BSA, Flamma® 488
Product#: RSC0102_5 mg
$466.87
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BSA, Flamma® 488
Cat. No. List below
Description
BSA, Flamma® 488 is a high-performance fluorescent conjugate of bovine serum albumin (BSA) labeled with the advanced Flamma® Fluor 488 dye. This versatile fluorescent protein conjugate combines the well-characterized properties of BSA with the superior fluorescence characteristics of Flamma® Fluor dyes, making it an excellent choice for a wide range of biological and biochemical applications.
Key Features:
A. Superior Fluorescence Properties
i. Strong absorption and high fluorescence quantum yield
ii. Excellent photostability for extended imaging and analysis
iii. Excitation/Emission maxima at 495/519 nm, ideal for green fluorescence detection
iiii. Maintains robust fluorescence activity and stability after conjugation
B. Versatile Protein Carrier
i. BSA provides a stable, inert protein scaffold
ii. Well-defined physical dimensions and properties
iii. Minimal interference with biological systems
BSA, Flamma® 488 can be applied in quantitative studies of electroporation, measurement of plasma volume, intracellular protein processing investigations, fluorescent tracer in various biological systems, cell permeability assays, protein uptake studies, fluorescence microscopy, and flow cytometry.
BSA, Flamma® 488 offers researchers a reliable and high-performance fluorescent tool for various applications in cell biology, biochemistry, and biophysics. Its combination of a well-characterized protein carrier with an advanced fluorescent dye provides excellent signal-to-noise ratios and consistent results in fluorescence-based experiments. This conjugate is particularly useful in studies requiring precise tracking of protein movement, quantification of cellular uptake, or visualization of fluid dynamics in biological systems.
What are the advantages?
1. Bright and photostable fluorescent tracer
2. Well-defined physical dimensions for quantitative studies
3. Compatible with standard green fluorescence detection systems
4. Minimal autofluorescence interference in biological samples
5. Suitable for multiplexing with other fluorophores
6. Long shelf life when stored properly
Key Features:
A. Superior Fluorescence Properties
i. Strong absorption and high fluorescence quantum yield
ii. Excellent photostability for extended imaging and analysis
iii. Excitation/Emission maxima at 495/519 nm, ideal for green fluorescence detection
iiii. Maintains robust fluorescence activity and stability after conjugation
B. Versatile Protein Carrier
i. BSA provides a stable, inert protein scaffold
ii. Well-defined physical dimensions and properties
iii. Minimal interference with biological systems
BSA, Flamma® 488 can be applied in quantitative studies of electroporation, measurement of plasma volume, intracellular protein processing investigations, fluorescent tracer in various biological systems, cell permeability assays, protein uptake studies, fluorescence microscopy, and flow cytometry.
BSA, Flamma® 488 offers researchers a reliable and high-performance fluorescent tool for various applications in cell biology, biochemistry, and biophysics. Its combination of a well-characterized protein carrier with an advanced fluorescent dye provides excellent signal-to-noise ratios and consistent results in fluorescence-based experiments. This conjugate is particularly useful in studies requiring precise tracking of protein movement, quantification of cellular uptake, or visualization of fluid dynamics in biological systems.
What are the advantages?
1. Bright and photostable fluorescent tracer
2. Well-defined physical dimensions for quantitative studies
3. Compatible with standard green fluorescence detection systems
4. Minimal autofluorescence interference in biological samples
5. Suitable for multiplexing with other fluorophores
6. Long shelf life when stored properly
Specifications
- Fluorophore: Flamma® 488
- Protein subtype: Albumin protein
- Excitation/Emission Max.(nm): 495/519
- Molecular weight: ~66.5 kDa
- Appearance: Yellow Solid
- Storage conditions: 4 ℃, protect from light
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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