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H5041

Sigma-Aldrich

Cystatin C human

HumanKine®, ≥95% (SDS-PAGE), recombinant, expressed in HEK 293 cells, suitable for cell culture

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About This Item

MDL number:
UNSPSC Code:
12352202
NACRES:
NA.77

product name

Cystatin C human, recombinant, expressed in HEK 293 cells, HumanKine®, suitable for cell culture

biological source

human

Quality Level

recombinant

expressed in HEK 293 cells

Assay

≥95% (SDS-PAGE)

form

lyophilized powder

potency

≤5 μM IC50

quality

endotoxin tested

mol wt

dimer 12-13 kDa (non-glycosylated)

packaging

pkg of 10 μg

storage condition

avoid repeated freeze/thaw cycles

technique(s)

cell culture | mammalian: suitable

impurities

≤1 EU/mg

UniProt accession no.

storage temp.

−20°C

Gene Information

human ... CYTC(1471)

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General description

HumanKine human Cystatin C is expressed as a non-glycosylated monomer in human HEK 293 cells. Cystatin C belongs to the cystatin superfamily. Two isoforms (pI = 7.8, 9.2) of native Cystatin C are found in human urine differentiated by the elimination of small basic peptides or amino acids from the N-terminal end of the protein. This protein is coded by a housekeeping gene, CST3 located on human chromosome 20p11.21 and is generated by nucleated cells.

Application

Cystatin C human has been used as a standard in western blot assay. It has also been used to study its effect on the endopeptidase activity of activated Trichobilharzia regenti isoform of cathepsin B1 peptidase (TrCB1).

Biochem/physiol Actions

Cystatin C is an inhibitor of cysteine proteases including cathepsin B which has been identified as the most important β-amyloid-degrading enzyme. Measurement of cystatin C in serum is replacing creatinine as an indicator of kidney function (glomerular filtration rate, GFR). Studies show its role in predicting new-onset or deteriorating cardiovascular disease. It also seems to play a role in brain disorders involving amyloid, such as Alzheimer′s disease. Cystatin C inhibits transforming growth factor β signaling in normal and cancer cells.

Physical form

Lyophilized from a 0.2 μm filtered solution of 1×PBS

Analysis Note

The inhibitory function of cystatin c on papain′s protease activity was measured by a colorimetric assay using L-BAPA as substrate. IC50 value was measured at 5 to 20 μg/mL (0.3 to 1.5 μM) with a range of 1.56 μg/mL to 50 μg/mL cystatin C in presence of 0.55 μM papain and 0.44 μM L-BAPA.

Legal Information

HumanKine is a registered trademark of Proteintech Group, Inc. and Humanzyme, Inc

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Assessment of glomerular filtration rate in acute and chronic settings
National Kidney Foundation Primer on Kidney Diseases, 26-32 (2014)
Assessing kidney function
Chronic Renal Disease, 31-42 (2015)
M S N Murty et al.
Indian journal of nephrology, 23(3), 180-183 (2013-07-03)
In patients with acute kidney injury (AKI), serum creatinine level does not increase until moderate to severe reduction in glomerular filtration rate (GFR) occurs. Thus its use for estimating GFR in early AKI delays detection of kidney damage and making
Can-E Tang et al.
Journal of proteome research, 9(12), 6101-6111 (2010-10-05)
The epidermal growth factor receptor (EGFR) is usually overexpressed in nasopharyngeal carcinoma (NPC) and is associated with pathogenesis of NPC. However, while EGFR-modulated intracellular proteins have been extensively studied, little is known concerning their extracellular counterparts. To identify EGFR-regulated secreted
Paul M Mathews et al.
Ageing research reviews, 32, 38-50 (2016-06-24)
Under normal conditions, the function of catalytically active proteases is regulated, in part, by their endogenous inhibitors, and any change in the synthesis and/or function of a protease or its endogenous inhibitors may result in inappropriate protease activity. Altered proteolysis

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