVTLGAHN IKEQERTQQF IPVKRPIPHP AYNPKNFSND IMLLQLERKA KWTTAVRPLR LPSSKAQVKP GQLCSVAGWG YVSMSTLATT LQEVLLTVQK DCQCERLFHG NYSRATEICV GDPKKTQTGF KGDSGGPLVC KDVAQGILSY GNKKGTPP

Additional Info

Tissue Specificity Constitutively expressed in NK cells.
Function Cytotoxic chymotrypsin-like serine protease with preference for bulky and aromatic residues at the P1 position and acidic residues at the P3' and P4' sites. Probably necessary for target cell lysis in cell-mediated immune responses. Participates in the antiviral response via direct cleavage of several proteins essential for viral replication.
Protein Name Granzyme H
Ccp-X
Cathepsin G-Like 2
Ctsgl2
Cytotoxic T-Lymphocyte Proteinase
Cytotoxic Serine Protease C
Csp-C
Database Links Reactome: R-HSA-2022377
Reactome: R-HSA-381426
Cellular Localisation Cytolytic Granule
Alternative Protein Names Granzyme H protein
Ccp-X protein
Cathepsin G-Like 2 protein
Ctsgl2 protein
Cytotoxic T-Lymphocyte Proteinase protein
Cytotoxic Serine Protease C protein
Csp-C protein
GZMH protein
CGL2 protein
CTSGL2 protein

Information sourced from Uniprot.org

Citations

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