Recombinant Human Cyclin-dependent kinase 5 (CDK5)

SKU:BHP10500414
Overview
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Recombinant CDK5 Human protein produced in E. coli, N-terminal 6xHis-SUMO-tagged spanning 1-292aa. Suitable for binding assays, functional studies, and assay development.
Expression System E. coli
Tag N-terminal 6xHis-SUMO-tagged
Purity Greater than 90% as determined by SDS-PAGE.
Species Homo sapiens (Human)
Molecular Weight 49.3 kDa
Available Options

Select the variant that best fits your experiment. Availability and lead time may vary by option.

  • Options: Size (3) - 1 mg, 100 ug, 20 ug
  • Lead time: Made to Order — production begins after purchase. Lead time is typically 13-23 business days.
  • Storage: The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.
  • Shipping: cold-chain shipment (typically with ice packs).
  • Upon receipt: store at recommended temperature as soon as possible.
  • Sales terms and conditions: Please review prior to ordering.
Options selector
Catalog no. Size
CSB-EP005067HU-1MG 1 mg
CSB-EP005067HU-100UG 100 ug
CSB-EP005067HU-20UG 20 ug
Field Specification
Activity
  • Not Test
Alternative Names Cell division protein kinase 5Serine/threonine-protein kinase PSSALRETau protein kinase II catalytic subunit ;TPKII catalytic subunit
Endotoxin Level Not test
Expression System
  • E. coli
Form Liquid or Lyophilized powder
Function
  • Proline-directed serine/threonine-protein kinase essential for neuronal cell cycle arrest and differentiation and may be involved in apoptotic cell death in neuronal diseases by triggering abortive cell cycle re-entry. Interacts with D1 and D3-type G1 cyclins. Phosphorylates SRC
  • NOS3
  • VIM/vimentin
  • p35/CDK5R1
  • MEF2A
  • SIPA1L1
  • SH3GLB1
  • PXN
  • PAK1
  • MCAM/MUC18
  • SEPT5
  • SYN1
  • DNM1
  • AMPH
  • SYNJ1
  • CDK16
  • RAC1
  • RHOA
  • CDC42
  • TONEBP/NFAT5
  • MAPT/TAU
  • MAP1B
  • histone H1
  • p53/TP53
  • HDAC1
  • APEX1
  • PTK2/FAK1
  • huntingtin/HTT
  • ATM
  • MAP2
  • NEFH and NEFM. Regulates several neuronal development and physiological processes including neuronal survival
  • migration and differentiation
  • axonal and neurite growth
  • synaptogenesis
  • oligodendrocyte differentiation
  • synaptic plasticity and neurotransmission
  • by phosphorylating key proteins. Activated by interaction with CDK5R1 (p35) and CDK5R2 (p39)
  • especially in post-mitotic neurons
  • and promotes CDK5R1 (p35) expression in an autostimulation loop. Phosphorylates many downstream substrates such as Rho and Ras family small GTPases (e.g. PAK1
  • RAC1
  • RHOA
  • CDC42) or microtubule-binding proteins (e.g. MAPT/TAU
  • MAP2
  • MAP1B)
  • and modulates actin dynamics to regulate neurite growth and/or spine morphogenesis. Phosphorylates also exocytosis associated proteins such as MCAM/MUC18
  • SEPT5
  • SYN1
  • and CDK16/PCTAIRE1 as well as endocytosis associated proteins such as DNM1
  • AMPH and SYNJ1 at synaptic terminals. In the mature central nervous system (CNS)
  • regulates neurotransmitter movements by phosphorylating substrates associated with neurotransmitter release and synapse plasticity; synaptic vesicle exocytosis
  • vesicles fusion with the presynaptic membrane
  • and endocytosis. Promotes cell survival by activating anti-apoptotic proteins BCL2 and STAT3
  • and negatively regulating of JNK3/MAPK10 activity. Phosphorylation of p53/TP53 in response to genotoxic and oxidative stresses enhances its stabilization by preventing ubiquitin ligase-mediated proteasomal degradation
  • and induces transactivation of p53/TP53 target genes
  • thus regulating apoptosis. Phosphorylation of p35/CDK5R1 enhances its stabilization by preventing calpain-mediated proteolysis producing p25/CDK5R1 and avoiding ubiquitin ligase-mediated proteasomal degradation. During aberrant cell-cycle activity and DNA damage
  • p25/CDK5 activity elicits cell-cycle activity and double-strand DNA breaks that precedes neuronal death by deregulating HDAC1. DNA damage triggered phosphorylation of huntingtin/HTT in nuclei of neurons protects neurons against polyglutamine expansion as well as DNA damage mediated toxicity. Phosphorylation of PXN reduces its interaction with PTK2/FAK1 in matrix-cell focal adhesions (MCFA) during oligodendrocytes (OLs) differentiation. Negative regulator of Wnt/beta-catenin signaling pathway. Activator of the GAIT (IFN-gamma-activated inhibitor of translation) pathway
  • which suppresses expression of a post-transcriptional regulon of proinflammatory genes in myeloid cells; phosphorylates the linker domain of glutamyl-prolyl tRNA synthetase (EPRS) in a IFN-gamma-dependent manner
  • the initial event in assembly of the GAIT complex. Phosphorylation of SH3GLB1 is required for autophagy induction in starved neurons. Phosphorylation of TONEBP/NFAT5 in response to osmotic stress mediates its rapid nuclear localization. MEF2 is inactivated by phosphorylation in nucleus in response to neurotoxin
  • thus leading to neuronal apoptosis. APEX1 AP-endodeoxyribonuclease is repressed by phosphorylation
  • resulting in accumulation of DNA damage and contributing to neuronal death. NOS3 phosphorylation down regulates NOS3-derived nitrite (NO) levels. SRC phosphorylation mediates its ubiquitin-dependent degradation and thus leads to cytoskeletal reorganization. May regulate endothelial cell migration and angiogenesis via the modulation of lamellipodia formation. Involved in dendritic spine morphogenesis by mediating the EFNA1-EPHA4 signaling. The complex p35/CDK5 participates in the regulation of the circadian clock by modulating the function of CLOCK protein
Molecular Weight 49.3 kDa
Product Type
  • Recombinant Protein
Purity Greater than 90% as determined by SDS-PAGE.
Reconstitution We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Species Homo sapiens (Human)
Storage The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.
UniProt # Q00535

