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AB157067

Recombinant human Cathepsin K protein (Active)

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(3 Publications)

Recombinant human Cathepsin K protein (Active) is a Human Full Length protein, in the 1 to 329 aa range, expressed in Baculovirus infected insect cells, with >95%, suitable for SDS-PAGE, FuncS.

View Alternative Names

CTSO, CTSO2, CTSK, Cathepsin K, Cathepsin O, Cathepsin O2, Cathepsin X

2 Images
Functional Studies - Recombinant human Cathepsin K protein (Active) (AB157067)
  • FuncS

Supplier Data

Functional Studies - Recombinant human Cathepsin K protein (Active) (AB157067)

Each lane contains 1 ug of total protein during time-course activation at low pH.

Lane 1 : Pre-Activation.

Lane 2 : 0 min

Lane 3 : 1 hour

Lane 4 : 2 hours

Lane 5 : 3 hours

Lane 6 : 4 hours

SDS-PAGE - Recombinant human Cathepsin K protein (Active) (AB157067)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant human Cathepsin K protein (Active) (AB157067)

ab157067 on SDS-PAGE.

Lane 1 : 1 ug.

Lane 2 : 2 ug.

Key facts

Purity

>95% SDS-PAGE

Expression system

Baculovirus infected insect cells

Tags

Tag free

Applications

FuncS, SDS-PAGE

applications

Biologically active

Yes

Biological activity

≥ 1.5 U/mg protein. Activity is lot specific.

One unit is defined as the amount of enzyme that will hydrolyze 1μmol Z-Phe-Arg-AMC substrate per min. at 37°C.

Accession

P43235

Animal free

No

Carrier free

No

Species

Human

Storage buffer

Constituents: 0.41% Sodium acetate, 0.29% Sodium chloride, 0.08% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.015% EDTA

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"MWGLKVLLLPVVSFALYPEEILDTHWELWKKTHRKQYNNKVDEISRRLIWEKNLKYISIHNLEASLGVHTYELAMNHLGDMTSEEVVQKMTGLKVPLSHSRSNDTLYIPEWEGRAPDSVDYRKKGYVTPVKNQGQCGSCWAFSSVGALEGQLKKKTGKLLNLSPQNLVDCVSENDGCGGGYMTNAFQYVQKNRGIDSEDAYPYVGQEESCMYNPTGKAAKCRGYREIPEGNEKALKRAVARVGPVSVAIDASLTSFQFYSKGVYYDESCNSDNLNHAVLAVGYGIQKGNKHWIIKNSWGENWGNKGYILMARNKNNACGIANLASFPKM","proteinLength":"Full Length","predictedMolecularWeight":"26 kDa","actualMolecularWeight":null,"aminoAcidEnd":329,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Baculovirus infected insect cells","accessionNumber":"P43235","tags":[]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Storage information
Avoid freeze / thaw cycle
True

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Cathepsin K also known as CTSK is a protease enzyme that belongs to the papain family of cysteine proteases. With a molecular weight of approximately 37 kDa Cathepsin K is mainly expressed in osteoclasts which are cells involved in bone resorption. This enzyme functions by cleaving collagen a vital component of bone extracellular matrix which facilitates bone remodeling and turnover. Known for its collagenolytic activity Cathepsin K is important in processes where breakdown of collagen fibers is required.
Biological function summary

Cathepsin K plays a significant role in bone metabolism. It operates within the osteoclasts where it degrades type I collagen and other matrix proteins essential for normal bone maintenance and repair. Cathepsin K does not function as part of a complex but acts independently in its enzymatic role. It is highly specific to substrates found in the bone matrix differentiating it from other cathepsins like cathepsin L or B that may have broader expression and role.

Pathways

Cathepsin K is an important player in the bone remodeling pathway. This pathway involves a series of coordinated actions between osteoclasts and osteoblasts to maintain bone health. Cathepsin K's activity is tightly regulated within this pathway to ensure proper bone density and structure. It is associated with other proteins such as osteopontin and matrix metalloproteinases which work together to modulate bone turnover. Within the RANK/RANKL pathway Cathepsin K acts as a downstream effector following osteoclast activation by RANKL.

Cathepsin K is most notably linked to osteoporosis and pycnodysostosis. Osteoporosis arises due to excessive bone resorption where elevated Cathepsin K activity leads to weakened bone structure increasing fracture risk. Pycnodysostosis is a rare genetic disorder caused by mutations in the gene coding for Cathepsin K resulting in impaired bone resorption and abnormally dense but brittle bones. In these conditions proteins such as RANKL and osteoprotegerin also play critical roles by influencing osteoclast differentiation and activity thereby modulating Cathepsin K's effects.

Specifications

Form

Liquid

Additional notes

ab157067 was purified as full-length proenzyme, then auto-activated at low pH.

General info

Function

Thiol protease involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation. Involved in the release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (PubMed : 11082042).

Sequence similarities

Belongs to the peptidase C1 family.

Subcellular localisation

Lysosome

Product protocols

Target data

Thiol protease involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation. Involved in the release of thyroid hormone thyroxine (T4) by limited proteolysis of TG/thyroglobulin in the thyroid follicle lumen (PubMed : 11082042).
See full target information CTSK

Publications (3)

Recent publications for all applications. Explore the full list and refine your search

Biochemistry 61:228-238 PubMed35119840

2022

Molecular Features of CA-074 pH-Dependent Inhibition of Cathepsin B.

Applications

Unspecified application

Species

Unspecified reactive species

Michael C Yoon,Mitchell P Christy,Von V Phan,William H Gerwick,Gregory Hook,Anthony J O'Donoghue,Vivian Hook

ACS chemical biology 16:1628-1643 PubMed34416110

2021

Selective Neutral pH Inhibitor of Cathepsin B Designed Based on Cleavage Preferences at Cytosolic and Lysosomal pH Conditions.

Applications

Unspecified application

Species

Unspecified reactive species

Michael C Yoon,Angelo Solania,Zhenze Jiang,Mitchell P Christy,Sonia Podvin,Charles Mosier,Christopher B Lietz,Gen Ito,William H Gerwick,Dennis W Wolan,Gregory Hook,Anthony J O'Donoghue,Vivian Hook

Science advances 7: PubMed33893096

2021

A non-immunological role for γ-interferon-inducible lysosomal thiol reductase (GILT) in osteoclastic bone resorption.

Applications

Unspecified application

Species

Unspecified reactive species

Benjamin W Ewanchuk,Corey R Arnold,Dale R Balce,Priyatha Premnath,Tanis L Orsetti,Amy L Warren,Alexandra Olsen,Roman J Krawetz,Robin M Yates
View all publications

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