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PARK2 protein, human

The PARK2 gene encodes the Parkin protein, which plays a crucial role in mitochondrial homeostasis and is associated with the development of Parkinson's disease.
Parkin functions as an E3 ubiquitin ligase, regulating the turnover of damaged mitochondria through a process called mitophagy.
Mutations in the PARK2 gene can lead to an autosomal recessive form of early-onset Parkinson's disease.
Understandig the biology of the PARK2 protein is essential for advancing research into Parkinson's disease pathogenesis and developing potential therapeutic interventions.
Leverageing AI-powered platforms like PubCompare.ai can help optimize experimental protocols and enhance the reproducibility of PARK2 protein research.

Most cited protocols related to «PARK2 protein, human»

Confocal Imaging of Mitophagy Dynamics

Cited 40 times

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Publication 2015

Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone Cell Lines Cells DAPI Epistropheus Fluorescence HeLa Cells Hyperostosis, Diffuse Idiopathic Skeletal Lens, Crystalline Microscopy, Confocal Mitophagy neuro-oncological ventral antigen 2, human Oligomycins PARK2 protein, human Penicillins Streptomycin Student Submersion Tissues Training Programs Triton X-100 Vision

Genetic Screening for Familial Parkinson's Disease

Cited 17 times

PD cases negative for the LRRK2 G2019S mutation (n = 935) were selected from two ongoing studies of familial PD. Additional genes, such as PARK2 (parkin), PARK7 (DJ1), and NR4A2, were screened for many, but not all subjects (Foroud et al. 2003 (link); Karamohamed et al. 2005 (link); Nichols et al. 2004 (link), 2007 (link); Pankratz et al. 2006 (link); Sun et al. 2006 (link)); no subjects were included who had known disease producing mutation(s). Both studies (PROGENI and GenePD) initially ascertained multiplex PD families consisting of at least a sibling pair, both of whom were reported to be affected with PD. In a small proportion (9%), the PD case may have had another affected relative rather than an affected sibling. On average, each PD participant had an additional 1.8 relatives who were reported to have PD. Only a single individual per family was genotyped ensuring sample independence. Both studies ascertained primarily Caucasian, non-Hispanic participants. PD cases underwent a uniform neurological evaluation that employed PD diagnostic criteria based broadly on the United Kingdom PD Society Brain Bank Criteria (Gibb and Lees 1988 (link)), although modified by both studies. A detailed description of the inclusion and exclusion criteria has been previously published for both the PROGENI (Pankratz et al. 2002 (link)) and GenePD (Maher et al. 2002 (link)) studies.
Control samples (n = 895) were obtained from the NINDS Human Genetics Resource Center at the Coriell Institute Coriell Cell Repositories (Camden, NJ); older individuals were preferentially selected in an effort to have the mean age at recruitment of the controls be similar to the mean age at onset of the PD cases. All selected control samples were reported to be Caucasian, non-Hispanic. Based on self-report, the control subjects did not have a personal history of PD, and none reported a positive family history of PD (family history data was available for 91% of controls). Appropriate written informed consent was obtained for all samples included in this study.

Pankratz N., Wilk J.B., Latourelle J.C., DeStefano A.L., Halter C., Pugh E.W., Doheny K.F., Gusella J.F., Nichols W.C., Foroud T, & Myers R.H. (2008). Genomewide association study for susceptibility genes contributing to familial Parkinson disease. Human genetics, 124(6), 593-605.

Publication 2008

Brain Caucasoid Races Cells Diagnosis Family Member Genes Hispanics LRRK2 protein, human Manpower Mutation Neurologic Examination PARK2 protein, human PARK7 protein, human Parkinson Disease 2, Autosomal Recessive Juvenile

Estimating Cancer Burden Attributable Factors

Cited 16 times

PAFs for all risk factors combined, for each cancer type and for all cancers combined, were obtained by first applying the first relevant PAF in the sequence shown in Table 1 to the total number of observed cases, to obtain the number of cases attributable to that factor only. The order of risk factors within the sequence does not affect the result of the sum, the order in Table 1 runs from highest to lowest UK PAF within males, females and persons separately. Each subsequent PAF in the sequence was applied only to the number of observed cases not yet explained by the risk factors earlier in the sequence, as described by Parkin et al.^{26 (link)} Though the RRs used in the PAFs calculations are generally adjusted and therefore should represent only the effect of the specific risk factor in isolation, residual confounding remains possible. This aggregation method avoids overestimating PAFs for all risk factors combined but does not account for cases caused by exposure to risk factors in combination, e.g. the synergistic effect of tobacco and alcohol on oesophageal cancer risk, or of HPV and tobacco smoking on cervical cancer risk.Table 1

