
Katalognummer: 209 - 102-P103G
Produktkategori: Företag och industri > Vetenskap och laboratorium
Storlek: 100 µg
102-P103G
Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The α-defensins are distinguished from the β-defensins by the pairing of their three disulfide bonds. To date, six human β-defensins have been identified; BD-1, BD-2, BD-3, BD-4, BD-5 and BD-6. β-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they can act as chemoattractants towards immature dendritic cells and memory T cells. The β-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and in some cases, a propeptide sequence. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds.
102-P219
Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The α-defensins are distinguished from the β-defensins by the pairing of their three disulfide bonds. To date, six human β-defensins have been identified; BD-1, BD-2, BD-3, BD-4, BD-5 and BD-6. β-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they can act as chemoattractants towards immature dendritic cells and memory T cells. The β-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and in some cases, a propeptide sequence. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds.
102-P220
Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The α-defensins are distinguished from the β-defensins by the pairing of their three disulfide bonds. To date, six human β-defensins have been identified; BD-1, BD-2, BD-3, BD-4, BD-5 and BD-6. β-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they can act as chemoattractants towards immature dendritic cells and memory T cells. The β-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and in some cases, a propeptide sequence. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds.
101-M327
Tripeptidyl-peptidase I (TPP1), also known as CLN2, is a lysosomal serine protease detected in all tissues examined, with highest levels shown in heart and placenta. It is an aminopeptidase that cleaves tripeptides from the free N-terminus of polypeptides and may also have endopeptidase activity. Defects in TPP1 are the cause of classical late-infantile neuronal ceroid lipofusionosis, also known as ceroid lipofusionosis neuronal 2 (CLN2), a fatal childhood neurodegenerative disease characterized by progressive visual and mental decline, motor disturbance, epilepsy, and behavioral changes.
101-M446
HGF Activator Inhibitor type II (HAI2), also known as placental bikunin, is a Kunitztype protease inhibitor. It is a type I membrane protein containing 2 Kunitz inhibitor domains in its extracellular region. In mouse, at least three isoforms of HAI2 exist as a result of alternative splicing. Isoforms 2 and 3, also known as HAI2B and HAI2C, respectively, are both missing the first aminoterminal Kunitz inhibitor domain.
101-M456
Insulin-like growth factor (IGF)-I (also known as somatomedin C and somatomedin A) and IGF-II (multiplication stimulating activity or MSA) belong to the family of insulin-like growth factors that are structurally homologous to proinsulin. Mature IGF-I and IGF-II share approximately 70% sequence identity. Both IGF-I and IGF-II are expressed in many tissues and cell types and may have autocrine, paracrine and endocrine functions. Mature IGF-I and IGF-II are highly conserved between the human, bovine and porcine proteins (100% identity), and exhibit cross-species activity.

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