Active Recombinant Human CASP3, Met&His-tagged
Cat.No. : | CASP3-192H |
Product Overview : | Recombinant Human CASP3 (Accession # AAA65015) Met1-His277, fused with an N-terminal Met and 6-His tag, was produced in E. coli-derived. |
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Source : | E. coli |
Species : | Human |
Tag : | His |
Predicted N Terminal : | Not tested: Met predicted. |
Form : | Lyophilized from a 0.2 µm filtered solution in Tris, NaCl, Sucrose and DTT. |
Bio-activity : | The activity of the activated Caspase-3 was measured by its ability to cleave DEVD-AFC. The specific activity is >500 pmol/min/µg, as measured under the described conditions. |
Molecular Mass : | Recombinant Human CASP3, Met&His-tagged has a calculated MW of 33 kDa. In SDS-PAGE migrates as 35 kDa, reducing conditions. |
Purity : | >90%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Storage : | Avoid repeated freeze-thaw cycles. No activity loss was observed after storage at: In lyophilized state for 1 year (4ºC); After reconstitution under sterile conditions for 3 months (-70ºC). |
Protein length : | Met1-His277 |
Gene Name : | CASP3 caspase 3, apoptosis-related cysteine peptidase [ Homo sapiens ] |
Official Symbol : | CASP3 |
Synonyms : | CASP3; caspase 3, apoptosis-related cysteine peptidase; caspase 3, apoptosis related cysteine protease; caspase-3; apopain; CPP32; CPP32B; Yama; CASP-3; CPP-32; procaspase3; protein Yama; PARP cleavage protease; cysteine protease CPP32; SREBP cleavage activity 1; caspase 3, apoptosis-related cysteine protease; SCA-1; |
Gene ID : | 836 |
mRNA Refseq : | NM_004346 |
Protein Refseq : | NP_004337 |
MIM : | 600636 |
UniProt ID : | P42574 |
Chromosome Location : | 4q34 |
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◆ Lysates | ||
CASP3-7839HCL | Recombinant Human CASP3 293 Cell Lysate | +Inquiry |
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For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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03/29/2024
Casp3-748R, the rat caspase3 worked/is working very well for us.
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