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Bovine VEGF-A (Yeast-derived Recombinant Protein) - 25 micrograms

RP0072B-025
$300.00
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Vascular endothelial growth factor (VEGF) proteins stimulate vasculogenesis and angiogenesis. They are part of the system that restores the oxygen supply to tissues when blood circulation is inadequate. The normal function of VEGF proteins is to create new blood vessels during embryonic development, new blood vessels after injury, muscle following exercise, and new vessels (collateral circulation) to bypass blocked vessels. The VEGF family has six members, including VEGF-A, VEGF-B, VEGF-C, VEGF-D, VEGF-E, and Placental Growth Factor (PGF). Activity of VEGF-A, as its name implies, has been studied mostly on cells of the vascular endothelium, although it does have effects on a number of other cell types (e.g., stimulation monocyte/macrophage migration, neurons, cancer cells, kidney epithelial cells). In vitro, VEGF-A has been shown to stimulate endothelial cell mitogenesis and cell migration. VEGF-A is also a vasodilator and increases microvascular permeability and was originally referred to as vascular permeability factor (VPF).

VEGF-A Homology Across Species
Bos taurus (cattle) VEGF-A – 100%
Bison bison (bison) VEGF-A – 100%
Bos mutus (wild yak) VEGF-A – 100%
Bubalus bubalis (water buffalo) VEGF-A – 100%
Ovis aries (sheep)VEGF-A – 99%
Capra hircus (goat) VEGF-A – 99%
Orcinus orca (killer whale) VEGF-A – 96%
Physeter catodon (sperm whale) VEGF-A – 96%
Lipotes vexillifer (Yangtze River dolphin) VEGF-A – 96%
Orcinus orca (killer whale) VEGF-A – 96%
Ictidomys tridecemlineatus (thirteen-lined ground squirrel) VEGF-A – 96%
Chrysochloris asiatica (Cape golden mole) VEGF-A – 96%
Condylura cristata (star-nosed mole) VEGF-A – 95%
Camelus ferus (Wild Bactrian camel) VEGF-A – 95%
Neovison vison (American mink) VEGF-A – 95%
Ochotona curzoniae (black-lipped pika) VEGF-A – 95%
Callithrix jacchus (white-tufted-ear marmoset) VEGF-A – 95%
Cebus capucinus imitator(white-faced capuchin) VEGF-A – 95%
​Ursus maritimus (polar bear) VEGF-A – 95%

Bovine VEGF-A (Yeast-derived Recombinant Protein) - 25 micrograms
Catalog No.:
RP0072B-025
Quantity:
25 ug
Source:
The Bovine VEGF-A recombinant protein was produced in yeast and therefore does not have endotoxin, is naturally folded, and post-translationally modified.
MW:
The Bovine VEGF-A recombinant protein has a predicted molecular weight of 19.2 kDa.
Protein Sequence:
APMAEGGQKP HEVVKFMDVY QRSFCRPIET LVDIFQEYPD EIEFIFKPSC VPLMRCGGCC NDESLECVPT EEFNITMQIM RIKPHQSQHI GEMSFLQHNK CECRPKKDKA RQENPCGPCS ERRKHLFVQD PQTCKCSCKN TDSRCKARQL ELNERTCRCD KPRR (164)
Country of Origin:
USA
Applications:
The bovine VEGF-A endotoxin-free recombinant protein can be used in cell culture, as an VEGF-A ELISA Standard, and as a Western Blot Control.

31888628

Effect of ovarian steroids on vascular endothelial growth factor a expression in bovine uterine endothelial cells during adenomyosis.

Lupicka M, Zadroga A, Szczepańska A, Korzekwa AJ.

BMC Vet Res. 2019 Dec 30;15(1):473. doi: 10.1186/s12917-019-2222-0.

Applications: Measurement of bovine VEGF-A in culture media by ELISA

Abstract

BACKGROUND:

Adenomyosis is a uterine dysfunction defined as the presence of endometrial glands within the myometrium. There is evidence that proangiogenic factors may play a role during the development of adenomyosis; however, exact mechanism remains unknown. The aim of the study was to determine the action of vascular endothelial growth factor A (VEGFA) in uterine tissue and uterine vascular endothelial cells during adenomyosis.

RESULTS:

Uterine tissues were collected and examined for the presence and extent of adenomyosis. Gene and protein expression of VEGFA and its two receptors (VEGFR1 and VEGFR2) was evaluated with quantitative polymerase chain reaction and Western blotting, respectively, in endometrium and myometrium during adenomyosis. Immunolocalization of VEGFA and its receptors within uterine tissues during adenomyosis was also determined. In an in vitro experiment, endothelial cells from non-adenomyotic bovine uteri were treated with media conditioned by non-adenomyotic or adenomyotic uterine slices treated with 17-beta-oestradiol (E2) or progesterone (P4). Both gene and protein expression of VEGFR2 were elevated in endometrium in stages 3-4 of adenomyosis. Protein expression of VEGFA and VEGFR2 as well as VEGFA secretion were increased in endothelial cells treated with media conditioned by adenomyotic uterine slices after E2 treatment.

CONCLUSIONS:

Results suggest that VEGFA signalling is an important component, next to E2, that enhances VEGFA action and participates in adenomyosis development in cows.


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