Skip to content

Basket

You currently have no items in your basket.

Total (excl. vat) £0.00
View basket & checkout
Biomaterials

Bovine Serum Albumin - Fraction V

Product Sizes
10 g
BSA-10-10G
About this Product
SKU:
BSA-10
Additional Names:
Bovine serum albumin fraction V, Bovine Albumin, BSA, BSA Blocker, BSA Blocking
Application:
Cell-based/Functional Assay, ELISA, FLISA, Flow Cytometry, Immunofluorescence, Immunohistochemistry, Immunoprecipitation, Lateral Flow Assay, Western Blot
Buffer:
None
CE/IVD:
RUO
Extra Details:
Bovine Serum Albumin (BSA) is used for various biochemical applications including ELISA (Enzyme-Linked Immunosorbent Assay), high content screening assays, western blotting, FACS Buffer and immunohistochemistry. BSA as a blocking reagent is particularly useful with casein-sensitive antibodies, such as phospho-specific antibodies. Also used as a nutrient in cell and microbial culture. In restriction digests, BSA is used to stabilize some enzymes during digestion of DNA and to prevent adhesion of the enzyme to reaction tubes and other vessels. Bovine Serum Albumin can also be used to determine the quantity of other proteins, by comparing an unknown quantity of protein to known amounts of BSA. PLEASE READ: This product contains blood so may require extra documentation and/or clearances, please contact sales@2bscientific.com for further information and a more Accurate quote and lead time
Physical State:
Lyophilized
Shipping Conditions:
Ambient
Specificity:
Purity (%): 100% by Agarose Zone electrophoresis Moisture (%) 5% Loss on Drying pH: 7.0 Ash: <2.0% Protein (%): 98% by nitrogen analysis Protease: <0.005 Units/mg Heavy Metals: (Pb) < 10 ppm by ICP Endotoxin: < 3 EU/mg by LAL IgG: Not Detected NEFA: N/A
Storage Conditions:
2-8[o]C
Supplier:
Rockland Inc
Type:
Biomaterials: Blood Products
Bovine Serum Albumin - Fraction V
(I) Immunostaining for 8OhdG: (A) negative control, (B) muscle from subject 465 yr (positive control), (C) muscle from weight maintainer, and (D) muscle from weight gainer. For the 8OHdG assay, samples were treated with 10 mg/ml Proteinase K in phosphate-buffered saline (PBS) (0.05 M phosphate, 0.15 M NaCl, pH 7.4) with 1% bovine serum albumin (p/n BSA-50) for 40 min at 37 1C, and incubated in 5% skim milk in PBS for 2 h. Figure 1. PMID: 16687193.
IDO1 is selectively induced in cDC1 cells following LPS stimulation (A) IDO1 expression was analyzed by IS in BMDCs (n = 5). (B) Immunoblot analysis was carried out for IDO1, IDO2, TDO2, and B Beta-actin expression (n = 3). (C) Supernatants from cells prepared as in (B) were analyzed for l-kynurenine content by HLPC. (D and E) Flow plot (left) and quantification (right) of CD284 (D), and flow plot of CD40, CD80, and CD86 (E) on DC subsets (n = 3). (F) BM-derived cDC1 and cDC2 were treated as in (B) and IDO1 expression evaluated in CCR7- and CCR7+ populations treated as in (B), pre-gated on cDC1 and cDC2 (n = 3). (G) Immunofluorescence analysis of l-kynurenine expression in sorted CCR7+ cDC1 of different genotypes treated as in (B) (n = 3). (H) IDO1 expression (MFI) in thymic CCR7- and CCR7+ dendritic cell subsets, gated on CD11c+MHCII+XCRI+CD117- and CD11c+MCHII+CD172+CD117- (n = 3). Data are shown as mean +/- SD. ** p < 0.01, *** p < 0.001, **** p < 0.0001, one-way (D and H) or two-way (C) ANOVA followed by Bonferroni multiple comparison test. Isotype control as gray histogram. Figure 1. PMID: 35704993.
Strong responses to polyclonal anti-HA antiserum are readily observable on an AIR hemagglutinin microarray.(a) 1% BSA control (p/n BSA-10). (b) Anti-H7 polyclonal antiserum (A/Netherlands/219/2003, H7N7), 1:80 dilution (1.3%) in 1% BSA. Spots showing substantially increased brightness indicate binding to immobilized H7. In both cases, antigens were arrayed in square patterns as indicated by the yellow boxes in (a); a mouse IgG Fc domain (p/n 010-0103) was included as negative control (red boxes). Slight differences in spot intensity in the control (a) are due to differences in deposition efficiency for different antigens or controls. Specific antigens used in these experiments are indicated in Table 2. Goat anti-fluorescein, (p/n 600-101-096) used as an internal negative control. Fig 1. PMID: 26241048.
FGF21 activates ERK1/2 in cultured cardiac myocytes in the presence of high glucose and in heart tissue of mice. (a-c) Length, width and width to length ratio for ARVMs treated with BSA (control), FGF21 (25 ng/ml), increased glucose and/or the MEK inhibitor PD98059 (20 uM) for 48 h. Bars and colored symbols indicate average mean and means of independent experiments using different myocyte preparations, respectively. (d-f) Western blot analysis of ARVMs treated with BSA (control) or mouse recombinant FGF21 (25 ng/ml) with or without 10 mM glucose for 6 h. ERK1 is p44 and ERK2 is p42. (g) Analysis of cardiac tissue from FGF21 Tg mice and wild-type littermates at 8-12 weeks of age by Western blotting. (h, i) qRT-PCR for Egr-1 and c-Fos mRNA using total RNA from heart tissue of FGF21 Tg mice and wild-type littermates at 8-12 weeks of age. (j) Binding of 1 ug of soluble B Beta-klotho (B BetaKL) or PBS, 500 ng of Fc-tagged FGFR 1c, 2c, 3c, or 4 to 96-well plates coated with 200 ng of FGF21. (k) qRT-PCR for FGFR4 mRNA using total RNA isolated from ARVMs treated with BSA (control), FGF21 (25 ng/ml), and/or increased glucose (15.6 mM total). Comparison between groups was performed in form of a one-way (a-c, k) or two-way (e-f) ANOVA followed by post-hoc Tukey test or a two tailed t-test (h, i). All values are expressed as mean +/- SEM. (a-c) N = 3, ^p ≤ 0.05 vs. BSA CTR, *p ≤ 0.05 vs. Glucose + FGF21 CTR; (e, f) N = 5, ^p ≤ 0.05 vs. BSA CTR, #p ≤ 0.05 vs. FGF21 CTR; (h, i) N = 9-19, *p ≤ 0.05 vs. WT; (k) N = 4, *p ≤ 0.05 vs. CTR. All Western blots are cropped, and original blots are presented in Supplementary Fig. 3. Figure 3. PMID: 35513431.