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Recombinant Human Cystatin F Protein

Features and benefitsView More
  • Expression System: HEK293
  • Accession #: O76096
  • Protein Tag: C-His
  • Bioactivity: Measured by its ability to inhibit active Cathepsin L cleavage of a fluorogenic peptide substrate Z-LR-AMC. The IC50 value is <6.0 nM, as measured under the described conditions.
  • Endotoxin Concentration: <0.1 EU/μg
Item Number
rp144941
Grouped product items
SKUSizeAvailabilityPrice Qty
rp144941-10μg
10μg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$139.90
rp144941-50μg
50μg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$419.90
rp144941-100μg
100μg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$669.90
rp144941-1mg
1mg
Available within 8-12 weeks(?)
Production requires sourcing of materials. We appreciate your patience and understanding.
$4,899.90

Animal Free, ≥95% (SDS-PAGE), Active, 293F, C-His tag, 20-145 aa

Basic Description

Product NameRecombinant Human Cystatin F Protein
SynonymsCMAP | Cystatin-7 | Cystatin-like metastasis-associated protein | Leukocystatin | CMAP | CST7 | Cystatin 7 | cystatin F (leukocystatin) | Cystatin F | Cystatin-7 | cystatin-F | Cystatin-like metastasis-associated protein | Leukocystatin | CST7 | CMAP | Cy
GradeActiBioPure™, Animal Free, Bioactive, Carrier Free
Product Description

Function
Inhibits papain and cathepsin L but with affinities lower than other cystatins. May play a role in immune regulation through inhibition of a unique target in the hematopoietic system.

Specifications & PurityAnimal Free, Carrier Free, Bioactive, ActiBioPure™, ≥95%(SDS-PAGE)
BioactivityMeasured by its ability to inhibit active Cathepsin L cleavage of a fluorogenic peptide substrate Z-LR-AMC. The IC50 value is <6.0 nM, as measured under the described conditions.
Endotoxin Concentration<0.1 EU/μg
Expression SystemHEK293
SpeciesHuman
Amino Acids20-145 aa
SequenceGPSPDTCSQDLNSRVKPGFPKTIKTNDPGVLQAARYSVEKFNNCTNDMFLFKESRITRALVQIVKGLKYMLEVEIGRTTCKKNQHLRLDDCDFQTNHTLKQTLSCYSEVWVVPWLQHFEVPVLRCHHHHHHH
Protein TagC-His
Accession #O76096
Predicted molecular weight15 kDa
SDS-PAGE16&21&26 kDa, under reducing conditions

Product Specifications

FormLyophilized
ReconstitutionReconstitute in sterile water to a concentration of 0.1-0.5 mg/ml.
Storage TempStore at -20°C,Avoid repeated freezing and thawing
Shipped InIce chest + Ice pads
Stability And StorageStore at -20~-80℃ for more than 1 year. Upon delivery aliquot. Avoid freeze/thaw cycle.

Certificates

Certificate of Analysis(COA)

Enter Lot Number to search for COA:

Related Documents

References

1. Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J.  (2001)  The DNA sequence and comparative analysis of human chromosome 20..  Nature,  414  (6866): (865-71).  [PMID:11780052] [10.1021/op500134e]
2. Halfon, S S and 17 more authors..  (1998)  Leukocystatin, a new Class II cystatin expressed selectively by hematopoietic cells..  The Journal of biological chemistry,    (26):   [PMID:9632704]
3. Ni, J J and 8 more authors..  (1998)  Cystatin F is a glycosylated human low molecular weight cysteine proteinase inhibitor..  The Journal of biological chemistry,    (18):   [PMID:9733783]
4. Morita, M M, Hara, Y Y, Tamai, Y Y, Arakawa, H H and Nishimura, S S..  (2000)  Genomic construct and mapping of the gene for CMAP (leukocystatin/cystatin F, CST7) and identification of a proximal novel gene, BSCv (C20orf3)..  Genomics,    (1):   [PMID:10945474]
5. Nathanson, Carl-Michael CM, Wassélius, Johan J, Wallin, Hanna H and Abrahamson, Magnus M..  (2002)  Regulated expression and intracellular localization of cystatin F in human U937 cells..  European journal of biochemistry,      [PMID:12423348]
6. Schüttelkopf, Alexander W AW, Hamilton, Garth G, Watts, Colin C and van Aalten, Daan M F DM..  (2006)  Structural basis of reduction-dependent activation of human cystatin F..  The Journal of biological chemistry,    (16):   [PMID:16601115]

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