Recombinant Human cIAP1 Protein (AVI Tag)

Name: Recombinant Human cIAP1 Protein (AVI Tag)
Brand: Beta LifeScience
SKU: BLPSN-1269
Availability: InStock

Collections: Avi-tagged proteins, Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	AVI
Host Species	Human
Accession	NP_001157.1
Synonym	API1, c-IAP1, cIAP1, Hiap-2, HIAP2, MIHB, RNF48
Background	The cellular inhibitor of apoptosis protein-1 (cIAP1) is a member of the Inhibitor of Apoptosis family proteinsare (IAP) whose members are characterized by a novel domain of about 7 amino acids termed baculoviral IAP repeats (BIRs). The BIR domains of cIAP1 and cIAP2 bind to caspases, the key effector proteases of apoptosis. The IAP protein family which can enhance cell survival are crucial regulators of programmed cell death. Both cIAP1 and cIAP2 are the E3 ubiquitin protein isopeptide ligases for Smac, taking part in promoting cancer survival through functioning as E3 ubiqitin ligases. Removal of cIAP1 by genetic deletion may result in NF-κB signaling activation that induces TNFalpha production and in killing sensitive tumor cells through enhanced TNF-R1 death-receptor signaling and caspase 8 activation. The substrate-dependent E3 activity of cIAPs is mediated by their RING domains and is dependent on the specific interactions between cIAPs and Smac. cIAP1 and cIAP2 are also reported to be regulators of NF-kB activation upon TNFalphatreatment.
Description	A DNA sequence encoding the BIR2 & BIR3 domains (Glu 144-Leu 356) of human cIAP1 (NP_001157.1) was expressed, fused with the AVI tag at the C-terminus, and two additional amino acids (Gly & Pro) at the N-terminus.
Source	E.coli
Predicted N Terminal	Gly
AA Sequence	Glu 144-Leu 356
Molecular Weight	The recombinant human cIAP1 consists of 230 a.a. and has a calculated molecular mass of 26.5 kDa as estimated by SDS-PAGE under reducing conditions.
Purity	>92% as determined by SDS-PAGE
Endotoxin	Please contact us for more information.
Bioactivity	Measured by its ability to inhibit DEVD-AFC cleavage activity in cell extracts activated by addition of cytochrome c and dATP. The IC50 for this effect is typically 25-750 nM.
Formulation	Lyophilized from sterile 10mM Tris, 5% glycerol, 0.5mM EDTA, 5mM DTT, pH 7.5.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

FAQs

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.