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Possible Answers: CAMP.

Last seen on: LA Times Crossword 3 Feb 19, Sunday

Random information on the term “—”:

E (named e /iː/, plural ees)[1] is the fifth letter and the second vowel in the modern English alphabet and the ISO basic Latin alphabet. It is the most commonly used letter in many languages, including Czech, Danish, Dutch, English, French, German, Hungarian, Latin, Latvian, Norwegian, Spanish, and Swedish.[2][3][4][5][6]

The Latin letter ‘E’ differs little from its source, the Greek letter epsilon, ‘Ε’. This in turn comes from the Semitic letter hê, which has been suggested to have started as a praying or calling human figure (hillul ‘jubilation’), and was probably based on a similar Egyptian hieroglyph that indicated a different pronunciation. In Semitic, the letter represented /h/ (and /e/ in foreign words); in Greek, hê became the letter epsilon, used to represent /e/. The various forms of the Old Italic script and the Latin alphabet followed this usage.

Although Middle English spelling used ⟨e⟩ to represent long and short /e/, the Great Vowel Shift changed long /eː/ (as in ‘me’ or ‘bee’) to /iː/ while short /ɛ/ (as in ‘met’ or ‘bed’) remained a mid vowel. In other cases, the letter is silent, generally at the end of words.

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— on Wikipedia

Random information on the term “CAMP”:

4EYC, 2FBS, 2FBU, 2FCG, 2K6O, 2LMF











Cathelicidin-related antimicrobial peptides are a family of polypeptides primarily stored in the lysosomes of macrophages and polymorphonuclear leukocytes (PMNs).[5] Cathelicidins serve a critical role in mammalian innate immune defense against invasive bacterial infection.[6] The cathelicidin family of peptides are classified as antimicrobial peptides (AMPs). The AMP family also includes the defensins. Whilst the defensins share common structural features, cathelicidin-related peptides are highly heterogeneous.[6]

Members of the cathelicidin family of antimicrobial polypeptides are characterized by a highly conserved region (cathelin domain) and a highly variable cathelicidin peptide domain.[6]

Cathelicidin peptides have been isolated from many different species of mammals. Cathelicidins were originally found in neutrophils, but have since been found in many other cells including epithelial cells and macrophages after activation by bacteria, viruses, fungi, or the hormone 1,25-D, which is the hormonally active form of vitamin D.[7] The protein encoded by the human cathelicidin gene, CAMP, is cleaved into the LL-37 peptide, which has several immunological functions.

CAMP on Wikipedia