SRP3011
Beta D-1 (36 aa) human
recombinant, expressed in E. coli, ≥98% (SDS-PAGE), ≥98% (HPLC), suitable for cell culture
Synonyme(s) :
DEFB1, beta-Defensin-1
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About This Item
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.32
Produits recommandés
Source biologique
human
Produit recombinant
expressed in E. coli
Pureté
≥98% (HPLC)
≥98% (SDS-PAGE)
Forme
lyophilized
Poids mol.
7.8 kDa
Conditionnement
pkg of 20 μg
Technique(s)
cell culture | mammalian: suitable
Impuretés
<0.1 EU/μg endotoxin, tested
Couleur
white to off-white
Numéro d'accès UniProt
Spectre d'activité de l'antibiotique
fungi
mycobacteria
viruses
Mode d’action
cell membrane | interferes
Conditions d'expédition
wet ice
Température de stockage
−20°C
Informations sur le gène
human ... DEFB1(1672)
Description générale
Chemical structure: peptide
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, four human β-defensins have been identified; BD-1, BD-2, BD-3 and BD-4. β-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they are chemoattractant towards immature dendritic cells and memory T cells. The b-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and, in the case of BD-1 (36a.a.), a propeptide region. β-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. b-defensins are 3-5 kDa peptides ranging in size from 33-47 amino acid residues. Recombinant human BD-1 is a 3.9 kDa protein containing 36 amino acid residues.
Actions biochimiques/physiologiques
Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. Recombinant human BD-1 is a 3.9 kDa protein containing 36 amino acid residues.
Séquence
DHYNCVSSGG QCLYSACPIF TKIQGTCYRG KAKCCK
Forme physique
Lyophilized from 10 mM Acetic Acid.
Reconstitution
Centrifuge the vial prior to opening. Reconstitute in 10 mM Acetic Acid to a concentration of 0.1-1.0 mg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 week. For extended storage, it is recommended to further dilute in a buffer containing a carrier protein (example 0.1% BSA) and store in working aliquots at -20°C to -80°C.
Mention d'avertissement
Warning
Mentions de danger
Conseils de prudence
Classification des risques
Eye Irrit. 2 - Skin Irrit. 2
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".
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Ainhoa Revilla-Guarinos et al.
Applied and environmental microbiology, 86(14) (2020-05-18)
Bce-like systems mediate resistance against antimicrobial peptides in Firmicutes bacteria. Lactobacillus casei BL23 encodes an "orphan" ABC transporter that, based on homology to BceAB-like systems, was proposed to contribute to antimicrobial peptide resistance. A mutant lacking the permease subunit was
Y Q Tang et al.
Science (New York, N.Y.), 286(5439), 498-502 (1999-10-16)
Analysis of rhesus macaque leukocytes disclosed the presence of an 18-residue macrocyclic, tridisulfide antibiotic peptide in granules of neutrophils and monocytes. The peptide, termed rhesus theta defensin-1 (RTD-1), is microbicidal for bacteria and fungi at low micromolar concentrations. Antibacterial activity
Robert I Lehrer et al.
Current opinion in immunology, 14(1), 96-102 (2002-01-16)
During the past year, novel beta-defensins of mice and men have been identified, together with a novel defensin subfamily (the circular or 'theta' minidefensins) in primates. Insight into the evolution of defensins has been obtained from structural studies, and several
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