Recombinant Human Cyclin-Dependent Kinase 5 Activator 1 (CDK5R1) Protein (His)

Name: Recombinant Human Cyclin-Dependent Kinase 5 Activator 1 (CDK5R1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-01213P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Cyclin-Dependent Kinase 5 Activator 1 (CDK5R1) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q15078
Target Symbol	CDK5R1
Synonyms	(CDK5 activator 1)(Cyclin-dependent kinase 5 regulatory subunit 1)(TPKII regulatory subunit)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	AQPPPAQPPAPPASQLSGSQTGGSSSVKKAPHPAVTSAGTPKRVIVQASTSELLRCLGEFLCRRCYRLKHLSPTDPVLWLRSVDRSLLLQGWQDQGFITPANVVFLYMLCRDVISSEVGSDHELQAVLLTCLYLSYSYMGNEISYPLKPFLVESCKEAFWDRCLSVINLMSSKMLQINADPHYFTQVFSDLKNESGQEDKKRLLLGLDR
Expression Range	99-307aa
Protein Length	Partial
Mol. Weight	27.3 kDa
Research Area	Cell Biology
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	p35 is a neuron specific activator of CDK5. The complex p35/CDK5 is required for neurite outgrowth and cortical lamination. Involved in dendritic spine morphogenesis by mediating the EFNA1-EPHA4 signaling. Activator of TPKII. The complex p35/CDK5 participates in the regulation of the circadian clock by modulating the function of CLOCK protein: phosphorylates CLOCK at 'Thr-451' and 'Thr-461' and regulates the transcriptional activity of the CLOCK-ARNTL/BMAL1 heterodimer in association with altered stability and subcellular distribution.
Subcellular Location	[Cyclin-dependent kinase 5 activator 1, p35]: Cell membrane; Lipid-anchor; Cytoplasmic side. Cell projection, neuron projection.; [Cyclin-dependent kinase 5 activator 1, p25]: Nucleus. Cytoplasm, perinuclear region. Perikaryon.
Protein Families	Cyclin-dependent kinase 5 activator family
Database References	HGNC: 1775 OMIM: 603460 KEGG: hsa:8851 STRING: 9606.ENSP00000318486 UniGene: PMID: 29997370 the downregulation of the miR-15/107 family might have a role in the pathogenesis of AD by increasing the levels of CDK5R1/p35 and consequently enhancing CDK5 activity. PMID: 27343180 It is shown that p5 binds the kinase at the same CDK5/p25 and CDK5/p35 interfaces, and is thus a non-selective competitor of both activators, in agreement with available experimental data in vitro. PMID: 27387995 the minor allele of CDK5R1 3'-UTR rs735555 polymorphism was associated with increased risk for NS-ID. In conclusion, our data suggest that mutations and polymorphisms in CDK5 and CDK5R1 genes may contribute to the onset of the NS-ID phenotype PMID: 26657932 Under cell-free in vitro conditions, p35 is covalently modified by SUMO1. SUMO2 is conjugated to p35 in cells. The 2 major SUMO acceptor lysines in p35 are K246 and K290. Different degrees of oxidative stress resulted in differential p35 sumoylation. PMID: 25391294 Cdk5/p35 is required for motor learning and involved in long-term synaptic plasticity. PMID: 24802945 Expression of p35 is upregulated in human pituitary adenomas. PMID: 24550687 These results reveal a physiological role of p25 production in synaptic plasticity and memory and provide new insights into the function of p25 in Abeta-associated neurotoxicity and Alzheimer's disease-like pathology. PMID: 24725413 Structural basis for the different stability and activity between the Cdk5 complexes with p35 and p39 activators. PMID: 24085300 Reduced p35 basal content and down--regulation of CDK5/p35/p25 by antipsychotics are demonstrated in postmortem prefrontal cortex of schizophrenic subjects. PMID: 22964075 The present study dissects the role of 3 single nucleotide polymorphisms (rs334558 and rs6438552 of GSK3B, and rs735555 of CDK5R1) in Parkinson's disease pathogenesis among eastern Indians. PMID: 21130530 p10, the N-terminal domain of p35, protects against CDK5/p25-induced neurotoxicity. PMID: 23151508 The decrease in membrane-associated p35 in socially isolated transgenic mice reduces associated levels of p35, alpha-CaMKII, and GluR1 and leads to endocytosis of AMPA receptors. PMID: 21544067 CDK5/p35 may represent a biomarker for prognosis in patients with non-small cell lung cancer PMID: 20354813 findings indicate that miR-103 and miR-107 regulate CDK5R1 expression, allowing us to hypothesize that a miRNA-mediated mechanism may influence CDK5 activity and the associated molecular pathways PMID: 21625387 This study suggested that reduced p35 expression in schizophrenia has an impact on synaptic protein expression and cognition and that these deficits can be rescued, at least in part, by the inhibition of histone deacetylase 1. PMID: 21772061 Study reveals a unique role of Cdk5/p35 in activation of the major noncanonical function of EPRS, namely translational control of macrophage inflammatory gene expression. PMID: 21220307 These are the first quantitative and site-specific measurements of phosphorylation of p35 PMID: 20097924 both proteasomal degradation and calpain cleavage of p35 and p39 are stimulated by membrane association, which is in turn mediated via myristoylation of their p10 regions. PMID: 