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Rat Anti-HTRA1 Recombinant Antibody (CBFYM-1135) (CBMAB-M1292-FY)


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Summary

Host Animal
Rat
Specificity
Mouse
Clone
CBFYM-1135
Antibody Isotype
IgG1
Application
ELISA, IP, WB

Basic Information

Immunogen
NS0-derived recombinant mouse MCP-11/Prss34
Specificity
Mouse
Antibody Isotype
IgG1
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
Lyophilized
Buffer
PBS, 5% trehalose
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
HtrA Serine Peptidase 1
Introduction
This gene encodes a member of the trypsin family of serine proteases. This protein is a secreted enzyme that is proposed to regulate the availability of insulin-like growth factors by cleaving IGF-binding proteins. It has also been suggested to be a regulator of cell growth. Variations in the promoter region of this gene are the cause of susceptibility to age-related macular degeneration type 7.
Entrez Gene ID
5654
UniProt ID
Q92743
Alternative Names
HtrA Serine Peptidase 1; High-Temperature Requirement A Serine Peptidase 1; Protease, Serine, 11 (IGF Binding); PRSS11; HtrA; L56; Serine Protease HTRA1; Serine Protease 11; IGFBP5-Protease
Function
Serine protease with a variety of targets, including extracellular matrix proteins such as fibronectin. HTRA1-generated fibronectin fragments further induce synovial cells to up-regulate MMP1 and MMP3 production. May also degrade proteoglycans, such as aggrecan, decorin and fibromodulin. Through cleavage of proteoglycans, may release soluble FGF-glycosaminoglycan complexes that promote the range and intensity of FGF signals in the extracellular space. Regulates the availability of insulin-like growth factors (IGFs) by cleaving IGF-binding proteins. Inhibits signaling mediated by TGF-beta family members. This activity requires the integrity of the catalytic site, although it is unclear whether TGF-beta proteins are themselves degraded. By acting on TGF-beta signaling, may regulate many physiological processes, including retinal angiogenesis and neuronal survival and maturation during development. Intracellularly, degrades TSC2, leading to the activation of TSC2 downstream targets.
Biological Process
Chorionic trophoblast cell differentiation Source: Ensembl
Dentinogenesis Source: Ensembl
Negative regulation of BMP signaling pathway Source: Ensembl
Negative regulation of defense response to virus Source: Ensembl
Negative regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
Placenta development Source: Ensembl
Positive regulation of apoptotic process Source: GO_Central
Positive regulation of epithelial cell proliferation Source: Ensembl
Programmed cell death Source: GO_Central
Proteolysis Source: UniProtKB
Cellular Location
Secreted; Cytosol; Cell membrane. Predominantly secreted (PubMed:15208355). Also found associated with the plasma membrane (PubMed:21297635).
Involvement in disease
Macular degeneration, age-related, 7 (ARMD7):
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.
Cerebral arteriopathy, autosomal recessive, with subcortical infarcts and leukoencephalopathy (CARASIL):
A cerebrovascular disease characterized by non-hypertensive arteriopathy of cerebral small vessels with subcortical infarcts, alopecia, and spondylosis. Small cerebral arteries show arteriosclerotic changes, fibrous intimal proliferation, and hyaline degeneration with splitting of the intima and/or the internal elastic membrane. Neurologic features include progressive dementia, gait disturbances, extrapyramidal and pyramidal signs, and demyelination of the cerebral white matter with sparing of U fibers.
Cerebral arteriopathy, autosomal dominant, with subcortical infarcts and leukoencephalopathy, 2 (CADASIL2):
A cerebrovascular disease characterized by multiple subcortical infarcts, pseudobulbar palsy, dementia, and the presence of granular deposits in small cerebral arteries producing ischemic stroke.
More Infomation

Tossetta, G., Fantone, S., Licini, C., Marzioni, D., & Mattioli-Belmonte, M. (2022). The multifaced role of HtrA1 in the development of joint and skeletal disorders. Bone, 157, 116350.

Pan, Y., Fu, Y., Baird, P. N., Guymer, R. H., Das, T., & Iwata, T. (2022). Exploring the contribution of ARMS2 and HTRA1 genetic risk factors in age-related macular degeneration. Progress in Retinal and Eye Research, 101159.

Tossetta, G., Fantone, S., Gesuita, R., Di Renzo, G. C., Meyyazhagan, A., Tersigni, C., ... & Marzioni, D. (2022). HtrA1 in Gestational Diabetes Mellitus: A Possible Biomarker?. Diagnostics, 12(11), 2705.

Oka, C., Saleh, R., Bessho, Y., & Reza, H. M. (2022). Interplay between HTRA1 and classical signalling pathways in organogenesis and diseases. Saudi Journal of Biological Sciences, 29(4), 1919-1927.

Al-Rabadi, L. F., Caza, T., Trivin-Avillach, C., Rodan, A. R., Andeen, N., Hayashi, N., ... & Beck Jr, L. H. (2021). Serine protease HTRA1 as a novel target antigen in primary membranous nephropathy. Journal of the American Society of Nephrology: JASN, 32(7), 1666.

Malik, R., Beaufort, N., Frerich, S., Gesierich, B., Georgakis, M. K., Rannikmäe, K., ... & Dichgans, M. (2021). Whole-exome sequencing reveals a role of HTRA1 and EGFL8 in brain white matter hyperintensities. Brain, 144(9), 2670-2682.

Williams, B. L., Seager, N. A., Gardiner, J. D., Pappas, C. M., Cronin, M. C., Amat di San Filippo, C., ... & Hageman, G. S. (2021). Chromosome 10q26–driven age-related macular degeneration is associated with reduced levels of HTRA1 in human retinal pigment epithelium. Proceedings of the National Academy of Sciences, 118(30), e2103617118.

Uemura, M., Nozaki, H., Kato, T., Koyama, A., Sakai, N., Ando, S., ... & Onodera, O. (2020). HTRA1-related cerebral small vessel disease: a review of the literature. Frontiers in neurology, 545.

Fasano, A., Formichi, P., Taglia, I., Bianchi, S., Di Donato, I., Battisti, C., ... & Dotti, M. T. (2020). HTRA1 expression profile and activity on TGF‐β signaling in HTRA1 mutation carriers. Journal of Cellular Physiology, 235(10), 7120-7127.

Zellner, A., Scharrer, E., Arzberger, T., Oka, C., Domenga-Denier, V., Joutel, A., ... & Haffner, C. (2018). CADASIL brain vessels show a HTRA1 loss-of-function profile. Acta neuropathologica, 136, 111-125.

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

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