Summary population attributable fractions and attributable cases, by risk factor, sex and country, 2015

	All cancers excluding non-melanoma skin cancer (ICD-10 C00-C97 excluding C44), 2015
	England		Scotland		Wales		Northern Ireland		UK
	PAF (%)	Attrib. cases	PAF (%)	Attrib. cases	PAF (%)	Attrib. cases	PAF (%)	Attrib. cases	PAF (%)	Attrib. cases
Males
Cancer incidence	152,891		15,184		9,837		4,650		182,562
Tobacco smoking	17.3	26,375	21.1	3,204	18.6	1,832	17.8	830	17.7	32,242
Overweight and obesity	5.2	7,960	6.0	909	4.6	450	5.3	248	5.2	9,567
Occupation	4.9	7,458	5.8	875	5.3	520	5.0	234	5.0	9,087
Radiation—UV	3.9	5,899	3.9	587	3.7	364	3.8	174	3.8	7,025
Insufficient fibre	3.1	4,713	3.5	529	3.3	322	3.7	171	3.1	5,735
Alcohol	3.0	4,634	3.8	572	3.2	319	3.5	164	3.1	5,689
Infections	3.0	4,539	4.0	608	2.8	279	3.8	178	3.1	5,605
Processed meat	2.0	3,096	2.3	346	2.1	204	2.4	112	2.1	3,758
Radiation—ionising	1.7	2,675	1.6	239	2.0	196	1.7	80	1.7	3,190
Air pollution	1.1	1,636	1.0	146	0.8	82	0.8	38	1.0	1,901
Insufficient physical activity	0.5	794	0.6	85	0.5	51	0.6	27	0.5	957
All of the above	38.0	58,141	43.3	6,567	39.0	3,838	39.9	1,856	38.6	70,425
Females
Cancer incidence	146,862		16,266		9,251		4,606		176,985
Tobacco smoking	12.1	17,738	15.6	2,532	13.4	1,241	11.3	519	12.4	22,029
Overweight and obesity	7.5	11,036	7.6	1,244	6.4	590	7.0	324	7.5	13,194
Infections	4.0	6,083	5.1	832	3.9	364	4.4	202	4.2	7,481
Radiation—UV	3.8	5,541	3.5	570	3.4	311	3.4	157	3.7	6,579
Alcohol	3.5	5,202	3.3	538	3.3	301	3.5	163	3.5	6,205
Insufficient fibre	3.3	4,917	3.5	564	3.4	316	3.5	161	3.4	5,958
Occupation	2.4	3,528	2.8	462	2.6	241	2.5	114	2.5	4,338
Radiation—ionising	2.1	3,128	1.9	314	2.4	221	2.2	100	2.1	3,764
Not breastfeeding	1.4	2,117	1.5	248	1.4	132	1.9	86	1.5	2,582
Air pollution	1.0	1,442	0.9	142	0.8	74	0.7	32	1.0	1,690
Processed meat	0.9	1,330	0.9	145	0.8	73	1.0	46	0.9	1,594
Postmenopausal hormones	0.7	1,089	0.8	132	1.2	107	0.9	43	0.8	1,371
Insufficient physical activity	0.5	801	0.5	86	0.5	49	0.5	25	0.5	959
Oral contraceptives	0.5	667	0.5	79	0.3	32	0.7	30	0.5	807
All of the above	36.4	53,480	39.7	6,455	36.5	3,373	36.1	1,663	36.8	65,130
Persons
Cancer incidence	299,753		31,450		19,088		9,256		359,547
Tobacco smoking	14.7	44,113	18.2	5,736	16.1	3,073	14.6%	1,349	15.1	54,271
Overweight and obesity	6.3	18,996	6.8	2,153	5.4%	1,040	6.2	572	6.3	22,761
Radiation—UV	3.8	11,440	3.7	1,157	3.5	675	3.6	332	3.8	13,604
Occupation	3.7	11,078	4.4	1,373	4.0	765	3.8	353	3.8	13,558
Infections	3.5	10,622	4.6	1,441	3.4	643	4.1	380	3.6	13,086
Alcohol	3.3	9,836	3.5	1,110	3.3	621	3.5	327	3.3	11,894
Insufficient fibre	3.2	9,630	3.5	1,093	3.3	638	3.6	332	3.3	11,693
Radiation—ionising	1.9	5,803	1.8	553	2.2	417	1.9	180	1.9	6,954
Processed meat	1.5	4,426	1.6	490	1.4	276	1.7	159	1.5	5,352
Air pollution	1.0	3,078	0.9	288	0.8	156	0.8	70	1.0	3,591
Not breastfeeding	0.7	2,117	0.8	248	0.7	132	0.9	86	0.7	2,582
Insufficient physical activity	0.5	1,595	0.5	171	0.5	100	0.6	51	0.5	1,917
Postmenopausal hormones	0.4	1,089	0.4	132	0.6	107	0.5	43	0.4	1,371
Oral contraceptives	0.2	667	0.2	79	0.2	32	0.3	30	0.2	807
All of the above	37.3	111,722	41.5	13,038	37.8	7,207	38.0	3,519	37.7	135,507

