Anti -TPP-1(Tripeptidyl-peptidase 1, TPP-l, Tripeptidyl aminopeptidase, Lysosomal pepstatin-insensitive protease, LPIC, Cell growth-inhibiting gene 1 protein, TPP1, CLN2)

For Research Use Only. Not for use in diagnostic procedures.

Chromosome: 11; NC_000011.9 (6633997..6640692, complement). Location: 11p15

Monoclonal

IgG

9G454

Mouse

Recognizes human TPP1(195-305).

Affinity Purified
Purified by affinity chromatography.

Supplied as a lyophilized powder in PBS, pH 7.6. Reconstitute with 100ul sterile ddH2O.

Lyophilized powder may be stored at -20 degree C. Stable for 12 months at -20 degree C. Reconstitute with sterile 40-50% glycerol, ddH2O. Reconstituted product is stable for 12 months at -20 degree C. Aliquot and store at -20 degree C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Small volumes of anti-TPP1 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

TPP1 is a lysosomal serine protease with tripeptidyl-peptidase I activity. It may act as a non-specific lysosomal peptidase which releases an N-terminal tripeptide from the breakdown products produced by lysosomal proteinases. Requires substrates with an unsubstituted N-terminus. TPP1 is detected in lysosomes and melanosomes in all tissues but it is highest in the heart and placenta. TPP1 is activated by autocatalytic proteolytic processing upon acidification within lysosomes. Defects in TPP1 cause classical late-infantile neuronal ceroid lipofuscinosis (LINCL) which is also known as ceroid lipofuscinosis 2 (CLN2). It is a fatal childhood neurodegenerative disease characterised by progressive visual and mental deterioration, motor disturbance, epilepsy and behavioral changes.

Antibodies; Abs to Proteins

ELISA (EL/EIA), Western Blot (WB), Immunohistochemistry (IHC)

Suitable for use in ELISA, Western Blot and Immunohistochemistry.

61,248 Da[Similar Products]

tripeptidyl peptidase I

tripeptidyl-peptidase 1; OTTHUMP00000164588; tripeptidyl aminopeptidase; growth-inhibiting protein 1; cell growth-inhibiting gene 1 protein; lysosomal pepstatin insensitive protease

Tripeptidyl-peptidase 1

CLN2??[Similar Products]

TPP1_HUMAN

This gene encodes a member of the sedolisin family of serine proteases. The protease functions in the lysosome to cleave N-terminal tripeptides from substrates, and has weaker endopeptidase activity. It is synthesized as a catalytically-inactive enzyme which is activated and auto-proteolyzed upon acidification. Mutations in this gene result in late-infantile neuronal ceroid lipofuscinosis, which is associated with the failure to degrade specific neuropeptides and a subunit of ATP synthase in the lysosome. [provided by RefSeq]

TPP1: Lysosomal serine protease with tripeptidyl-peptidase I activity. May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Requires substrates with an unsubstituted N-terminus. Defects in TPP1 are the cause of neuronal ceroid lipofuscinosis type 2 (CLN2). A form of neuronal ceroid lipofuscinosis. Neuronal ceroid lipofuscinoses are progressive neurodegenerative, lysosomal storage diseases characterized by intracellular accumulation of autofluorescent liposomal material, and clinically by seizures, dementia, visual loss, and/or cerebral atrophy. The lipopigment pattern seen most often in CLN2 consists of curvilinear profiles. Belongs to the peptidase S53 family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Mitochondrial; Protease; EC 3.4.14.9; Secreted, signal peptide; Secreted

Chromosomal Location of Human Ortholog: 11p15

Cellular Component: lysosomal lumen; mitochondrion; lysosome; melanosome

Molecular Function: tripeptidyl-peptidase activity; peptidase activity; protein binding; serine-type peptidase activity; metal ion binding; serine-type endopeptidase activity; endopeptidase activity; peptide binding

Biological Process: nervous system development; cellular protein metabolic process; unfolded protein response, activation of signaling protein activity; epithelial cell differentiation; lysosome organization and biogenesis; unfolded protein response; peptide catabolic process; protein catabolic process; lipid metabolic process; neuromuscular process controlling balance; proteolysis; bone resorption

Disease: Ceroid Lipofuscinosis, Neuronal, 2

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