추천 제품
생물학적 소스
human
재조합
expressed in FreeStyle™ 293-F cells
분석
≥90% (SDS-PAGE)
양식
aqueous solution
특이 활성도
≥8100 pmol/min-μg
분자량
37 kDa
기술
activity assay: suitable
적합성
suitable for molecular biology
NCBI 수납 번호
응용 분야
life science and biopharma
배송 상태
dry ice
저장 온도
−70°C
유전자 정보
human ... CTSS(1520)
일반 설명
Research area: Cell Signaling
Human cathepsin S (GenBank Accession No. NM_004079.3), CD33 signal peptide (amino acids 1-16) + cathepsin S (amino acids 17-331), with C-terminal HIS tag, MW = 37 kDa, expressed in FreeStyle 293-F cells. Cathepsin S belongs to the cysteine cathepsin protease family. It has limited tissue expression, being associated with antigen-presenting cells localized in lymph and spleen, as well as other immune cells like macrophages. Human cathepsin S is produced from its corresponding CTSS gene on chromosome 1q21 and is synthesized as a pre-proenzyme.[1]
Human cathepsin S (GenBank Accession No. NM_004079.3), CD33 signal peptide (amino acids 1-16) + cathepsin S (amino acids 17-331), with C-terminal HIS tag, MW = 37 kDa, expressed in FreeStyle 293-F cells. Cathepsin S belongs to the cysteine cathepsin protease family. It has limited tissue expression, being associated with antigen-presenting cells localized in lymph and spleen, as well as other immune cells like macrophages. Human cathepsin S is produced from its corresponding CTSS gene on chromosome 1q21 and is synthesized as a pre-proenzyme.[1]
애플리케이션
Active human cathepsin S has been used:
- to assess the pathogenesis of Alzheimer′s disease. [2]
- to investigate the optimization of selectivity of Azepanone-based inhibitors. [3]
- for the immunocytochemical detection of cathepsin-S in mouse samples.[4]
- for incubating mouse brain sections to test the impact of cathepsin-S on perineuronal nets (PNNs) integrity.[4]
생화학적/생리학적 작용
Cathepsin S, as a lysosomal protease, facilitates the breakdown of unwanted and damaged proteins in the endo-lysosomal pathway. Moreover, it plays specific roles, such as contributing to major histocompatibility complex (MHC) class II antigen presentation by aiding in the degradation of the invariant chain. Dysregulation of cathepsin S has been associated with various pathological conditions, such as cancer, arthritis, and cardiovascular disease.[1] Cathepsin S is useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling. It is also used as a biomarker for atherosclerosis, diabetes, adiposity, and atherogenesis. Moreover, it acts as a promising target against brain-penetrating and for the treatment of multiple sclerosis and neuropathic pain.
단위 정의
One unit is defined as the amount of enzyme that will cleave 1 pmol of substrate per min at 37°C
물리적 형태
Formulated in 45 mM Tris-HCl, pH 8.0, 124 mM NaCl, 2.4 mM KCl, 225 mM imidazole, 3 mM DTT, and 10% glycerol.
제조 메모
Thaw on ice. Upon first thaw, briefly spin tube containing enzyme to recover full content of the tube. Aliquot enzyme into single use aliquots. Store remaining undiluted enzyme in aliquots at -70°C. Note: Enzyme is very sensitive to freeze/thaw cycles.
법적 정보
FreeStyle is a trademark of Invitrogen Corp.
신호어
Danger
유해 및 위험 성명서
Hazard Classifications
Eye Irrit. 2 - Repr. 1B - Skin Irrit. 2
Storage Class Code
6.1C - Combustible acute toxic Cat.3 / toxic compounds or compounds which causing chronic effects
WGK
WGK 3
Flash Point (°F)
Not applicable
Flash Point (°C)
Not applicable
가장 최신 버전 중 하나를 선택하세요:
시험 성적서(COA)
Lot/Batch Number
D Brömme et al.
Protein science : a publication of the Protein Society, 5(4), 789-791 (1996-04-01)
We have expressed active human cathepsin S to 60 mg/L in Sf9 cells using a baculovirus system. Production of milligram quantities has facilitated crystallographic studies to determine the structure of this enzyme, which has unique properties among lysosomal cysteine proteinases.
Harry Pantazopoulos et al.
eNeuro, 7(4) (2020-07-29)
Perineuronal nets (PNNs) are extracellular matrix (ECM) structures that envelop neurons and regulate synaptic functions. Long thought to be stable structures, PNNs have been recently shown to respond dynamically during learning, potentially regulating the formation of new synapses. We postulated
Richard D A Wilkinson et al.
Biological chemistry, 396(8), 867-882 (2015-04-16)
Cathepsin S is a member of the cysteine cathepsin protease family. It is a lysosomal protease which can promote degradation of damaged or unwanted proteins in the endo-lysosomal pathway. Additionally, it has more specific roles such as MHC class II
Azepanone-based inhibitors of human cathepsin S: optimization of selectivity via the P2 substituent.
Jeffrey K Kerns et al.
Bioorganic & medicinal chemistry letters, 21(15), 4409-4415 (2011-07-08)
A series of azepanone inhibitors of cathepsin S is described. Selectivity over both cathepsin K and cathepsin L was achieved by varying the P2 substituent. Ultimately, a balanced potency and selectivity profile was achieved in compound 39 possessing a 1-methylcyclohexyl
Israel Schechter et al.
Biological chemistry, 392(6), 555-569 (2011-05-19)
β-site APP-cleaving enzyme (BACE1) cleaves the wild type (WT) β-site very slowly (k(cat)/K(m): 46.6 m(-1) s(-1)). Therefore we searched for additional β-secretases and identified three cathepsins that split the WT β-site much faster. Human cathepsin S cleaves the WT β-site
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