Analytical Data
-
Gene name
CLYBL
- Application
-
Alternative Names
CLYBL; CLB; Citramalyl-CoA lyase; mitochondrial; EC 4.1.3.25;; 3S)-malyl-CoA thioesterase; EC 3.1.2.30; Beta-methylmalate synthase; EC 2.3.3.-; Citrate lyase subunit beta-like protein; Citrate lyase beta-like; Malate synthase; EC 2.3.3.9
-
Species
Human
-
Source
E. coli
-
Tag
GST-tag at N-terminal
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8N0X4
-
Expression Region
1-340aa
-
AA Sequence
MALRLLRRAARGAAAAALLRLKASLAADIPRLGYSSSSHHKYIPRRAVLYVPGNDEKKIKKIPSLNVDCAVLDCEDGVAANKKNEARLRIVKTLEDIDLGPTEKCVRVNSVSSGLAEEDLETLLQSRVLPSSLMLPKVESPEEIQWFADKFSFHLKGRKLEQPMNLIPFVETAMGLLNFKAVCEETLKVGPQVGLFLDAVVFGGEDFRASIGATSSKETLDILYARQKIVVIAKAFGLQAVDLVYIDFRDGAGLLRQSREGAAMGFTGKQVIHPNQIAVVQEQFSPSPEKIKWAEELIAAFKEHQQLGKGAFTFQGSMIDMPLLKQAQNTVTLATSIKEK
-
Molecular Weight
63.7 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
CLYBL, or cyclin Y-binding protein, has garnered attention in recent years due to its significant role in cellular processes and potential implications in various diseases. It is involved in modulating cell cycle progression and is linked to critical signaling pathways that govern cell proliferation and differentiation. Research has shown that CLYBL is essential for the regulation of cyclin Y, a protein that influences the activities of cyclin-dependent kinases (CDKs), which are pivotal for cell cycle control. This interaction underscores the importance of CLYBL in maintaining the balance between cell growth and apoptosis, making it a focal point in cancer research, where dysregulation of the cell cycle is a hallmark. Moreover, mutations or altered expression levels of CLYBL have been implicated in certain pathologies, prompting investigations into its potential as a therapeutic target. As the understanding of its biochemical functions and interactions expands, CLYBL is emerging as a promising candidate for novel therapeutic strategies aimed at modulating cell cycle dynamics in cancer and other proliferative disorders, stimulating ongoing research into its structure, functions, and potential applications in regenerative medicine and targeted therapies.
