Oilfield Money Explained Pt 1

Working in the oilfield isn't all its cracked up to be. Trust me, I've been doing it my whole life. Most people that have never experienced it only see the dollar signs. Sure, we can pull $100,000 a year with a highschool education or a few years of college experience. But what people don't realize is how much work it takes to make that kind of money.

If you ever meet someone that says they are making six figures in the oil and gas industry; the first thing you should do is ask them how many hours a week they work, the second thing you should ask is when their last day off was.

Currently the industry standard for inspections (the field I am in) is six days a week, ten hours a day. This is at a minimum. When the "big" projects hit, we transition to seven days a week, twelve or fourteen hours a day. This is where the money is made, everything over fourty hours a week is time and a half. When you start talking the base wage of $20/hr for 40 hours ($800 for the slow ones in the crowd) then $30/hr for the next 44 hours ($1320), you are going to get $2120 a week before taxes. A week. That works out to right around $100,000 a year (pre taxes) when you account for the couple days off a year that the average oilfield worker gets.

A basic laborer is starting out at $24/hr around these parts, but they are also working every day of the week for a minimum of ten hours a day.

So think about it before you just start seeing the dollar signs.

Then there comes the bullshit that we, the oilfield workers, deal with on a daily basis. Things such as $1700+ a month for a single bedroom apartment in the middle of fucking nowhere Wyoming where three years ago the same apartment was maybe $300/month. The constant attitude we get from all the "locals" that don't like all the "oilfield trash" that is moving in. But then they smile as they fuck you with the prices. They don't like us here, but they sure do love our money.

Or how about $80/night to live in a shithole motel? Yeah, thats just awesome.


Then there is dealing with all the fucking idiots that come from all over the nation because they heard about how good the money is. They last a few weeks at the most. Most of them go crawling back home with their tails tucked between there legs. But that will be another rant.