C8511

Cathepsin C from bovine spleen

Type X, lyophilized powder, ≥5 units/mg protein

• 동의어(들): Dipeptidyl aminopeptidase, Dipeptidyl peptidase I
• CAS Number: 9032-68-2
• 효소 위원회 번호: 3.4.14.1 (BRENDA, IUBMB)
• EC Number: 232-881-4
• MDL number: MFCD00081490
• UNSPSC 코드: 12352204
• NACRES: NA.54

속성

• 생물학적 소스: bovine spleen
• 유형: Type X
• 분석: >25% protein (biuret)
• 양식: lyophilized powder
• 특이 활성도: ≥5 units/mg protein
• 구성: Protein, ≥25% biuret
• 제조업체/상표: Sigma-Aldrich
• 저장 조건: OK to freeze (Unstable. Keep frozen)
• 농도: ≥5 unit/mg protein
• 기술: activity assay: suitable
• 적합성: suitable for molecular biology
• 응용 분야: life science and biopharma
• 배송 상태: dry ice
• 저장 온도: −20°C
• 유전자 정보: cow ... CTSC(352958)

설명

일반 설명

Research Area: Cell Signaling
Dipeptidyl peptidase I (DPPI), also known as cathepsin C, is an abundant lysosomal cysteine protease from the papain superfamily with a molecular weight of approximately 200 kDa.[1] It is widely expressed in a variety of mammalian tissues, with the highest levels found in the lungs, kidneys, liver, and spleen, and relatively lower levels in the brain.[2]
DPPI is the only member of its family that is functional as a tetramer, consisting of four identical subunits, each composed of an N-terminal fragment, a heavy chain, and a light chain. It is identified as one of the multifaceted protease-processing machines, having been shown to function beyond its role as a non-specific lysosomal protease.[1]

애플리케이션

Cathepsin C from bovine spleen has been used for the in vitro enzyme activity assays.[3] It has also been used as a digestion enzyme for in vitro myelin oligodendrocyte glycoprotein (MOG) digestion.[4]

Cathepsin C has been used in a study that demonstrated the potential of a proteomics approach to identify novel proteins expressed by extravillous trophoblast and to uncover the mechanisms leading to disease states in pregnancy. Cathepsin C has also been used in a study to evaluate biodegradable thermogels.

The enzyme from Sigma has been used in the activation of granzyme k (Gzmk) precursor from E. coli. Granzymes are granule-stored lymphocyte serine proteases that are implicated in T- and natural killer cell-mediated cytotoxic defense reactions.[5]

생화학적/생리학적 작용

Cathepsin C (Cat C) serves as the physiological activator of groups of serine proteases within immune and inflammatory cells, playing a crucial role in the defense mechanisms of an organism. It may play a role in chronic airway diseases such as asthma. Cat C also acts as a protease link between inflammation and thrombosis.[1]
Cat C participates in neutrophil recruitment and production of chemokines and cytokines in many inflammatory diseases. Cathepsin C plays a crucial role as an essential enzyme in activating granule serine proteases in cytotoxic T lymphocytes, natural killer cells (granzymes A and B), mast cells (chymase and tryptase), and neutrophils (cathepsin G, proteinase 3, and elastase).[2]

Cathespin C is a dipeptidyl aminopeptidase that can sequentially remove dipeptides from a peptide chain with an unsubstituted N-terminus. The enzyme exhibits a preference for glycine and proline as N-terminal aminoacids. Substrates that have an N-terminal lysyl or arginyl residue, or a penultimate proryl residue are not targeted by this enzyme.[6] The endopeptidase activity requires the presence of halide ions and sulfydryl activators.[7]

주의사항

Unstable. Keep frozen.

단위 정의

One unit will produce 1 μmole of Gly-Phe-NHOH from Gly-Phe-NH₂ and hydroxylamine per min at pH 6.8 at 37 °C using DL-phenylalanine hydroxamic acid as the standard. In addition to its hydrolytic properties, cathepsin C catalyzes the polymerization of dipeptide amides.

물리적 형태

Lyophilized from a 1 M sodium chloride solution.

안전성 정보

• Storage Class Code: 11 - Combustible Solids
• WGK: WGK 3
• Flash Point (°F): Not applicable
• Flash Point (°C): Not applicable
• 개인 보호 장비: Eyeshields, Gloves, type N95 (US)