CTSF Antilichaam

Cathepsins are papain family cysteine proteinases that represent a major component of the lysosomal proteolytic system. Cathepsins generally contain a signal sequence, followed by a propeptide and then a catalytically active mature region. The very long (251 amino acid residues) proregion of the cathepsin F precursor contains a C-terminal domain similar to the pro-segment of cathepsin L-like enzymes, a 50-residue flexible linker peptide, and an N-terminal domain predicted to adopt a cystatin-like fold. The cathepsin F proregion is unique within the papain family cysteine proteases in that it contains this additional N-terminal segment predicted to share structural similarities with cysteine protease inhibitors of the cystatin superfamily. This cystatin-like domain contains some of the elements known to be important for inhibitory activity. CTSF encodes a predicted protein of 484 amino acids which contains a 19 residue signal peptide. Cathepsin F contains five potential N-glycosylation sites, and it may be targeted to the endosomal/lysosomal compartment via the mannose 6-phosphate receptor pathway. The cathepsin F gene is ubiquitously expressed, and it maps to chromosome 11q13, close to the gene encoding cathepsin W.

8722

Q9UBX1

Human, Mouse

Recombinant fusion protein containing a sequence corresponding to amino acids 270-484 of human CTSF (NP_003784.2) .

Unconjugated

Primary Antibodies

Immunology, Innate Immunity

Affinity purification

U-251MG

Batch dependent

PBS with 0.02% sodium azide, 50% glycerol, pH7.3.

None

Blue Ice

Store at -20˚ C. Avoid freeze / thaw cycles.

Observed: 53kDa

IgG

CTSF

SKOV3

Cathepsin F

Homo sapiens

CTSF, cathepsin F, HGNC:2531, CATSF, CLN13

WB, IHC, IF

Liquid