BSA, Flamma® 675

Product#: RSC0112_5 mg
$466.87
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BSA, Flamma® 675

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Description

BSA, Flamma® 675 is an advanced fluorescent conjugate that combines the well-characterized properties of bovine serum albumin (BSA) with the exceptional fluorescence capabilities of the Flamma® 675 dye. This versatile reagent offers researchers a powerful tool for a wide range of biological imaging and quantitative applications, particularly in the far-red to near-infrared spectrum.

BSA, Flamma® 675 serves as a powerful tool in numerous biological research areas such as quantitative studies of electroporation, measurement of plasma volume, intracellular protein processing investigations, fluorescent tracer in applications requiring well-defined physical dimensions, deep tissue and in vivo imaging, fluorescence-guided surgery, near-infrared fluorescence microscopy, flow cytometry, single-molecule detection studies, and protein trafficking and localization experiments. 

BSA, Flamma® 675 is part of the Flamma® Fluor family of dyes, known for their superior performance in bioconjugation applications. The dye maintains its excellent fluorescence properties when conjugated to BSA, ensuring minimal self-quenching and high signal-to-noise ratios in experimental settings.

The conjugate's excitation maximum at 675 nm makes it compatible with common far-red laser lines used in advanced fluorescence microscopy and flow cytometry systems. Its emission maximum at 691 nm provides bright far-red/near-IR fluorescence that is ideal for deep tissue imaging, in vivo studies, and multi-color experiments where spectral separation is crucial.

The BSA component of this conjugate serves as an excellent model protein for various biological studies. Its well-defined structure and size make it particularly useful for applications where a specific molecular dimension is required, such as in studies of membrane permeability or cellular uptake mechanisms.

BSA, Flamma® 675 represents an advanced fluorescent tool that combines the benefits of a well-understood protein carrier with cutting-edge fluorophore technology. Its exceptional brightness, photostability, and far-red/near-IR spectral properties make it an ideal choice for researchers seeking a reliable and high-performance option for their fluorescence-based studies in cellular and molecular biology, particularly in applications where deep tissue penetration, minimal autofluorescence, and defined molecular size are critical factors.

What are the advantages? 
1. Brightness: The high absorption and quantum yield of Flamma® 675 ensure strong fluorescence signals, even at low concentrations.
2. Stability: Excellent photostability allows for extended imaging sessions without significant signal loss.
3. Far-Red/Near-IR Emission: Reduced autofluorescence and improved tissue penetration compared to shorter wavelength dyes.
4. Versatility: The well-characterized BSA molecule provides a reliable platform for various experimental designs.
5. Defined Size: The known dimensions of BSA make it ideal for studies requiring precise molecular size control.
6. Biocompatibility: BSA's natural properties ensure good compatibility with biological systems.
7. Minimal Spectral Overlap: The far-red emission reduces bleed-through in multi-color imaging experiments.
8. Low Phototoxicity: Near-IR excitation minimizes damage to live specimens during imaging.
 
Specifications
  • Fluorophore: Flamma® 675
  • Protein subtype: Albumin protein
  • Excitation/Emission Max.(nm): 675/691 
  • Strong Absorption: High molar extinction coefficient
  • High Fluorescence Quantum Yield: Ensures bright fluorescence signals
  • Excellent Photostability: Ideal for long-term imaging studies and applications requiring extended illumination
  • Molecular weight: ~66.5 kDa
  • Appearance: Yellow Solid
  • Storage conditions: 4 ℃, protect from light

    ***These properties are maintained after conjugation to BSA, ensuring reliable and consistent performance in various experimental settings. The dye's spectral characteristics make it an excellent alternative to other popular far-red fluorophores, such as Cy5.5 or Alexa Fluor 680***

Table 1. List of Fluorescent BSA
 
Quick link (Cat.#) Series Ex * (nm) Em* (nm)
RSC0102 BSA, Flamma® 488 495 519
RSC0105 BSA, Flamma® 552 550 565
RSC0106 BSA, Flamma® 560 560 589
RSC0110 BSA, Flamma® 581 581 596
RSC0111 BSA, Flamma® 648 648 663
RSC0112 BSA, Flamma® 675 675 691
RSC0113 BSA, Flamma® 749 749 774
RSC0114 BSA, Flamma® 774 774 806


Overview

Albumin, making up 55 to 62% of the serum protein, is one of the few carbohydrate-free proteins in blood plasma that plays an important role in maintaining the colloidal osmotic pressure. Albumin also acts as a plasma carrier of several hydrophobic steroid hormones and as a transport protein for hemin and fatty acids. Bovine serum albumin (BSA) is a small (~66.5 kDa), stable, moderately non-reactive protein that has been utilized in numerous biochemical applications including ELISA, Western blot, immunohistochemistry, etc. BSA enable to increase antibody functionality and longevity and serves as both a standard in protein quantitation and a stabilizing component in DNA blunt end and replacement assays. Bovine serum albumin (BSA) conjugates are commonly used as tracers in applications where physical dimensions are important. Specifically, fluorescent BSA conjugates have been used in many applications such as quantitative studies of electroporation, measurement of plasma volume, intra cellular protein processing. BioActs provides a wide range of fluorophore-conjugated BSA analogs as well-defined molecular weight tracers for a variety of applications.

Citation & Reference

1. A beta Pix Pak2a signaling pathway regulates cerebral vascular stability in zebrafish. Liu J. Proc Natl Acad Sci U S A. 2007 Aug 28;104(35):13990-5

2. Cell mechanics control rapid transitions between blebs and lamellipodia during migration. Bergert M. Proc Natl Acad Sci U S A.2012 Sep 4;109(36):14434-9.

3. Measuring molecular rupture forces between single actin filaments and actin-binding proteins. Ferrer JM. Proc Natl Acad Sci U S A.2008 Jul 8;105(27):9221-


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