Brown K.F., Rumgay H., Dunlop C., Ryan M., Quartly F., Cox A., Deas A., Elliss-Brookes L., Gavin A., Hounsome L., Huws D., Ormiston-Smith N., Shelton J., White C, & Parkin D.M. (2018). The fraction of cancer attributable to modifiable risk factors in England, Wales, Scotland, Northern Ireland, and the United Kingdom in 2015. British Journal of Cancer, 118(8), 1130-1141.

Publication 2018

Cervical Cancer Esophageal Cancer Ethanol Familial Atypical Mole-Malignant Melanoma Syndrome Females isolation Males Malignant Neoplasms PARK2 protein, human Physical Examination Radiotherapy Tobacco Products

Cited 15 times

pMXs-puro-GFP-WIPI1 and pMXs-puro-GFP-DFCP1 were a kind gift from Dr. N. Mizushima (University of Toyko, Japan) and pMXs-IP-GFP-ULK1 was purchased from Addgene (#38193). To generate pBMN-mEGFP-C1, mEGFP-C1 (Addgene #36412) was PCR amplified (together with the multiple cloning site) and cloned into pBMN-Z at BamHI/SalI sites using the Gibson Cloning kit (New England BioLabs) according to manufacturer's instructions. The BamHI and SalI sites used to insert mEGFP-C1 were not regenerated. The following GFP-tagged plasmids were generated by PCR amplification of open reading frames followed by ligation into pBMN-mEGFP-C1: OPTN, NDP52, p62, TAX1BP1, NBR1, LC3A, LC3B, LC3C, GABARAP, GABARAPL1, GABARAPL2. The Gateway Cloning (Invitrogen) system was used to generate GFP-, mCherry-, myc- and FLAG/HA-constructs. Briefly, TBK1, TBK1-K38M, NDP52, OPTN, p62, DFCP1, WIPI1 and ULK1 were cloned into pDONR2333. Mutations in cDNA sequences were introduced using PCR site directed mutagenesis in the pDONR2333 vector, (sequences of mutagenesis primers used are available upon request) then recombined into pHAGE-N-FLAG/HA, pHAGE-N-GFP, pHAGE-N-mCherry and/or pDEST-N-myc using LR Clonase (Invitrogen) as per the manufacturer's protocol. All constructs generated in this study were verified by sequencing.
To generate stably transfected cell lines, retroviruses (for pBMN-mEGFP-C1 constructs, pBMN-mCherry-Parkin, pBMN-puro-P2A-FRB-Fis1, pCHAC-mt-mKeima-IRES-MCS2) and lentiviruses (for pHAGE- and pDEST- constructs) were packaged in HEK293T cells. HeLa cells were transduced with virus for 24 h with 8 μg/ml polybrene (Sigma) then optimized for protein expression via selection (puromycin or blasticidin) or fluorescence sorting.

