Albumin, Nuclease-Free

Albumin, Nuclease-Free

Albumin, Nuclease-Free

C.A.S.: 9048-46-8

According to SDS PAGE, 90% of the material is intact BSA.
Exonuclease, endonuclease, ribonuclease, and protease were all tested.
A 50 mg/ml aqueous solution with a neutral pH and 50 percent glycerol.

Store between 2 and 8 degrees Celsius.

Call 440-463-4480 For Availability

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CAS Number: C.A.S.: 9048-46-8
Albumin, Nuclease-Free

According to SDS PAGE, 90% of the material is intact BSA.
Exonuclease, endonuclease, ribonuclease, and protease were all tested.
A 50 mg/ml aqueous solution with a neutral pH and 50 percent glycerol.

Store between 2 and 8 degrees Celsius.

Call 440-463-4480 For Availability
SIZE

100 mg, 5×100 mg, Bulk

History

The name albumin comes from the Latin word albus, which meaning white, and refers to the fact that it is found in egg white.

Howe demonstrated variations in albumin/globulin ratios in neonatal and older animals’ albumin serum in 1921. (Howe 1921).
Pederson discovered that this difference in calves was attributable to the existence of a fetal-specific alpha-globulin in 1947. (Pederson 1947).
Further variations in numerous plasma proteins of fetal and adult animals were shown in a variety of species in the 1950s and 1960s (Andreoli and Robbins 1962, Pantelouris and Hale 1962, and Wise et al. 1963).

The effects of low pH on albumin were examined in the 1960s (Bloomfield 1966, and Slayter 1965), and albumin production was investigated in the 1970s, leading to the discovery of the N-terminal amino acid sequences (Peters 1977, and McGillivray et al. 1979).

The conformational changes that occur during thermal denaturation were studied in the 1980s and 1990s (Takeda et al. 1989)
In 1990, the main structure of bovine serum albumin was discovered (Hirayama et al. 1990).

Albumin is now predominantly used in molecular studies in the academic and medical communities (Kreader 1996).
Albumin polymorphisms are also being investigated, leading to the finding of new albumin variations in cattle (Ibeagha-Awemu et al. 2004).

Molecular Characteristics:

Preproalbumin is the precursor protein that is used to make the protein.
The proregion is made up of residues 19-24.
The signal sequence of bovine preproalbumin shares a lot of similarities with that of rat preproalbumin, but it doesn’t have any similarities with other bovine proteins (MacGillivray et al. 1979, and Fujiwara and Amisaki 2006).

Composition:

Bovine serum albumin is made up of nine loops joined by 17 disulfide bridges in the protein’s core, which are protected (Restani et al. 2004).
Although bovine serum albumin is highly soluble in water, it is not easily digested.

Protein Accession Number: P02769

CATH Classification (v. 3.2.0):

  • Class: Mainly Alpha
  • Architecture: Orthogonal Bundle
  • Topology: Serum Albumin; Chain A, Domain 1

(Based on human serum albumin, which is 76% identical to bovine)

Molecular weight:

  • 66.4 kDa (Theoretical)

Optimal pH Range: 5.0-7.0 (El Kadi et al. 2006)

Isoelectric Point:

  • 5.60 (Theoretical)

Extinction Coefficient:

  • 41,180 cm-1 M-1 (Theoretical)
  • E1%,280 = 6.20 (Theoretical)

Application

Albumin is used in techniques that require the inhibition or reduction of non-specific protein-protein interactions as well as interactions between proteins and biological macromolecules, such as:

  • Enzymatic reactions (Gianfreda and Scarfi 1991, and Chang 1994 and 1995)
  • Nucleic acid hybridizations (Sambrook 2001)
  • Western, Northern, Southern, and dot blots (Sambrook 2001)
  • PCR and RT-PCR reactions (Kreader 1996, and Pandya et al. 1994)

SDS

COA

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