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Mouse Anti-BIK Recombinant Antibody (CBYY-0585) (CBMAB-0588-YY)

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Published Data

Summary

Host Animal
Mouse
Specificity
Human
Clone
CBYY-0585
Antibody Isotype
IgG1, κ
Application
WB, IP, IF, ELISA, IHC-P

Basic Information

Immunogen
Amino acids 1-160 representing full length NBK (Natural Born Killer) of human origin.
Host Species
Mouse
Specificity
Human
Antibody Isotype
IgG1, κ
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:100-1:1,000
IP1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
IF(ICC)1:50-1:500
ELISA1:100-1:1,000
IHC-P1:50-1:500

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
PBS, 0.1% gelatin
Preservative
< 0.1% sodium azide
Concentration
0.2 mg/ml
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Target

Full Name
BCL2-interacting killer (apoptosis-inducing)
Introduction
The protein encoded by this gene shares a critical BH3 domain with other death-promoting proteins, such as BID, BAK, BAD and BAX, that is required for its pro-apoptotic activity, and for interaction with anti-apoptotic members of the BCL2 family, and viral survival-promoting proteins. Since the activity of this protein is suppressed in the presence of survival-promoting proteins, it is suggested as a likely target for anti-apoptotic proteins.
Entrez Gene ID
UniProt ID
Alternative Names
BCL2 Interacting Killer; BCL2-Interacting Killer (Apoptosis-Inducing); Apoptosis Inducer NBK; Natural Born Killer; BIP1; BP4; NBK; Bcl-2-Interacting Killer; Apoptosis-Inducing NBK;
Function
Accelerates programmed cell death. Association to the apoptosis repressors Bcl-X(L), BHRF1, Bcl-2 or its adenovirus homolog E1B 19k protein suppresses this death-promoting activity. Does not interact with BAX.
Biological Process
Apoptotic mitochondrial changes Source: GO_Central
Apoptotic process Source: UniProtKB
Male gonad development Source: GO_Central
Positive regulation of protein-containing complex assembly Source: BHF-UCL
Positive regulation of release of cytochrome c from mitochondria Source: BHF-UCL
Regulation of apoptotic process Source: InterPro
Cellular Location
Mitochondrion membrane; Endomembrane system. Around the nuclear envelope, and in cytoplasmic membranes.
Topology
Helical: 136-156 aa
PTM
Proteolytically cleaved by RHBDL4/RHBDD1. RHBDL4/RHBDD1-induced cleavage is a necessary step prior its degradation by the proteosome-dependent mechanism.
More Infomation

López-Muñoz, E., Corres-Molina, M., & García-Hernández, N. (2020). Correlation of the protein expression of GRP78 and BIK/NBK with prognostic markers in patients with breast cancer and neoadjuvant chemotherapy. Journal of Obstetrics and Gynaecology, 40(3), 419-426.

Pandya, V., Githaka, J. M., Patel, N., Veldhoen, R., Hugh, J., Damaraju, S., ... & Goping, S. (2020). BIK drives an aggressive breast cancer phenotype through sublethal apoptosis and predicts poor prognosis of ER-positive breast cancer. Cell death & disease, 11(6), 1-19.

Chen, X., Li, C., Li, J., Sheng, L., & Liu, X. (2019). Upregulation of miR-1306-5p decreases cerebral ischemia/reperfusion injury in vitro by targeting BIK. Bioscience, biotechnology, and biochemistry, 83(12), 2230-2237.

Pandya, V. K. (2019). Investigation of BCL-2 interacting killer (BIK) as a breast cancer biomarker and its role in failed apoptosis.

Miguel, V. F., REG R, K. A., Javier, T. L., & Juan, R. C. (2018). Accurate Identification of BIK Binding Sites at the MDA-MB-231 Cell Genome by Human Tiling Arrays. Cancer Biol Ther Oncol, 2(1), 2.

Mebratu, Y. A., & Tesfaigzi, Y. (2018). Does the BCL-2 family member BIK control lung carcinogenesis?. Molecular & cellular oncology, 5(4), e1435182.

Mebratu, Y. A., & Tesfaigzi, Y. (2018). Bcl-2 Interacting Killer (BIK) Augments Influenza A Virus Replication and Severity of Flu. In B62. LUNG CYTOPROTECTION AND IMMUNITY DURING INFECTIONS (pp. A3845-A3845). American Thoracic Society.

Lin, M. L., & Chen, S. S. (2017). Activation of Casein Kinase II by Gallic Acid Induces BIK–BAX/BAK-Mediated ER Ca++-ROS-Dependent Apoptosis of Human Oral Cancer Cells. Frontiers in physiology, 8, 761.

Borst, A., Haferkamp, S., Grimm, J., Rösch, M., Zhu, G., Guo, S., ... & Houben, R. (2017). BIK is involved in BRAF/MEK inhibitor induced apoptosis in melanoma cell lines. Cancer letters, 404, 70-78.

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For research use only. Not intended for any clinical use.

Custom Antibody Labeling

We also offer labeled antibodies developed using our catalog antibody products and nonfluorescent conjugates (HRP, AP, Biotin, etc.) or fluorescent conjugates (Alexa Fluor, FITC, TRITC, Rhodamine, Texas Red, R-PE, APC, Qdot Probes, Pacific Dyes, etc.).

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