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.

News

Two more of our excellent products have been published by PubMed:

Potential actionable targets in appendiceal cancer detected by immunohistochemistry, fluorescent in situ hybridization, and mutational analysis
Borazanci, E., et al., J. Gastrointest. Oncol., 8, 164-172 (2017)
Using Exalpha SPARC Antibody (Cat. No. X1867P)

Molecular mechanism underlying the pharmacological interactions of the protein kinase C-β inhibitor enzastaurin and erlotinib in non-small cell lung cancer cells
Steen, N.V., et al., Am. J. Cancer Res., 7, 816-830 (2017)
Using Exalpha's FITC labeled anti PY20 Antibody (Cat. No. X1017)

SPARC

Background

Secreted Protein Acid Rich in Cysteine (SPARC), also known as ON (osteonectin) and BM-40 (basement-membrane protein 40), is a prototypic member of the SPARC family of proteins, a diverse group of proteins that each have an acidic domain, a follistatin-like domain and an extracellular calcium binding E-F hand motif. SPARC is a 34-35kD non-structural matricellular protein that is primarily expressed in tissues that have a continuous cellular turnover rate, and at site of tissue injury or disease. Reports suggest that SPARC binds to numerous different extracellular matrix (ECM) components and growth factors to modulate cell-matrix interaction and cell function. SPARC influences multiple biological processes including wound healing, development, bone formation, fibrosis, angiogenesis and tumour progression.

The precise role SPARC plays in tumorigenesis is hotly debated, with some reports indicating a positive correlation with more aggressive cancers and a poor clinical outcome and others indicating a protective effect. For example, in breast cancer, SPARC expression has been associated with a more aggressive phenotype and poor prognosis – with normal mammary tissue containing undetectable levels of SPARC expression, benign breast lesions are weakly positive and 75% of both in situ and invasive breast carcinomas are strongly positive for SPARC in stromal cells.

The precise role SPARC plays in tumorigenesis is hotly debated, with some reports indicating a positive correlation with more aggressive cancers and a poor clinical outcome and others indicating a protective effect. For example, in breast cancer, SPARC expression has been associated with a more aggressive phenotype and poor prognosis – with normal mammary tissue containing undetectable levels of SPARC expression, benign breast lesions are weakly positive and 75% of both in situ and invasive breast carcinomas are strongly positive for SPARC in stromal cells.

SPARC Related Products

X1858B SPARC Blocking Peptide
X1860P SPARC, Polyclonal Antibody
X1867P SPARC, Immunoaffinity Purified Polyclonal Antibody
X2745P SPARC, Biotin Conjugated Immunoaffinity Purified Polyclonal Antibody
X2546M SPARC, Monoclonal Antibody

References

  1. 1. Bradshaw AD, and Sage EH. (2001). SPARC, a matricellular protein that functions in cellular differentiation and tissue response to injury. J Clin Invest.107(9): 1049–1054.
  2. 2. Bradshaw AD. (2012). Diverse biological functions of the SPARC family of proteins. Int J Biochem Cell Biol. 44(3):480-8.
  3. 3. Nagaraju GP et al. (2014). Molecular mechanisms underlying the divergent roles of SPARC in human carcinogenesis. Carcinogenesis. 35(5):967-73.
  4. 4. Bellahcène A., Castronovo V. (1995). Increased expression of osteonectin and osteopontin, two bone matrix proteins, in human breast cancer. Am. J. Pathol. 146:95–100. 
  5. 5. Barth PJ. et al. (2005). Stromal remodeling and SPARC (secreted protein acid rich in cysteine) expression in invasive ductal carcinomas of the breast. Wirchows Arch. 446:532–536.
  6. 6. Watkins G, et al. (2005). Increased levels of SPARC (osteonectin) in human breast cancer tissues and its association with clinical outcomes. Prostaglandins Leukot Essent Fatty Acids. 72:267–72.
  7. 7. Jones C, et al. (2004). Expression profiling of purified normal human luminal and myoepithelial breast cells: identification of novel prognostic markers for breast cancer. Cancer Res. 64:3037–45.
  8. 8. Sharon L I Wong and Maria B Sukkar. The SPARC protein: an overview of its role in lung cancer and pulmonary fibrosis and its potential role in chronic airways disease Correspondence Dr Maria B Sukkar, Received 8 November 2015; Revised 5 October 2016; Accepted 11 October 2016

Sample Images


Western Blot- Detection of endogenous SPARC in mouse heart lysate using X1867P (0.75 ug/ml) and anti-rabbit HRP (1:75k) and using Pierce's Super Signal West Femto. IHC- Detection of endogenous SPARC in human hepatocellular carcinoma (HCC). 2 ug/ml X1867P, developed with Vector ImmPress anti-rabbit HRP and DAB substrate.).

Detection of endogenous SPARC in mouse heart lysate using X1860P (5 ug/ml) and anti-rabbit HRP (1:75k) and using Pierce's Super Signal West Femto.