Lazarou M., Sliter D.A., Kane L.A., Sarraf S.A., Wang C., Burman J.L., Sideris D.P., Fogel A.I, & Youle R.J. (2015). The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy. Nature, 524(7565), 309-314.

Publication 2015

Bacteriophages Cell Lines Cells Cloning Vectors DNA, Complementary Fluorescence HeLa Cells Internal Ribosome Entry Sites Lentivirus Ligation Mutagenesis Mutagenesis, Site-Directed Mutation Oligonucleotide Primers Open Reading Frames PARK2 protein, human Plasmids Polybrene Proteins Puromycin Retroviridae TBK1 protein, human ULK1 protein, human Virus

Comprehensive Cell Culture and Antibody Protocol

Cited 14 times

HEK293T, HeLa and PINK1 KO³⁵ cells were cultured in Dulbecco's modified eagle medium (Life Technologies) supplemented with 10% (v/v) Fetal Bovine Serum (Gemini Bio Products), 10 mM HEPES (Life Technologies), 1 mM Sodium Pyruvate (Life Technologies), nonessential amino acids (Life Technologies) and GlutaMAX (Life Technologies). HeLa cells were acquired from the ATCC and authenticated by the Johns Hopkins GRCF Fragment Analysis Facility using STR profiling. All cells were tested for mycoplasma contamination bimonthly using the PlasmoTest kit (InvivoGen). Transfection reagents used were: Effectene (Qiagen), Lipofectamine LTX (Life Technologies), Avalanche-OMNI (EZ Bio-systems), X-tremeGENE HP (Roche) and X-tremeGENE 9 (Roche).
Rabbit monoclonal and polyclonal antibodies used: Beclin, pULK1-S317, pULK1-S757, TBK1, pTBK1-S172, NDP52, TAX1BP1, ATG5, Actin, and HA (Cell Signaling Technologies); GAPDH and LC3B (Sigma); ULK1 and Tom20 (Santa Cruz Biotechnology); Optineurin (OPTN) (Proteintech); GFP (Life Technologies); pSer65 ubiquitin (Millipore) and Mfn1 was generated previously^{36 (link)}. Mouse monoclonal antibodies used: NBR1 and p62 (Abnova), Cytochrome C oxidase subunit II (CoxII, Abcam), Parkin (Santa Cruz Biotechnology), DNA (Progen Biotechnik), ubiquitin (Cell Signaling). Chicken anti-GFP (Life Technologies) was also used. For catalog numbers see Supplementary Table 1. Human tissue panel blots were purchased (NOVUS Biologicals).

Publication 2015

Actins Amino Acids Antibodies Avalanches Biological Factors Cells Chickens Culture Media cytochrome C oxidase subunit II Eagle Effectene Fetal Bovine Serum GAPDH protein, human HeLa Cells HEPES Homo sapiens Lipofectamine Monoclonal Antibodies Mus Mycoplasma Novus OPTN protein, human PARK2 protein, human Progens PTGS2 protein, human Pyruvate Rabbits Sodium TBK1 protein, human Tissues Transfection Ubiquitin ULK1 protein, human

Most recents protocols related to «PARK2 protein, human»

Temporal Trends of AYA Stomach Cancer

As previously defined by AYA oncology, the study age group was 15–39 years (28 (link)). Based on the GBD 2019 study, data on stomach cancer burden among AYA patients were extracted at global, regional, and national levels for both sexes from 1990 to 2019. Cancer data were structured according to age groups (15–19, 20–24, 25–29, 30–34, and 35–39 years-old). The total number of incidence cases, deaths, and DALYs in all related aged groups (15–19 years to 35–39 years) were calculated. The truncated age standardized rates were computed using age-specific rate for age-groups, weighed using the GBD 2019 world standard population (24 (link)), according to methods proposed by Boyle and Parkin (29 (link)).
The outcomes were presented at the global, regional, and national levels for AYA stomach cancer. The SDI was analyzed using the LOWESS regression method to determine its association with age-standardized incidence, death, and DALY rates. With regard to the cancer burden, uncertainty exists owing to the diversity in availability and quality. Based on the 2.5th and 97.5th percentiles of the allocation of 1,000 draws within the Bayesian modeling, 95% uncertainty intervals (95% UI) were calculated in conjunction with evaluations of cancer burden.
The Joinpoint regression program, version 4.9.1.0 (Statistical Research and Applications Branch, National Cancer Institute, Bethesda, MD), was used to calculate the annual percent changes (APCs) and 95% confidence intervals (CIs) in age-standardized rates as described (30 (link)).