20518484 Like p25, p29 was more stable than p39 and caused redistribution of Cdk5 in cortical neurons. Our data suggest that neurotoxic insults lead to calpain-mediated conversion of p39 to p29, which might contribute to deregulation of Cdk5. PMID: 11784720 cleavage of p35 to p25 greatly enhances the kinase activity of CDK5 and increases the phosphorylation of Ser(202)/Thr(205) and may play a pivotal role in neuronal cell death in Alzheimer's disease PMID: 12226093 a short peptide (amino acid residues 154-279; Cdk5 inhibitory peptide; CIP), derived from p35, specifically inhibits Cdk5 activity in vitro and in HEK293 cells cotransfected with the peptide and Cdk5/p25, but had no effect on endogenous cdc2 kinase PMID: 12230554 p25-Cdk5 is responsible for the mitotic-like phosphoepitopes present in neurofibrillary tangles PMID: 12826674 Neither the CDK5 activator p25 immunoreactivity nor the p25/p35 ratio was elevated in Alzheimer disease brains or in other tauopathies (n = 34) compared with controls (n = 11) PMID: 12859671 Expression of p35 and CDK5 in insulin-producing beta-cellsis new signaling pathway controlled by glucose, and its functional role may comprise regulation of various biological processes in beta-cells, such as expression of the insulin gene. PMID: 14976144 These results suggest that Cdk5/p35 and p25 are novel players in digoxin-triggered prostate cancer cell apoptosis and, therefore, become potential therapeutic targets. PMID: 15123618 significantly lower levels of cyclin-dependent kinase 5, regulatory subunit 1 (p35) gene transcripts were detected in gangliogliomas compared to controls PMID: 15175076 CK2 acts as an inhibitor of Cdk5 in the brain PMID: 15342635 data suggest that Cyclin-dependent kinase 5 (Cdk5)-Cdk5 activator p35 is required to elicit the maximum GTP-induced secretory response from neutrophils PMID: 15492003 Cdk5 activity and p35 translocation in the ventral striatum were upregulated in methamphetamine sensitized rats. PMID: 15536496 an early event in neuronal cell death is p25/Cdk5-mediated retinoblastoma phosphorylation PMID: 15741232 role of the CDK5 molecular complex in the genetic etiology of early-onset Alzheimer disease; a yet unknown functional variant in CDK5 or in a nearby gene might lead to increased susceptibility for early onset Alzheimer disease PMID: 15917097 molecular analysis of the CDK5/p25 and CDK2/cyclin A systems PMID: 16407256 novel mutations and novel polymorphisms in coding regions and 3'UTR were detected in patients with with non-syndromic mental retardation PMID: 16425041 Cdk5 and Erk1/2 kinases share some common substrates but impact of their cross talk on tau phosphorylation has not previously been demonstrated. PMID: 16678793 nestin is a survival determinant whose action is based upon a novel mode of Cdk5 regulation, affecting the targeting, activity, and turnover of the Cdk5/p35 signaling complex PMID: 17036052 p35 employs pathways distinct from that used by Cdk5 for transport to the nucleus PMID: 17060323 phosphorylation of Thr(138) predominantly defines the susceptibility of p35 to calpain-dependent cleavage and dephosphorylation of this site is a critical determinant of Cdk5-p25-induced cell death associated with neurodegeneration PMID: 17121855 p35 is a microtubule-associated protein that modulates microtubule dynamics PMID: 17491008 Increased expression of Cdk5 was seen in stroke-affected tissue, with about a third showing increased p35 and p25 cleaved fragment. Increased Cdk5-, p-Cdk5- and p35-positive neurons and microvessels occurred in stroke-affected regions. PMID: 17493033 This experiment demonstrate increased immunoreactivity for the activators of cyclin-dependent kinase 5 in post-mortem human hippocampi affected by the neurodegenerative condition hippocampal sclerosis. PMID: 17496813 the involvement of 3'-UTR in the modulation of CDK5R1 expression PMID: 18053171 Data demonstrate that a decrease in the level of Egr-1, one of the targets for MAPK, by Tat has a negative impact on the level of p35 expression in NGF-treated neural cells. PMID: 18247371 p35 co-expression targets E-cadherin to lysosomes and p35-triggered disappearance of E-cadherin precursor can be blocked specifically by lysosomal protease inhibitors, indicating p35 induces endocytosis and subsequent degradation of precursor E-cadherin PMID: 18325333 p25 and cyclin-dependent kinase 5 play important roles as mediators of dopamine and glutamate in the neurotoxicity associated with Huntington's disease. PMID: 18829967 Subjects carrying both the CDK5R1 (3'-UTR, rs735555) AA genotype and the GSK-3beta (-50, rs334558) CC genotype had a 12.5-fold decrease in Alzheimer disease risk suggesting synergistic effects (epistasis) between both genes PMID: 19154537 a role for Cdk5-p35 as a survival factor in countering MPP+-induced neuronal cell death. PMID: 19638632 Performed functional studies in mouse. PMID: 9010203

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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