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Mouse Anti-CST3 Recombinant Antibody (678920) (CBMAB-C7939-LY)


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Summary

Host Animal
Mouse
Specificity
Rat
Clone
678920
Antibody Isotype
IgG2a
Application
IHC-F, IP

Basic Information

Immunogen
Mouse myeloma cell line NS0-derived recombinant rat Cystatin C Gly21-Ala140
Specificity
Rat
Antibody Isotype
IgG2a
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
5% trehalose
Concentration
0.2 mg/ml
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
Cystatin C
Introduction
CST3 (Cystatin C) is a Protein Coding gene. Diseases associated with CST3 include Cerebral Amyloid Angiopathy, Cst3-Related and Macular Degeneration, Age-Related, 11. Among its related pathways are Innate Immune System and Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3. Gene Ontology (GO) annotations related to this gene include identical protein binding and endopeptidase inhibitor activity.
An important paralog of this gene is CST2.
Entrez Gene ID
25307
UniProt ID
P14841
Alternative Names
Cystatin C; Neuroendocrine Basic Polypeptide; Post-Gamma-Globulin; Gamma-Trace; Cystatin C (Amyloid Angiopathy And Cerebral Hemorrhage); Epididymis Secretory Protein Li 2; BA218C14.4 (Cystatin C);
Function
As an inhibitor of cysteine proteinases, this protein is thought to serve an important physiological role as a local regulator of this enzyme activity.
Biological Process
Amyloid fibril formation Source: Reactome
Cellular protein metabolic process Source: Reactome
Defense response Source: BHF-UCL
Negative regulation of blood vessel remodeling Source: BHF-UCL
Negative regulation of collagen catabolic process Source: BHF-UCL
Negative regulation of elastin catabolic process Source: BHF-UCL
Negative regulation of extracellular matrix disassembly Source: BHF-UCL
Negative regulation of peptidase activity Source: ARUK-UCL
Negative regulation of proteolysis Source: UniProtKB
Neutrophil degranulation Source: Reactome
Post-translational protein modification Source: Reactome
Regulation of tissue remodeling Source: BHF-UCL
Supramolecular fiber organization Source: BHF-UCL
Cellular Location
Secreted
Involvement in disease
Amyloidosis 6 (AMYL6):
A hereditary generalized amyloidosis due to cystatin C amyloid deposition. Cystatin C amyloid accumulates in the walls of arteries, arterioles, and sometimes capillaries and veins of the brain, and in various organs including lymphoid tissue, spleen, salivary glands, and seminal vesicles. Amyloid deposition in the cerebral vessels results in cerebral amyloid angiopathy, cerebral hemorrhage and premature stroke. Cystatin C levels in the cerebrospinal fluid are abnormally low.
Macular degeneration, age-related, 11 (ARMD11):
A form of age-related macular degeneration, a multifactorial eye disease and the most common cause of irreversible vision loss in the developed world. In most patients, the disease is manifest as ophthalmoscopically visible yellowish accumulations of protein and lipid that lie beneath the retinal pigment epithelium and within an elastin-containing structure known as Bruch membrane.
PTM
The Thr-25 variant is O-glycosylated with a core 1 or possibly core 8 glycan. The signal peptide of the O-glycosylated Thr-25 variant is cleaved between Ala-20 and Val-21.
More Infomation

Zhang, X., Liu, X., Su, G., Li, M., Liu, J., Wang, C., & Xu, D. (2021). pH-dependent and dynamic interactions of cystatin C with heparan sulfate. Communications biology, 4(1), 1-11.

Christopher, J. R., Ponnaiyan, D., Parthasarathy, H., & Tadepalli, A. (2021). Association of CST3 Gene with Its Protein: Cystatin C in Health and Severe Periodontal Disease. Genetic Testing and Molecular Biomarkers, 25(6), 405-410.

Indacochea, A., Guerrero, S., Ureña, M., Araujo, F., Coll, O., LLeonart, M. E., & Gebauer, F. (2021). Cold-inducible RNA binding protein promotes breast cancer cell malignancy by regulating Cystatin C levels. Rna, 27(2), 190-201.

Tahir, N. A. M., Saffian, S. M., Islahudin, F. H., Gafor, A. H. A., Othman, H., Manan, H. A., & Makmor-Bakry, M. (2020). Effects of CST3 Gene G73A Polymorphism on Cystatin C in a Prospective Multiethnic Cohort Study. Nephron, 144(4), 204-212.

Hoghooghi, V., Palmer, A. L., Frederick, A., Jiang, Y., Merkens, J. E., Balakrishnan, A., ... & Ousman, S. S. (2020). Cystatin C Plays a Sex-Dependent Detrimental Role in Experimental Autoimmune Encephalomyelitis. Cell reports, 33(1), 108236.

Maniwa, K., Yano, S., Sheikh, A. M., Onoda, K., Mitaki, S., Isomura, M., ... & Nagai, A. (2020). Association between cystatin C gene polymorphism and the prevalence of white matter lesion in elderly healthy subjects. Scientific Reports, 10(1), 1-9.

Huda, M. N., VerHague, M., Albright, J., Smallwood, T., Bell, T. A., Que, E., ... & Bennett, B. J. (2020). Dissecting the genetic architecture of cystatin C in Diversity Outbred mice. G3: Genes, Genomes, Genetics, 10(7), 2529-2541.

Zeng, Q., Huang, Z., Wei, L., Fang, J., & Lin, K. (2019). Correlations of serum cystatin C level and gene polymorphism with vascular cognitive impairment after acute cerebral infarction. Neurological Sciences, 40(5), 1049-1054.

Lee, R. K. K., Tseng, H. C., Hwu, Y. M., Fan, C. C., Lin, M. H., Yu, J. J., ... & Li, S. H. (2018). Expression of cystatin C in the female reproductive tract and its effect on human sperm capacitation. Reproductive Biology and Endocrinology, 16(1), 1-10.

Li, Z., Wang, S., Huo, X., Yu, H., Lu, J., Zhang, S., ... & Chen, Z. (2018). Cystatin C expression is promoted by VEGFA blocking, with inhibitory effects on endothelial cell angiogenic functions including proliferation, migration, and chorioallantoic membrane angiogenesis. Journal of the American Heart Association, 7(21), e009167.

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For research use only. Not intended for any clinical use.

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