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)

Exalpha Biologicals, Inc.

Adiponectin

  • Product Code: X1832P
  • Size: 100 µg
  • Availability: In Stock In Stock
  • Price (USD): $383

Cat #

X1832P		 Quantity:      

Data Sheet

Product Name

Adiponectin

Synonyms

ACRP30, adipocyte complement-related protein 30 (NT)

Host/Source

Rabbit

Isotype

IgG

Product Type

Antigen Immunoaffinity Purified Polyclonal

Reactivity

Human, Mouse, Rat

Applications

Western Blot, Immunohistochemistry

Purification

Antigen Immunoaffiinity Purification

Size

100 µg

Price (USD)

$383

Background

Adipose tissue of an organism plays a major role in regulating physiologic and pathologic processes such as metabolism and immunity by producing and secreting a variety of bioactive molecules termed adipokines (reviewed in 1). One highly conserved family of adipokines is adiponectin/ACRP30 and its structural and functional paralogs, the C1q/tumor necrosis factor-?-related proteins (CTRPs) 1-7 (2). Unlike the CTRPs, which are expressed in a wide variety of tissues, adiponectin is reported to be expressed exclusively by differentiated adipocytes (3). These proteins are thought to act mainly on liver and muscle tissue to control glucose and lipid metabolism. An analysis of the crystal structure of adiponectin revealed a structural and evolutionary link between TNF and C1q-containing proteins, suggesting that these proteins arose from a common ancestral innate immunity gene (4). It is present in high levels in normal human plasma, but is reduced in obese subjects and often in those with increased insulin resistance and type 2 diabetes, suggesting that adiponectin may be a useful pharmacological target in various metabolic diseases (5).

Immunogen

Rabbit polyclonal adiponectin antibody was raised against a 15 amino acid peptide from near the amino terminus of human adiponectin.

Positive Control

Positive Control Rat brain cell lysate A secreted protein synthesized exclusively by adipocytes.6

Formulation

Provided as solution in phosphate buffered saline with 0.02% sodium azide

Customer Storage

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

Target Molecular Weight

26.4

Product Image

Image Legend

Western blot analysis of adiponectin in rat brain cell lysate with adiponectin antibody at (A) 1, (B) 2, and (C) 4 µg/ml.

Database Links:

SwissProtQ15848Human

References

1) Fantuzzi G. Adipose tissue, adipokines, and inflammation. J. Allergy Clin. Immunol. 2005; 115:911-9.
2) Tsao T-S, Lodish HF, and Fruebis J. ACRP30, a new hormone controlling fat and glucose metabolism. Euro. J. Pharmacol. 2002; 440:213-21.
3.) Wong GW, Wang J, Hug C, et al. A family of Acrp30/ adiponectin structural and functional paralogs. Proc. Natl. Acad. Sci. USA 2004; 101:10302-7.
4) Shapiro L and Scherer PE. The crystal structure of a complement-1q family protein suggests an evolutionary link to tumor necrosis factor. Curr. Biol. 1998; 8:335-8.
5) Lihn AS, Pedersen SB, and Richelsen B. Adiponectin: action, regulation and association to insulin sensitivity. Obes. Rev. 2005; 6:13-21.
6) UniProtKB/Swiss-Prot entry Q15848, http://au.expasy.org/uniprot/Q15848, Accessed February 27, 2007.