Recombinant Mouse BCL2L1 / Bcl-XL Protein (aa 1-212, His tag)

Supplier: Elabscience
Product Name: Recombinant Mouse BCL2L1 / Bcl-XL Protein (aa 1-212, His tag)
Catalog No. PKSM040918
Product Type: recombinant protein
Size: 100 ug
Activity: 1. Measured by its binding ability in a functional ELISA.2. Immobilized human BID at 10 ?g/mL (100 ?l/well) can bind  biotinylated mouse BCL2L1, The EC50 of biotinylated mouse BCL2L1 is 5.6 ng/mL.3. Immobilized mouse BID at 10 ?g/mL (100 ?l/well) can bind  biotinylated mouse BCL2L1, The EC50 of biotinylated mouse BCL2L1 is 7.1 ng/mL.
Protein Construction: A DNA sequence encoding the mouse BCL2L1 (Q64373-1) (Met 1-Arg 212) was expressed, with a C-terminal polyhistidine tag.
Sequence: Met 1-Arg 212
Fusion Tag: C-His
Accession: Q64373-1
Species: Mouse
Expressed Host: E.coli
Shipping Conditions: In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature.Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Purity: > 95 % as determined by SDS-PAGE
Endotoxin: Please contact us for more information.
Stability: Samples are stable for up to twelve months from date of receipt at -70?.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.
Molecular Weight: 25.2 kDa
Applied MM: 33 kDa
Formulation: Lyophilized from sterile PBS, pH 7.5
Reconstitution: Please refer to the printed manual for detailed information.

Background: B-cell lymphoma-extra large (Bcl-xl) is a transmembrane molecule in the mitochondria. Bcl-xL (BCL2L1) , belongs to the Bcl-2 family. Members of the bcl-2 family encode proteins that function either to promote or to inhibit apoptosis. Antiapoptotic members such as Bcl-2 and Bcl-xL prevent PCD in response to a wide variety of stimuli to take part in cancer survival. Conversely, proapoptotic proteins, exemplified by Bax and Bak, can accelerate death and in some instances are sufficient to cause apoptosis independent of additional signals. The crystal and solution structures of a Bcl-2 family member, Bcl-xL is like this: The structures consist of two central, primarily hydrophobic α-helices, which are surrounded by amphipathic helices. A 60-residue loop connecting helices αl and α2 was found to be flexible and non-essential for anti-apoptotic activity. Bcl-xL is chareacterized as important factors in autophagy, inhibiting Beclin 1-mediated autophagy by binding to Beclin 1. In addition, Beclin 1, Bcl-2 and Bcl-xL can cooperate with Atg5 or Ca2+ to regulate both autophagy and apoptosis. Bcl-xL is also implicated in anoxia induced cell death. The pathway is initiated by the loss of function of the prosurvival Bcl-2 family members Mcl-1 and Bcl-2 / Bcl-XL, resulting in Bax- or Bak-dependent release of cytochrome c and subsequent caspase-9-dependent cell death. Thus, Bcl-xL, the well-characterized apoptosis guards, appears to be important in cell death.