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Rabbit Anti-ANP32B Recombinant Antibody (CBYC-P015) (CBMAB-P0064-YC)

Provided herein is a Rabbit monoclonal antibody against Human Acidic Nuclear Phosphoprotein 32 Family Member B. The antibody can be used for immunoassay techniques, such as WB, IHC-P, FC, ICC, IF.
See all ANP32B antibodies

Summary

Host Animal
Rabbit
Specificity
Human, Mouse, Rat
Clone
CBYC-P015
Antibody Isotype
IgG
Application
ICC, IHC, WB

Basic Information

Immunogen
A synthetic peptide corresponding to a sequence within amino acids 1-100 of human ANP32B.
Host Species
Rabbit
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG
Clonality
Monoclonal
Application Notes
The COA includes recommended starting dilutions, optimal dilutions should be determined by the end user.
ApplicationNote
WB1:500-1:2,000
IF(ICC)1:50-1:200
IHC1:50-1:200

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

Format
Liquid
Buffer
PBS, 0.05% BSA, 50% glycerol, pH7.3
Preservative
0.02% sodium azide
Concentration
Batch dependent
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
Acidic Nuclear Phosphoprotein 32 Family Member B
Introduction
Multifunctional protein working as a cell cycle progression factor as well as a cell survival factor. Required for the progression from the G1 to the S phase. Anti-apoptotic protein which functions as a caspase-3 inhibitor. Has no phosphatase 2A (PP2A) inhibitor activity. Exhibits histone chaperone properties, stimulating core histones to assemble into a nucleosome.
Entrez Gene ID
Human10541
Mouse67628
Rat170724
UniProt ID
HumanQ92688
MouseQ9EST5
RatQ9EST6
Alternative Names
Acidic Nuclear Phosphoprotein 32 Family Member B; Acidic Protein Rich In Leucines; Acidic (Leucine-Rich) Nuclear Phosphoprotein 32 Family, Member B; Putative HLA-DR-Associated Protein I-2; Silver-Stainable Protein SSP29; PHAPI2; APRIL; Acidic Leucine-Rich Nuclear Phosphoprotein 32 Family Member B; SSP29;
Function
Multifunctional protein that is involved in the regulation of many processes including cell proliferation, apoptosis, cell cycle progression or transcription (PubMed:20015864, PubMed:18039846). Regulates the proliferation of neuronal stem cells, differentiation of leukemic cells and progression from G1 to S phase of the cell cycle. As negative regulator of caspase-3-dependent apoptosis, may act as an antagonist of ANP32A in regulating tissue homeostasis (PubMed:20015864). Exhibits histone chaperone properties, able to recruit histones to certain promoters, thus regulating the transcription of specific genes (PubMed:20538007, PubMed:18039846). Plays also an essential role in the nucleocytoplasmic transport of specific mRNAs via the uncommon nuclear mRNA export receptor XPO1/CRM1 (PubMed:17178712). Participates in the regulation of adequate adaptive immune responses by acting on mRNA expression and cell proliferation (By similarity).
(Microbial infection) Plays an essential role in influenza A and B viral genome replication (PubMed:33045004, PubMed:31217244). Plays also a role in foamy virus mRNA export from the nucleus to the cytoplasm (PubMed:21159877).
Biological Process
Activation of cysteine-type endopeptidase activity involved in apoptotic process Source: UniProtKB
Inner ear development Source: Ensembl
Negative regulation of cell differentiation Source: UniProtKB
Nucleosome assembly Source: UniProtKB
Positive regulation of protein export from nucleus Source: UniProtKB
Regulation of apoptotic process Source: GO_Central
Roof of mouth development Source: Ensembl
Vasculature development Source: Ensembl
Ventricular system development Source: Ensembl
Cellular Location
Isoform 1: Cytoplasm; Nucleus. Accumulates in the nuclei at the S phase.
Isoform 2: Cytoplasm. Lacks a nuclear localization signal.
PTM
Some glutamate residues are glycylated by TTLL8. This modification occurs exclusively on glutamate residues and results in a glycine chain on the gamma-carboxyl group (By similarity).
Directly cleaved by caspase-3/CASP3.

Rivero-Rodríguez, F., Díaz-Quintana, A., Velázquez-Cruz, A., González-Arzola, K., Gavilan, M. P., Velázquez-Campoy, A., ... & Díaz-Moreno, I. (2021). Inhibition of the PP2A activity by the histone chaperone ANP32B is long-range allosterically regulated by respiratory cytochrome c. Redox biology, 43, 101967.

Yang, S., Zhu, X. N., Zhang, H. L., Yang, Q., Wei, Y. S., Zhu, D., ... & Yu, Y. (2021). ANP32B-mediated repression of p53 contributes to maintenance of normal and CML stem cells. Blood.

Günther, M., Bauer, A., Müller, M., Zaeck, L., & Finke, S. (2020). Interaction of host cellular factor ANP32B with matrix proteins of different paramyxoviruses. Journal of General Virology, 101(1), 44-58.

Park, Y. H., Chungu, K., Lee, S. B., Woo, S. J., Cho, H. Y., Lee, H. J., ... & Han, J. Y. (2020). Host-specific restriction of avian influenza virus caused by differential dynamics of ANP32 family members. The Journal of infectious diseases, 221(1), 71-80.

Chemnitz, J., Pieper, D., Stich, L., Schumacher, U., Balabanov, S., Spohn, M., ... & Zinser, E. (2019). The acidic protein rich in leucines Anp32b is an immunomodulator of inflammation in mice. Scientific reports, 9(1), 1-14.

Barbeito, P., Sarandeses, C. S., Díaz-Jullien, C., Muras, J., Covelo, G., Moreira, D., ... & Freire, M. (2017). Prothymosin α interacts with SET, ANP32A and ANP32B and other cytoplasmic and mitochondrial proteins in proliferating cells. Archives of biochemistry and biophysics, 635, 74-86.

Ohno, Y., Koizumi, M., Nakayama, H., Watanabe, T., Hirooka, M., Tokumoto, Y., ... & Hiasa, Y. (2017). Downregulation of ANP32B exerts anti-apoptotic effects in hepatocellular carcinoma. PloS one, 12(5), e0177343.

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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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