Anti-Pink1 PTEN Induced Putative Kinase 1 Recombinant Chicken Chimeric mAb Biotin Conjugate (N4/15)
Our chicken Pink1 PTEN induced putative kinase 1 biotin conjugate recombinant antibody from Aves Labs is produced in-house from clone N4/15. It detects human, mouse, and rat Pink1 PTEN induced putative kinase 1 and is purified by affinity chromatography. Works in ELISA, IHC, ICC, WB.
Human, Mouse, Rat
ELISA, ICC, IHC, WB
Chicken
SKU: 78-060-BTN
Ships: 1-5 business days
Product Details
Pink1 PTEN induced putative kinase 1
PTEN Induced Kinase 1 is encoded by the gene PINK1. PINK1 is a member of the protein kinase superfamily, Ser/Thr protein kinase family. PINK1 is a serine/threonine protein kinase that protects against mitochondrial dysfunction during cellular stress by phosphorylating mitochondrial proteins. PINK1 is highly expressed in the heart, skeletal muscle, and testis. Diseases associated with PINK1 include Parkinson Disease 6, Autosomal Recessive Early-Onset and Parkinson Disease 2, Autosomal Recessive Juvenile.
Purified by affinity chromatography
Lot dependent: provided at 0.3-0.5 mg/mL
Recombinant
N4/15
IgY
ELISA, ICC, IHC, WB
Chicken
PINK1
63 kDa
Fusion Protein Amino acids 112-496 of human Pink1 (accession number NP_115785) produced recombinantly in E. Coli
Human
Human, Mouse, Rat
Aliquot and store at ≤ -20°C for long term storage. For short term storage, store at 2-8°C. For maximum recovery of product, centrifuge the vial prior to removing the cap.
Liquid
This recombinant antibody is a chimeric antibody created by replacing the mouse heavy and light constant regions of clone N4/15 with chicken IgY heavy and light constant regions. As such this antibody retains the same binding performance as the original clone N4/15 but can be detected using standard anti-chicken secondary antibodies allowing flexibility for multiplexing applications. This antibody is expressed recombinantly in mammalian cells and then affinity purified from the cell culture media.
1X PBS, 0.05% Sodium Azide pH 7.4
IHC: 1:200-1:1000
ICC: 1:200-1:1000
ICC: 1:200-1:1000
Biotin
No cross-reactivity reported
These antibodies are to be used as research laboratory reagents and are not for use as diagnostic or therapeutic reagents in humans.
United States
12 months from date of receipt
BRPK; Serine/threonine-protein kinase PINK1; PTEN-induced putative kinase protein 1; EC 2.7.11.1; protein kinase BRPK; mitochondrial
Q9BXM7
UniProt Summary: Serine/threonine-protein kinase which acts as a sensor of mitochondrial damage and protects against mitochondrial dysfunction during cellular stress. It phosphorylates mitochondrial proteins to coordinate mitochondrial quality control mechanisms that remove and replace dysfunctional mitochondrial components. In healthy mitochondria, PINK1 is translocated across the mitochondrial outer membrane (MOM) via the translocase of the outer membrane (TOM) complex, and inserted into the mitochondrial inner membrane (MIM) via the translocase of the inner membrane (TIM23) complex where it is cleaved and released into the cytosol. Depending on the severity of mitochondrial damage, activity ranges from preventing apoptosis and stimulating mitochondrial biogenesis to eliminating severely damaged mitochondria via PINK1-PRKN-dependent mitophagy. When cellular stress results in irreversible mitochondrial damage, PINK1 accumulates at the outer mitochondrial membrane (OMM) where it phosphorylates pre-existing polyubiquitin chains at 'Ser-65', recruits PRKN from the cytosol to the OMM and activates PRKN by phosphorylation at 'Ser-65'; activated PRKN then ubiquitinates VDAC1 and other OMM proteins to initiate mitophagy. The PINK1-PRKN pathway also promotes fission of damaged mitochondria through phosphorylation and PRKN-dependent degradation of mitochondrial proteins involved in fission such as MFN2. This prevents the refusion of unhealthy mitochondria with the mitochondrial network or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes. Also promotes mitochondrial fission independently of PRKN and ATG7-mediated mitophagy, via the phosphorylation and activation of DNM1L. Regulates motility of damaged mitochondria by promoting the ubiquitination and subsequent degradation of MIRO1 and MIRO2; in motor neurons, this likely inhibits mitochondrial intracellular anterograde transport along the axons which probably increases the chance of the mitochondria undergoing mitophagy in the soma. Required for ubiquinone reduction by mitochondrial complex I by mediating phosphorylation of complex I subunit NDUFA10. Phosphorylates LETM1, positively regulating its mitochondrial calcium transport activity.
UniProt Summary: Serine/threonine-protein kinase which acts as a sensor of mitochondrial damage and protects against mitochondrial dysfunction during cellular stress. It phosphorylates mitochondrial proteins to coordinate mitochondrial quality control mechanisms that remove and replace dysfunctional mitochondrial components. In healthy mitochondria, PINK1 is translocated across the mitochondrial outer membrane (MOM) via the translocase of the outer membrane (TOM) complex, and inserted into the mitochondrial inner membrane (MIM) via the translocase of the inner membrane (TIM23) complex where it is cleaved and released into the cytosol. Depending on the severity of mitochondrial damage, activity ranges from preventing apoptosis and stimulating mitochondrial biogenesis to eliminating severely damaged mitochondria via PINK1-PRKN-dependent mitophagy. When cellular stress results in irreversible mitochondrial damage, PINK1 accumulates at the outer mitochondrial membrane (OMM) where it phosphorylates pre-existing polyubiquitin chains at 'Ser-65', recruits PRKN from the cytosol to the OMM and activates PRKN by phosphorylation at 'Ser-65'; activated PRKN then ubiquitinates VDAC1 and other OMM proteins to initiate mitophagy. The PINK1-PRKN pathway also promotes fission of damaged mitochondria through phosphorylation and PRKN-dependent degradation of mitochondrial proteins involved in fission such as MFN2. This prevents the refusion of unhealthy mitochondria with the mitochondrial network or initiates mitochondrial fragmentation facilitating their later engulfment by autophagosomes. Also promotes mitochondrial fission independently of PRKN and ATG7-mediated mitophagy, via the phosphorylation and activation of DNM1L. Regulates motility of damaged mitochondria by promoting the ubiquitination and subsequent degradation of MIRO1 and MIRO2; in motor neurons, this likely inhibits mitochondrial intracellular anterograde transport along the axons which probably increases the chance of the mitochondria undergoing mitophagy in the soma. Required for ubiquinone reduction by mitochondrial complex I by mediating phosphorylation of complex I subunit NDUFA10. Phosphorylates LETM1, positively regulating its mitochondrial calcium transport activity.
65018
Shipped on ice packs