Scientific Background

Proline-directed serine/threonine-protein kinase essential for neuronal cell cycle arrest and differentiation and may be involved in apoptotic cell death in neuronal diseases by triggering abortive cell cycle re-entry. Interacts with D1 and D3-type G1 cyclins. Phosphorylates SRC, NOS3, VIM/vimentin, p35/CDK5R1, MEF2A, SIPA1L1, SH3GLB1, PXN, PAK1, MCAM/MUC18, SEPT5, SYN1, DNM1, AMPH, SYNJ1, CDK16, RAC1, RHOA, CDC42, TONEBP/NFAT5, MAPT/TAU, MAP1B, histone H1, p53/TP53, HDAC1, APEX1, PTK2/FAK1, huntingtin/HTT, ATM, MAP2, NEFH and NEFM.

Product Description

E. coli Expression

Recombinant Human Cyclin-dependent kinase 5 (CDK5) is a recombinant protein expressed in E. coli and purified to Greater than 90% as determined by SDS-PAGE. as determined by SDS-PAGE. Supplied as Liquid or Lyophilized powder, n-terminal 6xhis-sumo-tagged. For research use only.

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Protein Specifications

Molecular Weight 49.3 kDa
Expression Region 1-292aa
Expression System E. coli
Tag N-terminal 6xHis-SUMO-tagged
Purity Greater than 90% as determined by SDS-PAGE.
Form Liquid or Lyophilized powder
Storage Buffer If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Endotoxin Level Not test
UniProt Accession Q00535
Storage The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.

Safety & Handling

For Research Use Only (RUO). Not intended for diagnostic or therapeutic use. Handle as potentially biohazardous material. Follow your institution's biosafety guidelines when working with recombinant proteins.

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What expression system was used to produce this protein?

This recombinant protein is expressed in E. coli, a widely used system for producing soluble, biologically active proteins at scale. The E. coli expression platform enables efficient folding and high yields, suitable for functional and binding assays.

What is the tag and purity of this product?

This protein is supplied as N-terminal 6xHis-SUMO-tagged and has been purified to Greater than 90% as determined by SDS-PAGE. as determined by SDS-PAGE. High purity minimizes interference in downstream assays, particularly in cell-based bioactivity studies and ELISA development.

How should I reconstitute and store this product?

Briefly centrifuge the vial before opening. Reconstitute in sterile deionized water to 0.1–1.0 mg/mL. For long-term storage, add 5–50% glycerol and store in aliquots at -20°C or -80°C to avoid repeated freeze-thaw cycles. The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20℃/-80℃. The shelf life of lyophilized form is 12 months at -20℃/-80℃.

Is this protein biologically active?

Biological activity data are available in the product datasheet. Please contact our support team for activity specifications relevant to your specific application.

What applications is this recombinant protein suitable for?

This recombinant protein is suitable for a range of in vitro research applications including binding assays, protein–protein interaction studies, cell proliferation/bioactivity assays, ELISA standard curve calibration, and assay development. Confirm suitability for your specific assay conditions with the product datasheet.

We offer flexible ordering options including bulk quantities, custom formulations, and endotoxin removal services for many of our recombinant proteins. Lead times and minimum order quantities vary by product. For custom conjugation, specialized buffer formulations, or volume pricing, please contact our support team. All customization requests are handled in partnership with our manufacturing suppliers and are subject to feasibility review.

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