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White PlainsNew York(NY) Sapir, Donald L. personal infomation and areas of practice

New York White Plains Sapir Schragin, LLP attorney Sapir, Donald L.
  • Lawyer name:Sapir, Donald L.
  • Address:399 Knollwood Road Suite 310White Plains,NY
  • Phone:914-328-0366
  • Fax:914-682-9128
  • PostalCode:10603 -1936
  • WebSite:http://www.sapirschragin.com/
  • Areas of Practice:Labor and Employment Law Employment Benefits Employment Litigation 60% of

New York White PlainsSapir Schragin, LLP attorney Sapir, Donald L. is a Very good lawyer practice area in Labor and Employment Law Employment Benefits Employment Litigation 60% of Practice Devoted to Litigation ,Employment, Employment Law -- Employer, Labor, Litigation & Appeals,Sapir Schragin, LLP

if you have any problem in Practice Devoted to Litigation ,Employment, Employment Law -- Employer, Labor, Litigation & Appeals,please email to Sapir Schragin, LLP or call 914-328-0366 or Go to our company directly(addr:399 Knollwood Road Suite 310White Plains,NY) ,we will provide free legal advice for you.

  • Donald L. Sapir has been a practitioner of labor and employment law for more than thirty-six years.? He has had experience representing employees from all walks of life, businesses both large and small, and labor organizations and their affiliated pension and welfare funds.

    Mr. Sapir has handled thousands of matters involving virtually every type of claim known to labor and employment lawyers, including: unlawful terminations; discrimination based on race, national origin, disability, age, gender, and sexual orientation; wage and hour/overtime; sexual harassment; retaliation due to complaints of discriminatory, unlawful, or unethical practices; whistleblower protection Dodd/Frank, False Claims Act, and other laws; pension claims; unfair labor practices; restrictive covenants; employment agreements; separation/severance agreements; Family Medical Leave Act leave, disability leave, and military leave (USERRA); reasonable accommodations to disabilities; individual and class actions; injunctions, damages, and other relief; claims before N.Y.S. Division of Human Rights; U.S. Equal Employment Opportunity Commission, N.Y.C. Human Rights Commission, all state courts; all federal courts.? Litigation activities have resulted in precedent-setting decisions and impressive verdicts.? While he is always willing to discuss a reasonable settlement that will satisfy the objectives of his client, he will litigate when necessary and prosecute a claim to the full extent permitted by the law.? Mediation is often used as a technique to accomplish goals of clients and to minimize a client's costs of achieving those goals.

    In recognition of his achievements as a labor and employment lawyer, Mr. Sapir was elected as President of the prestigious College of Labor & Employment Lawyers in 2012, has been a Fellow of the College since 2000 and a member of the College's Board of Governors since 2009.? He is a past Chair (2009-2010) of the 2,500 member Labor and Employment Law Section of the N.Y.S. Bar Association, a past Chair of the Labor and Employment Law Committee of the Westchester County Bar Association, a past Executive Board Member of the National Employment Lawyers Association/New York Chapter, a past Chair of the Alternate Dispute Resolution Committee of the American Bar Association's Labor and Employment Law Section, and a member of the National Employment Lawyers Association virtually since its inception.

    Mr. Sapir has been a contributing author or editor to various treatises on labor and employment law, including Discrimination in the Workplace, New York Employment Litigation Guide, and Employment Discrimination Law.? His articles have been published in the New York State Bar Association’s Labor and Employment Law Section Newsletter, the New York Law Journal, and other legal publications.? Mr. Sapir has appeared as a guest commentator on CourtTV on several occasions.

    Donald L. Sapir

  • New York, 1976 U.S. District Court Southern District of New York, 1976 U.S. District Court Eastern District of New York, 1976 U.S. District Court Western District of New York, 1984 U.S. Court of Appeals 2nd Circuit, 1982 U.S. Court of Appeals Federal Circuit, 1984 U.S. Supreme Court, 1984

  • The College of Labor and Employment Lawyers ((President 2012), Fellow since 2000) American Bar Association (Labor and Employment Law Section (Past Chair, Committee on Alternative Dispute Resolution)) New York State Bar Association (Labor and Employment Law Section (Past Chair, 2009-2010), Executive Committee Member since 1995) National Employment Lawyers Association National Employment Lawyers Association/New York Chapter, 2000 - Present ((Past Executive Committee Member)) Westchester County Bar Association (Labor and Employment Law Committee (Past Chair))

  • Hofstra University School of Law, Hempstead, New York, 1975J.D.Law Review: Hofstra Law Review, Research Editor State University of New York - Buffalo, Buffalo, New York, 1972B.A., HistoryHonors: cum laude

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how should i write my cover letter?

hello, i have a photoshop template of a newspaper, and i need to use it on sony vegas after i type everything i need on photoshop and export it as a jpg with high resolution, something like 3000 * 4800, but when i put it on vegas and zoom on the part of the newspaper i want it blurs the letters, even after i render it at 720p on mp4... it shouldnt do that since it has more that plenty resolution... any ideas? maybe its my sony vegas config?.

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1. Initiation: The gene will have a promoter site approximately 30 basepairs upstream from the start site. This promoter sequence will have the consensus sequence TATA A/T A A/T and is called the TATA box. Its function is to act as a recognition point for RNA Polymerase, the enzyme that will with other enzymes called Transcription Factors bind to the DNA.. . 2. Part of the Transcription Factor proteins is a helicase and this uses ATP to unwind the DNA double helix. It phosphorylates RNA Polymerase II causing it to dissociate from the rest of the transcription complex and start moving along the DNA template synthesising RNA - this is the elongation phase.. . 3. Elongation: RNA Polymerase II will copy the DNA template into a strand of RNA, adding ribonucleotides complementary to the DNA template with the exception of Uracil which it adds when it encounters Adenine on the DNA (instead of adding Thymine which is unique to DNA). Elongation o the RNA chain will continue until the RNA Pol II reaches the termination site downstream of the gene.. . 4. RNA Processing: Soon after synthesis, the 5' end of the Primary RNA Transcript is altered by the addition of GTP and methyl groups to give the RNA a 5'cap. This cap protects the primary transcript from attack by ribonucleases and helps initiate protein synthesis at the ribosome.. . 5. RNA Splicing: This removes the sequences of RNA in the primary transcript that are copies of the introns or non-coding sequences of DNA. The 5' boundary between the exon and intron starts with the sequence GU and at the 3' exon-intron boundary the intron ends with AG. . Splicing uses several small nuclear RNAs (snRNAs) rich in U residues. Four of them associate to form a splicesome at the intron to be removed by looping it out of the strand, then ligates the two adjacent exons.. . 6. 3' Processing: At the 3' end of the RNA, about 200 Adenine residues are added - this is called polyadenylation and forms the "polyA-tail" which acts as a signal sequence.. . 7. This is now mRNA and exits the nucleus and heads to the ribosome to begin protein synthesis.. . 8. The ribosome is RNA subunits which bind to the mRNA to make a ribosome. It reads the nucleotide sequence from the 5' to 3' direction and adds amino acids in the amino terminal to carboxyl terminal direction.. . Amino acids bind to tRNA to form aminoacyl-tRNAs, each bearing a triplet of bases called an anticodon. The ribosome reads each codon of mRNA in turn, and an aminoacyl-tRNA with an anticodon complementary to the mRNA codon will bind with hydrogen bonds. The incoming amino acids are then joined with a covalent peptide bond to the previous amino acid in the sequence. As this continues, a polypeptide chain is formed - this is the protein.

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