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The cystatin superfamily encompasses proteins that contain multiple cystatin-like sequences. Additionally we are shipping Cystatin C Kits (115) and Cystatin C Proteins (78) and many more products for this protein.
Showing 10 out of 457 products:
Human Monoclonal CST3 Primary Antibody for ELISA, WB - ABIN969070
Helisalmi, Väkevä, Hiltunen, Soininen: Flanking markers of cystatin c (CST3) gene do not show association with Alzheimer's disease. in Dementia and geriatric cognitive disorders 2009
Show all 2 references for 969070
Human Monoclonal CST3 Primary Antibody for IHC, IHC (p) - ABIN4301883
Gren, Janciauskiene, Sandeep, Jonigk, Kvist, Gerwien, Håkansson, Grip: The protease inhibitor cystatin C down-regulates the release of IL-β and TNF-α in lipopolysaccharide activated monocytes. in Journal of leukocyte biology 2016
Human Polyclonal CST3 Primary Antibody for IHC, IHC (p) - ABIN4301882
Wu, Hsu, Chen, Yu, Chang, Tai, Liu, Su, Chang, Yu: Candidate serological biomarkers for cancer identified from the secretomes of 23 cancer cell lines and the human protein atlas. in Molecular & cellular proteomics : MCP 2010
Mouse (Murine) Polyclonal CST3 Primary Antibody for ELISA, WB - ABIN184744
Huh, Nagle, Kozak, Abrahamson, Karlsson: Structural organization, expression and chromosomal mapping of the mouse cystatin-C-encoding gene (Cst3). in Gene 1995
Human Monoclonal CST3 Primary Antibody for EIA - ABIN181125
Mussap, Plebani: Biochemistry and clinical role of human cystatin C. in Critical reviews in clinical laboratory sciences 2004
Human Polyclonal CST3 Primary Antibody for ELISA, WB - ABIN439722
Mi, Pawlik, Sastre, Jung, Radvinsky, Klein, Sommer, Schmidt, Nixon, Mathews, Levy: Cystatin C inhibits amyloid-beta deposition in Alzheimer's disease mouse models. in Nature genetics 2007
Data suggest that melanoma cells internalize/absorb cystatin C from culture media, leading to increased intracellular cystatin C levels; cystatin E/M (show CST6 Antibodies) is internalized as well but at modest rate due to down-regulation of cell migration; however, the effect of intracellular cystatin E/M (show CST6 Antibodies) on down-regulation of legumain (show LGMN Antibodies) activity is pronounced.
An elevated preoperative Cys (show DNAJC5 Antibodies)-C level was demonstrated to be related with worse survival in patients with renal cell carcinoma (show MOK Antibodies)(RCC (show XRCC1 Antibodies)). Measuring preoperative serum Cys (show DNAJC5 Antibodies)-C might be a simple way for finding poor prognostic patients and patients with elevated preoperative Cys (show DNAJC5 Antibodies)-C level should be more closely followed up
Acute kidney injury is common following deliberate self-poisoning with a combination washing powder containing oxalic acid and potassium permanganate and cystatin C monitoring may under estimate the severity of poisoning.
Cystatin C significantly decreased the lipopolysaccharide-stimulated release and expression of interleukin-1beta and tumor necrosis factor-alpha (show TNF Antibodies) in monocyte and peripheral blood mononuclear cultures from healthy donors and Crohn's patients. Cystatin C was internalized by monocytes via an active endocytic process, decreased phosphorylation of the MAP kinase (show MAPK1 Antibodies) pathway ERK-1 (show MAPK3 Antibodies)/2, and altered surface markers.
Fibrillation of CysC therefore likely initiates from the monomer and does not require domain-swapping. The non-swapped oligomers likely represent a dead-end (show DND1 Antibodies) offshoot of the amyloid pathway and must dissociate to monomers prior to rearranging to amyloid fibrils. These prefibrillar CysC oligomers were potent inhibitors of aggregation of the Alzheimer's-related peptide, beta-amyloid.
CysC plays an important regulatory role in combating cell death via the autophagic pathway in atherosclerosis.
Data show that cystatin C deposition in minimally affected samples was limited to the basement membrane (BM) between the dermis and epidermis.
Urinary cystatin C levels in the acute kidney injury (AKI) preterm infant group were not significantly higher than in no-AKI group on day of life 1, 3 and 7.
Serum cystatin C level was found to be associated with the development and worsening of AKI [Acute kidney injury ] in ICU [intensive care unit ] patients with sepsis.
Elevated cystatin C levels at admission were independently associated with impaired myocardial perfusion, poor cardiac functional recovery and development of congestive heart failure in patients with anterior STEMI undergoing PCI (show SERPINA5 Antibodies).
Data (including data from studies in mutant mice) suggest that up-regulation of Cst3, as observed in plasma of mice with type 2 diabetes, down-regulates insulin (show INS Antibodies) signaling and promotes endoplasmic reticulum stress in hepatocytes but not in myotubes.
Cystatin C is a potential pathogenic signal triggering neurodegeneration in multiple system atrophy.
The neuroprotective activity of CysC against Amyotrophic lateral sclerosis-linked mutant Cu/Zn-superoxide dismutase (SOD1 (show SOD1 Antibodies))-mediated toxicity.
an important role for macrophages, DC, and ROS (show ROS1 Antibodies) in diseases associated with the protease inhibitory activity or amyloidogenic properties of cystatin C.
APP (show APP Antibodies) expression stimulates NSPC proliferation; this effect is mediated via an increase in cystatin C secretion
Cystatin C, a protein targeted to the classical secretory pathway by its signal peptide sequence, is secreted by primary neurons in at least 9 different cystatin C glycoforms associated with exosomes.
The lack of cystatin C enhances Collagen-induced arthritis and primarily affects in vivo priming of the immune system
Inflammation causes downregulation of cystatin C expression in dendritic cells and reduces serum CstC levels.
Data show that the absence of cystatin C reduced epithelial cell apoptosis but increased proliferation in skin.
CST3 may be required to remodel endometrial and placental tissues for close apposition between maternal and fetal vasculatures and to facilitate transplacental transport of gases, micronutrients (amino acids, glucose), and macromolecules (proteins).
Increased production of cystatin C in osteoarthritis synovium does not alleviate synovitis or cartilage pathology.
Cystatin C in milk basic protein (MBP (show MBP Antibodies)) is suggested as one of the factors inhibiting bone resorption
The cystatin superfamily encompasses proteins that contain multiple cystatin-like sequences. Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never acquired this inhibitory activity. There are three inhibitory families in the superfamily, including the type 1 cystatins (stefins), type 2 cystatins and the kininogens. The type 2 cystatin proteins are a class of cysteine proteinase inhibitors found in a variety of human fluids and secretions, where they appear to provide protective functions. The cystatin locus on chromosome 20 contains the majority of the type 2 cystatin genes and pseudogenes. This gene is located in the cystatin locus and encodes the most abundant extracellular inhibitor of cysteine proteases, which is found in high concentrations in biological fluids and is expressed in virtually all organs of the body. A mutation in this gene has been associated with amyloid angiopathy. Expression of this protein in vascular wall smooth muscle cells is severely reduced in both atherosclerotic and aneurysmal aortic lesions, establishing its role in vascular disease.
, egg-white cystatin
, cystatin C
, cystatin 3
, hypothetical protein
, bA218C14.4 (cystatin C)
, neuroendocrine basic polypeptide
, Cystatin C (cysteine proteinase inhibitor)
, colostrum thiol proteinase inhibitor
, cystatin C (amyloid angiopathy and cerebral hemorrhage)