Zhang Z., Wang J., Song N., Shi L, & Du J. (2023). The global, regional, and national burden of stomach cancer among adolescents and young adults in 204 countries and territories, 1990–2019: A population-based study. Frontiers in Public Health, 11, 1079248.

Publication 2023

Age Groups Gastric Cancer Malignant Neoplasms Neoplasms PARK2 protein, human Patients

Western Blot Analysis of Mitochondrial Proteins

Mitochondrial, cytoplasmic and total proteins were extracted, and the corresponding kit (Beyotime) was used to detect the content. Thereafter, 25 µg of protein was subjected to sodium dodecylsulfate-polyacrylamide gel electrophoresis. The protein was transferred to a polyvinylidene fluoride film (Millipore, Billerica, Massachusetts, USA) using a semidry method. The polyvinylidene fluoride film was soaked in TBST containing 5% skimmed milk powder and sealed with a shaker for 2 h at room temperature. The blots were incubated overnight, with the primary antibodies diluted from 1:500 to 1:1000. The antibodies were used against the proteins listed below: Parkin (ab77924), PINK1 (ab23707), Bax (ab32503), Bcl-2 (ab32124), Cyt-c (ab110325), Collagen II (ab34712), Adamts5(ab41037) (Abcam, Cambridge, UK); P62 (#5114), LC3 (#2775), SIRT3 (#2627S), GAPDH (#5174), Caspase-3 (#9662) and Cleaved-Caspase-3 (#9664) (Cell Signaling Technology; Danvers, Massachusetts, USA); VDAC1 (sc-32063) (Santa Cruz Biotechnology; Dallas, Texas, USA); Aggrecan (13880-1-AP) and MMP3 (17873-1-AP) (Wuhan Sanying, Wuhan, China). After rinsing the film, the proper secondary antibody was incubated through the blot for 1 h at 25 °C. The film’s gray values were analyzed after darkroom exposure using Image J software v1.46 (NIH, Bethesda, MD, USA).

Liu W., Zhao X, & Wu X. (2023). Duhuo Jisheng Decoction suppresses apoptosis and mitochondrial dysfunction in human nucleus pulposus cells by miR-494/SIRT3/mitophagy signal axis. Journal of Orthopaedic Surgery and Research, 18, 177.

Publication 2023

Aggrecans Antibodies BCL2 protein, human CASP3 protein, human Collagen Cytoplasm GAPDH protein, human Immunoglobulins Milk, Cow's Mitochondria MMP3 protein, human PARK2 protein, human polyvinylidene fluoride Powder Proteins SDS-PAGE Sirtuin 3 VDAC1 protein, human

Ovariectomy-induced Osteoporosis Model

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Publication 2023

Acetylcysteine Actins Adenosine Triphosphatases Animals Antibodies Antioxidants Autophagosome Autophagy bafilomycin A1 Bone Marrow CDKN1A protein, human CDKN2A Gene Female Castrations Females Femur Fluorescein-5-isothiocyanate Genistein Goat leptin receptor, human Lysosomes Mus Operative Surgical Procedures Ovary Oxidative Stress PARK2 protein, human Penicillins PPARGC1A protein, human Protoplasm Rabbits Rats, Sprague-Dawley Rattus norvegicus Sirtuin 3 Streptomycin Tibia Vacuolar H+-ATPase

Immunofluorescence Analysis of DNA Damage

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Publication 2023

Antibodies Biological Assay Biopharmaceuticals Cell Nucleus Cells Culture Media, Conditioned DAPI Fluorescent Antibody Technique Gelatins Goat Microscopy, Fluorescence paraform PARK2 protein, human Proteins Serum Triton X-100

