Exalpha Biologicals, Inc.

Accelerating the Pace of Discovery

Product Highlight

Mouse anti-M13 phage coat protein g8p

Antibodies recognising M13 filamentous phage coat proteins are instrumental in the selection and detection of phages expressing specific antibody fragments or peptide sequences at their surface. The monoclonal antibodies manufactured and supplied by Exalpha react with either the pIII (g3p) or pVIII (g8p) proteins of M13 filamentous bacteriophage. All antibodies are available in a purified format. The antibodies are fully validated and are suitable for a wide range of techniques including:

  • ELISA
  • Flow Cytometry
  • Western Blot
  • Immunohistochemistry
  • Immunoprecipitation
For more information, click here for our M13 Bacteriophage information page.

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Borazanci, E., et al., J. Gastrointest. Oncol., 8, 164-172 (2017)
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Using Exalpha's FITC labeled anti PY20 Antibody (Cat. No. X1017)

Exalpha Biologicals, Inc.

Bnip3L (IN) (nix) (bcl 2 family)

  • Product Code: X1120P
  • Size: 100 µg
  • Availability: In Stock In Stock
  • Price (USD): $383

Cat #

X1120P		 Quantity:      

Data Sheet

Product Name

Bnip3L (IN) (nix) (bcl 2 family)

Synonyms

BNIP3A, BNIP3H, NIX

Host/Source

Rabbit

Isotype

IgG

Product Type

Polyclonal Antibody

Reactivity

Human

Applications

Western Blot

Purification

Antigen Immunoaffiinity Purification

Size

100 µg

Price (USD)

$383

Background

Members in the Bcl-2 family are critical regulators of apoptosis by either inhibiting or promoting cell death. Bcl-2 homology 3 (BH3) domain is a potent death domain. BH3 domain containing pro-apoptotic proteins, including Bad, Bax, Bid, Bik, Hrk, Nip3, and Bim, form a growing subclass of the Bcl-2 family. A novel BH3 domain containing protein was recently identified and designated Bnip3L, Bnip3α, and Nix (for Nip3-like protein X) (1-3). Bnip3L/Bnip3α/Nix is a homolog of the E1B 19K/Bcl-2 binding and pro-apoptotic protein Bnip3. Overexpression of Bnip3L induces apoptosis (2,3). Bnip3L interacts with and overcomes suppresses by Bcl-2 and Bcl-xL. Bnip3L is localized in mitochondria. The messenger RNA of Bnip3L is ubiquitously expressed in human tissues (1,2). Bnip3L and Bnip3 form a new subfamily of the pro-apoptotic mitochondrial proteins.

Immunogen

Synthetic peptide corresponding to amino acids 77 to 92 of the human Bnip3L protein. Immunogen sequence is identical in the mouse protein.

Positive Control

K562 cell lysate

Formulation

Provided in phosphate buffered saline solution containing 0.02% sodium azide as a preservative

Customer Storage

Product should be stored at -20°C. Aliquot to avoid freeze/thaw cycles

Target Molecular Weight

40

Product Image

Image Legend

Western blot analysis using anti-Bnip3L (IN) antibody at 1 µg/ml on K562 whole cell lysate in the absense (1) and presense (2) of immunogenic peptide.

Database Links:

SwissProtO60238Human

References

1. Matsushima, M., et al., Isolation, mapping, and functional analysis of a novel human cDNA (BNIP3L) encoding a protein homologous to human NIP3. Genes Chromosomes Cancer 1998, 21, 230-235

2. Yasuda, M., et al., BNIP3alpha: a human homolog of mitochondrial proapoptotic protein BNIP3. Cancer Res. 1999, 59, 533-537

3. Chen, G., et al., Nix and Nip3 form a subfamily of pro-apoptotic mitochondrial proteins. J. Biol. Chem. 1999, 274, 7-10

4. Imazu, T., et al., Bcl-2/E1B 19 kDa-interacting protein 3-like protein (Bnip3L) interacts with bcl-2/Bcl-xL and induces apoptosis by altering mitochondrial membrane permeability. Oncogene. 1999, 18, 4523-4529

Product Specific References:

1. Aerbajinai, W., et al. 'The proapoptotic factor Nix is coexpressed with Bcl-xL during terminal erythroid differentiation.' Blood, 2003, 102, 712-717.

2. Zhang, J., et al. 'Mitochondrial clearance is regulated by Atg7-dependent and -independent mechanisms during reticulocyte maturation.' Blood, 2009, 114, 157-164.


Product Specific References


This product has been used in:

1. Zhang, J., et al. ‘A short linear motif in BNIP3L (NIX) mediates mitochondrial clearance in reticulocytes.’ Autophagy, 8, 1325-1332 (2012)