Recombinant Kallikrein-11, Human 
Datasheet
COA
MSDS
SHIP
Recombinant :
Recombinant Kallikrein-11, Human Source :
SF9 insect cells Molecular Weight :
35.0 kDa, observed by reducing SDS-PAGE. Purity :
> 95% by SDS-PAGE and HPLC analyses. Biological Activity :
KLK-11 specific activity is > 2000 pmole/min/μg when measured by 100uM colormetric peptide substrate (D-Val-Leu-Lys-ThioBenzyl ester). Physical Appearance :
Sterile Filtered White lyophilized (freeze-dried) powder. Formulation :
Lyophilized after extensive dialysis against PBS, pH7.4 AA Sequence :
EFAATMLLVN QSHQGFNKEH TSKMVSAIVL YVLLAAAAHS AFAHHHHHHG SGSDDDDKET RIIKGFECKP HSQPWQAALF EKTRLLCGAT LIAPRWLLTA AHCLKPRYIV HLGQHNLQKE EGCEQTRTAT ESFPHPGFNN SLPNKDHRND IMLVKMASPV SITWAVRPLT LSSRCVTAGT SCLISGWGST SSPQLRLPHT LRCANITIIE HQKCENAYPG NITDTMVCAS VQEGGKDSCQ GDSGGPLVCN QSLQGIISWG QDPCAITRKP GVYTKVCKYV DWIQETMKNN Endotoxin :
< 0.2 EU/μg, determined by LAL method. Reconstitution :
Reconstituted in ddH2O at 100μg/ml. Storage :
Lyophilized recombinant human Kallikrein-11(rhKLK-11) remains stable up to 6 months at -80°C from date of receipt. Upon reconstitution, rhKLK-11 should be stable up to 2 weeks at 4°C or up to 3 months at -20°C. Usage :
This material is offered by USA Bioworld biotech for research, laboratory or further evaluation purposes. For research use only. Description :
Kallikreins are a subgroup of serine proteases having diverse physiological functions. Kallikrein-11 (KLK-11) is possible multifunctional protease.KLK11 efficiently cleaves 'bz-Phe-Arg-4-methylcoumaryl-7-amide', a kallikrein substrate, and weakly cleaves other substrates for kallikrein and trypsin. Kallikreins are a subgroup of serine proteases having diverse physiological functions. Growing evidence suggests that many kallikreins are implicated in carcinogenesis and some have potential as novel cancer and other disease biomarkers.Recombinant human Kallikrein-11(rhKLK-11) secreted in Sf9 insect cells is a single glycosylated polypeptide chain containing 232 amino acids. A fully biologically active molecule, rhKallikrein-11 has a molecular mass of 35.0 kDa analyzed by reducing SDS-PAGE and is obtained by proprietary chromatographic techniques at GenScript.
Recombinant Kallikrein-11, Human Source :
SF9 insect cells Molecular Weight :
35.0 kDa, observed by reducing SDS-PAGE. Purity :
> 95% by SDS-PAGE and HPLC analyses. Biological Activity :
KLK-11 specific activity is > 2000 pmole/min/μg when measured by 100uM colormetric peptide substrate (D-Val-Leu-Lys-ThioBenzyl ester). Physical Appearance :
Sterile Filtered White lyophilized (freeze-dried) powder. Formulation :
Lyophilized after extensive dialysis against PBS, pH7.4 AA Sequence :
EFAATMLLVN QSHQGFNKEH TSKMVSAIVL YVLLAAAAHS AFAHHHHHHG SGSDDDDKET RIIKGFECKP HSQPWQAALF EKTRLLCGAT LIAPRWLLTA AHCLKPRYIV HLGQHNLQKE EGCEQTRTAT ESFPHPGFNN SLPNKDHRND IMLVKMASPV SITWAVRPLT LSSRCVTAGT SCLISGWGST SSPQLRLPHT LRCANITIIE HQKCENAYPG NITDTMVCAS VQEGGKDSCQ GDSGGPLVCN QSLQGIISWG QDPCAITRKP GVYTKVCKYV DWIQETMKNN Endotoxin :
< 0.2 EU/μg, determined by LAL method. Reconstitution :
Reconstituted in ddH2O at 100μg/ml. Storage :
Lyophilized recombinant human Kallikrein-11(rhKLK-11) remains stable up to 6 months at -80°C from date of receipt. Upon reconstitution, rhKLK-11 should be stable up to 2 weeks at 4°C or up to 3 months at -20°C. Usage :
This material is offered by USA Bioworld biotech for research, laboratory or further evaluation purposes. For research use only. Description :
Kallikreins are a subgroup of serine proteases having diverse physiological functions. Kallikrein-11 (KLK-11) is possible multifunctional protease.KLK11 efficiently cleaves 'bz-Phe-Arg-4-methylcoumaryl-7-amide', a kallikrein substrate, and weakly cleaves other substrates for kallikrein and trypsin. Kallikreins are a subgroup of serine proteases having diverse physiological functions. Growing evidence suggests that many kallikreins are implicated in carcinogenesis and some have potential as novel cancer and other disease biomarkers.Recombinant human Kallikrein-11(rhKLK-11) secreted in Sf9 insect cells is a single glycosylated polypeptide chain containing 232 amino acids. A fully biologically active molecule, rhKallikrein-11 has a molecular mass of 35.0 kDa analyzed by reducing SDS-PAGE and is obtained by proprietary chromatographic techniques at GenScript.
Blocking peptide available as BK0356-10μgP