Immunoprecipitation and Western Blot Analysis

Cells were lysed on ice for 20 min in a buffer containing 1% Triton X-100, 10 mM Tris (pH 7.6), 50 mM NaCl, 30 mM sodium pyrophosphate, 50 mM NaF, 5 mM EDTA, protease inhibitor cocktail (Roche), and phosphatase inhibitor cocktail (Roche). The resulting lysates were centrifuged at 16,000 × g at 4 °C, and the supernatant fraction was incubated with antibodies against FLAG (Cell Signaling Technology), and HDAC6 (Cell Signaling Technology) for 2 h at 4 °C, followed by incubation with Protein G Plus Agarose (Merck Millipore). Immunoprecipitants were washed two times with the lysis buffer, boiled in 5× SDS loading buffer for 10 min, followed by separation on SDS-PAGE and analysis by western blot. Western blot analysis was performed as described above. For inflammatory IL-1β-induced protein interaction, WT or Parkin^−/− OCPs were cultured for 3 days with 10 ng/ml of IL-1β in the presence of RANKL and M-CSF. Then, the anti-HDAC6 immunoprecipitation was performed.

Kim E.Y., Kim J.E., Kim Y.E., Choi B., Sohn D.H., Park S.O., Chung Y.H., Kim Y., Robinson W.H., Kim Y.G, & Chang E.J. (2023). Dysfunction in parkin aggravates inflammatory bone erosion by reinforcing osteoclast activity. Cell & Bioscience, 13, 48.

Publication 2023

Antibodies Buffers Cells Edetic Acid G-substrate Immunoprecipitation Inflammation Interleukin-1 beta Interleukin-10 Macrophage Colony-Stimulating Factor Ocular Cicatricial Pemphigoid PARK2 protein, human Phosphoric Monoester Hydrolases Protease Inhibitors Proteins SDS-PAGE Sepharose Sodium Chloride sodium pyrophosphate TNFSF11 protein, human Triton X-100 Tromethamine Western Blot

Top products related to «PARK2 protein, human»

Parkin by Cell Signaling Technology

Sourced in United States, United Kingdom, China

Parkin is a protein that plays a role in regulating the ubiquitin-proteasome system, a cellular process involved in the degradation of damaged or unnecessary proteins. Parkin functions as an E3 ubiquitin ligase, which attaches ubiquitin molecules to target proteins, marking them for destruction by the proteasome.

Lipofectamine 2000 by Thermo Fisher Scientific

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Lipofectamine 2000 is a cationic lipid-based transfection reagent designed for efficient and reliable delivery of nucleic acids, such as plasmid DNA and small interfering RNA (siRNA), into a wide range of eukaryotic cell types. It facilitates the formation of complexes between the nucleic acid and the lipid components, which can then be introduced into cells to enable gene expression or gene silencing studies.

Parkin by Abcam

Sourced in United States, United Kingdom, Japan

Parkin is a protein that plays a role in the regulation of mitochondrial function and quality control. It is involved in the process of mitophagy, which is the selective degradation of damaged or dysfunctional mitochondria by the autophagy pathway.

Parkin by Santa Cruz Biotechnology

Sourced in United States

Parkin is a lab equipment product from Santa Cruz Biotechnology. It is a protein that plays a role in the regulation of mitochondrial function and quality control.

Pvdf membrane by Merck Group

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Ab23707 by Abcam

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Ab23707 is a mouse monoclonal antibody that recognizes an epitope within the C-terminus of the human Insulin Receptor (INSR) protein. This antibody is designed for use in various immunoassay applications to detect and quantify INSR levels in biological samples.

Pink1 by Abcam

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PINK1 is a lab equipment product manufactured by Abcam. It is a serine/threonine-protein kinase that plays a role in the regulation of mitochondrial function and quality control.

Ab77924 by Abcam

Sourced in United States, United Kingdom, China

Ab77924 is a laboratory equipment product. It is a device designed for use in scientific research and laboratory settings. The core function of this product is to facilitate specific tasks or procedures within the laboratory environment. No further details can be provided in an unbiased and factual manner.

Fetal bovine serum (fbs) by Thermo Fisher Scientific

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Fetal Bovine Serum (FBS) is a cell culture supplement derived from the blood of bovine fetuses. FBS provides a source of proteins, growth factors, and other components that support the growth and maintenance of various cell types in in vitro cell culture applications.

Anti parkin by Cell Signaling Technology

Sourced in United States, China

Anti-Parkin is a research antibody product that specifically binds to the Parkin protein, which is involved in the regulation of mitochondrial function and quality control. This antibody can be used to detect and study the Parkin protein in various experimental systems.

What are the key functions of the PARK2 protein in the human body?

The PARK2 gene encodes the Parkin protein, which plays a crucial role in mitochondrial homeostasis. Parkin functions as an E3 ubiquitin ligase, regulating the turnover of damaged mitochondria through a process called mitophagy. This process helps maintain healthy mitochondria and is essential for cellular function. Mutations in the PARK2 gene can lead to an autosomal recessive form of early-onset Parkinson's disease, highlighting the importance of the PARK2 protein in neuronal health and disease pathogenesis.

How can PubCompare.ai help researchers working with the PARK2 protein?

PubCompare.ai allows researchers to screen protocol literature more efficiently and leverage AI to pinpoint critical insights. The platform's AI-driven analysis can help identify the most effective protocols related to PARK2 protein research for your specific goals. By highlighting key differences in protocol effectiveness, PubCompare.ai enables researchers to choose the best option for reproducibility and accuracy, streamlining the research process and enhancing experimental success.

Are there any common usage challenges associated with the PARK2 protein?

One potential challenge with working with the PARK2 protein is ensuring reproducibility of experimental results. Due to the complex nature of mitochondrial biology and the role of Parkin in mitophagy, slight variations in experimental protocols can lead to divergent outcomes. This is where PubCompare.ai can be particularly helpful - the platform's AI-powered analysis can help researchers identify the most robust and reliable protocols, reducing the risk of irreproducible results and enhancing the overall quality of PARK2 protein research.

Are there different variations or types of the PARK2 protein that researchers should be aware of?

The PARK2 gene can have various mutations that result in different forms or variants of the Parkin protein. These mutant forms of Parkin can have altered functionlaity and are associated with the development of early-onset Parkinson's disease. Researchers studying the PARK2 protein need to be mindful of these different variants and how they may impact mitochondrial homeostasis and cellular health. PubCompare.ai can assist in this process by helping researchers identify the most relevant and well-characterized PARK2 protein variants for their specific research objectives.

What are some specific applications of the PARK2 protein in research and therapeutics?

The PARK2 protein is a key target for Parkinson's disease research, as mutations in the PARK2 gene are a leading cause of early-onset Parkinson's. Understanding the biology of the PARK2 protein and its role in mitophagy is essential for advancing our understanding of Parkinson's disease pathogenesis and developing potential therapeutic interventions. PARK2 protein research may also have broader applications in the field of mitochondrial biology and neurodegenerative diseases. PubCompare.ai can help researchers in this area by optimizing their experimental protocols and enhancing the reproducibility of their findings.

More about "PARK2 protein, human"

The PARK2 gene encodes the Parkin protein, a crucial player in maintaining mitochondrial homeostasis and a key factor in the development of Parkinson's disease.
Parkin functions as an E3 ubiquitin ligase, regulating the turnover of damaged mitochondria through a process called mitophagy.
Mutations in the PARK2 gene can lead to an autosomal recessive form of early-onset Parkinson's disease.
Understanding the biology of the PARK2/Parkin protein is essential for advancing research into Parkinson's disease pathogenesis and developing potential therapeutic interventions.
Leveraging AI-powered platforms like PubCompare.ai can help optimize experimental protocols and enhance the reproducibility of PARK2/Parkin protein research.
PubCompare.ai's AI-driven platform can assist researchers in locating the best protocols from literature, pre-prints, and patents, while utilizing real-time comparisons to identify the most effective products, such as Lipofectamine 2000 transfection reagent and PVDF membranes.
This can help streamline the research process and achieve greater experimental success.
Additionally, related proteins like PINK1 and their interaction with Parkin are also crucial for understanding mitochondrial quality control and Parkinson's disease.
Antibodies like Ab23707 and Ab77924 can be utilized to study the expression and localization of these proteins.
Supplementing cell culture experiments with fetal bovine serum (FBS) can also provide a more physiologically relevant environment for studying Parkin and its role in mitochondrial dynamics.
By leveraging the power of AI and optimizing experimental protocols, researchers can advance their understanding of the PARK2/Parkin protein and its implication in Parkinson's disease, ultimately paving the way for potential therapeutic interventions.